SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

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Fitness BLAST: loading...

Comparing 62 a.a. (SDEYKIRRER...) to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree

Found 11 hits to proteins with known functional sites (download)

P17676 CCAAT/enhancer-binding protein beta; C/EBP beta; Liver activator protein; LAP; Liver-enriched inhibitory protein; LIP; Nuclear factor NF-IL6; Transcription factor 5; TCF-5 from Homo sapiens (Human) (see 5 papers)
100% identity, 100% coverage: 1:62/62 of query aligns to 271:332/345 of P17676

query
sites
P17676

S

S

D

D

E

E

Y

Y

K

K

I

I

R

R

E

E

R

R

N

N

I

I

A

A

V

V

R

R

K

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S
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S

R

R

D

D

K

K

A

A

K

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M

M

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R

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N

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E

T

T

Q

Q

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H

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V

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A

A

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N

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Q

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K

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E

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Q

L

L

S

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E

E

L

L

S

S

T

T

L

L

R

R

N

N

L

L

F

F

K

K

S288 (= S18) mutation to A: Loss of nuclear translocation.

Sites not aligning to the query:

174 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
195 G → S: in dbSNP:rs4253440
235 modified: Phosphothreonine; by RPS6KA1, CDK2 and MAPK; T→S: Loss of transactivation activity in response to IFNG.

Q05826 CCAAT/enhancer-binding protein beta; C/EBP beta; Transcription factor NF-M; CCR protein from Gallus gallus (Chicken) (see 2 papers)
98% identity, 100% coverage: 1:62/62 of query aligns to 254:315/328 of Q05826

query
sites
Q05826

S

S

D

D

E

E

Y

Y

K

K

I

L

R

R

E

E

R

R

N

N

I

I

A

A

V

V

R

R

K

K

S

S

R

R

D

D

K

K

A

A

K

K

M

M

R

R

N

N

L

L

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E

T

T

Q

Q

H

H

K

K

V

V

L

L

E

E

L

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T

T

A

A

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E

N

N

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E

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L

Q

Q

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K

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V

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E

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Q

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S

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E

L

L

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S

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T

L

L

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N

N

L

L

F

F

K

K

Sites not aligning to the query:

3 modified: Asymmetric dimethylarginine; by CARM1; R→A: Not methylated. Increases interaction with SMARCA2 and MED23.; R→L: Decreases interaction with SMARCA2 and MED23.
39 K→A: Decreases methylation. Increases transactivation activity inhibition.
220 T→D: Decreases methylation by CARM1 and increases transactivation activity.

P21272 CCAAT/enhancer-binding protein beta; C/EBP beta; C/EBP-related protein 2; Interleukin-6-dependent-binding protein; IL-6DBP; Liver-enriched inhibitory protein; LIP; Liver-enriched transcriptional activator; LAP; Silencer factor B; SF-B from Rattus norvegicus (Rat) (see 2 papers)
98% identity, 100% coverage: 1:62/62 of query aligns to 223:284/297 of P21272

query
sites
P21272

S

S

D

D

E

E

Y

Y

K

K

I

M

R

R

E

E

R

R

N

N

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I

A

A

V

V

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S

S

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D

K

K

A

A

K

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M

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N

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T

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Q

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H

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T

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A

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N

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K

Sites not aligning to the query:

105 modified: Phosphoserine; by RPS6KA1 and PKC/PRKCA; S→A: No effect on DNA-binding. Loss of transactivation activity. Loss of hepatocyte proliferation induction by TGFA.; S→D: No effect on DNA-binding. Increases transactivation activity.

P28033 CCAAT/enhancer-binding protein beta; C/EBP beta; AGP/EBP; Interleukin-6-dependent-binding protein; IL-6DBP; Liver-enriched transcriptional activator; LAP from Mus musculus (Mouse) (see 12 papers)
98% identity, 100% coverage: 1:62/62 of query aligns to 222:283/296 of P28033

query
sites
P28033

S

S

D

D

E

E

Y

Y

K

K

I

M

R

R

E

E

R

R

N

N

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A

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S

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D

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K

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A

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M

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N

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Q

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H

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V

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T

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A

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N

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S

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L

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N

N

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F

K

K

S276 (= S55) mutation to A: Reduces phosphorylation in response to calcium.

Sites not aligning to the query:

3 modified: Asymmetric dimethylarginine; by CARM1
22:104 Required for MYC transcriptional repression
39 modified: N6-acetyllysine; alternate; mutation K->A,Q: No effect on interaction with EP300.; K→R: Dominant negative. Loss of transactivation activity. No effect on interaction with EP300.
98 K→R: No effect on transactivation activity. Not acetylated after glucocorticoid-stimulation and no increase of transactivation activity; when associated with R-101 and R-102.
101 K→R: Not acetylated after glucocorticoid-stimulation and no increase of transactivation activity; when associated with R-98 and R-102.
102 K→R: Not acetylated and no increase of transactivation activity after glucocorticoid-stimulation; when associated with R-98 and R-101.
133 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate; K→R: Not sumoylated. Decreases ubiquitination and increases stability. Loss of proliferation inhibition in T cells. No effect on transactivation activity.
135 E→A: Not sumoylated and not ubiquitinated.
179 modified: Phosphothreonine; by GSK3-beta; T→A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-184 and A-188.
180 modified: carbohydrate, O-linked (GlcNAc) serine; S→A: Highly increases transactivation activity; when associated with A-181.
181 modified: carbohydrate, O-linked (GlcNAc) serine; S→A: Highly increases transactivation activity; when associated with A-180.
184 modified: Phosphoserine; by GSK3-beta; S→A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-179 and A-188.
188 modified: Phosphothreonine; by RPS6KA1, CDK2 and MAPK; T→A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-179 and A-184.
215 K→R: No effect on transactivation activity.
217 modified: Phosphothreonine; by RPS6KA1 and PKC/PRKCA; T→A: Loss of hepatocyte proliferation induction by TGFA.; T→E: Induces hepatocyte proliferation.

1h88B Crystal structure of ternary protein-DNA complex1 (see paper)
100% identity, 100% coverage: 1:62/62 of query aligns to 6:67/71 of 1h88B

query
sites
1h88B

S

S

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D

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Y

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N

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A

A

V
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V

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R

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K

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S

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R

D

D

K

K

A

A

K

K

M

M

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R

N

N

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L

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E

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T

Q

Q

H

H

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T

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N

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E

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Q

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L

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E

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S

S

T

T

L

L

R

R

N

N

L

L

F

F

K

K

binding : Y9 (= Y4), R13 (= R8), N16 (= N11), N17 (= N12), V20 (= V15), S23 (= S18), R24 (= R19), R24 (= R19)

P05554 CCAAT/enhancer-binding protein alpha; C/EBP alpha from Rattus norvegicus (Rat) (see 6 papers)
76% identity, 100% coverage: 1:62/62 of query aligns to 282:343/358 of P05554

query
sites
P05554

S

S

D

N

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Y
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Y

K
x
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N

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N

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R

Y285 (= Y4) mutation to A: Decreased transcription factor activity. Strongly decreased transcription factor activity; when associated with R-293.; mutation to A: Increases interaction with TFDP1 and TFDP2, reduces DNA-binding, transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction.
285:300 (vs. 4:19, 88% identical) binding
V287 (≠ I6) mutation to A: No effect on repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-290.
R289 (= R8) mutation to A: Loss of DNA-binding and transcription factor activity.
E290 (= E9) mutation to A: No effect on repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-287.
N293 (= N12) mutation to R: Decreased transcription factor activity. Strongly decreased transcription factor activity; when associated with A-285.
I294 (= I13) mutation to A: Increases interaction with TFDP1 and TFDP2, reduces transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction, no effect on DNA-binding; when associated with A-297.
V296 (= V15) mutation to A: No effect on DNA-binding and transcription factor activity, but modified sequence specificity.
R297 (= R16) mutation to A: Increases interaction with TFDP1 and TFDP2, reduces transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction, no effect on DNA-binding; when associated with A-294.
S299 (= S18) mutation to D: Isoform 4: Stimulates nucleolar retention of isoform 4. No effect on interaction with NPM1, TAF1A and UBTF.
D301 (= D20) mutation to A: No effect neither on interaction with TFDP1 or TFDP2 nor on transactivation activity or repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-304.
K304 (= K23) mutation to A: No effect neither on interaction with TFDP1 or TFDP2 nor on transactivation activity or repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-301.

Sites not aligning to the query:

1:14 modified: Variant sequence, Missing (in isoform 2)
1:70 Required to repress E2F1:TFDP1-mediated transcription, to inhibit cell cycle and to induce adipocyte differentiation
1:117 modified: Variant sequence, Missing (in isoform 3)
126:200 Required to induce adipocyte differentiation
159 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate; mutation K->A,R: Not sumoylated. No effect of sumoylation on cell cycle inhibition.

P49715 CCAAT/enhancer-binding protein alpha; C/EBP alpha from Homo sapiens (Human) (see 3 papers)
76% identity, 100% coverage: 1:62/62 of query aligns to 282:343/358 of P49715

query
sites
P49715

S

S

D

N

E

E

Y

Y

K

R

I

V

R

R

E

E

R

R

N

N

I

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A

A

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S

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D

K

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A

A

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Q

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x
Q

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N

N

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K

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V

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E

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Q

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T

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N

G

L

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F

K

R

Q312 (≠ H31) natural variant: Q -> QK (in AML; nuclear; no effect on expression; loss of DNA-binding and transactivation activity)

Sites not aligning to the query:

54:72 Required for interaction with TRIB1
55 I→A: Decreased interaction with TRIB1.
57 E→T: No effect on interaction with TRIB1.
58 H→D: No effect on interaction with TRIB1.
59 E→A: Decreased interaction with TRIB1.
61 S→A: Decreased interaction with TRIB1.
62 I→A: Decreased interaction with TRIB1.
63 D→A: No effect on interaction with TRIB1.
64 I→A: Decreased interaction with TRIB1.
65 S→A: No effect on interaction with TRIB1.
67 Y→A: Decreased interaction with TRIB1.; Y→F: No effect on interaction with TRIB1.
68 I→A: Decreased interaction with TRIB1.
69 D→A: No effect on interaction with TRIB1.
84 H → L: in AML; no effect on expression; no effect on DNA-binding or transactivation activity; dbSNP:rs28931590
190 modified: Phosphoserine

P53566 CCAAT/enhancer-binding protein alpha; C/EBP alpha from Mus musculus (Mouse) (see 5 papers)
76% identity, 100% coverage: 1:62/62 of query aligns to 283:344/359 of P53566

query
sites
P53566

S
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S

D
x
N

E
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E

Y
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Y

K
x
R

I
x
V

R
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R

E
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E

R
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R

N
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N

I
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I

A
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A

V
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V

R
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R

K
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K

S
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S

R
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R

D
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D

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K

A
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A

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K

M
x
Q

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R

N
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N

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x
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E

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T

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Q

H
x
Q

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K

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V

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L

E
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E

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T

A
x
S

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D

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D

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R

Y286 (= Y4) mutation to A: No effect on DNA-binding, represses E2F1:TFDP1-mediated transcription and causes adipose hypoplasia and myeloid dysplasia.
V288 (≠ I6) mutation to A: No effect on DNA-binding, no effect on repression of E2F1:TFDP1-mediated transcription and no effect on adipogenesis and granulopoiesis; when associated with A-291.
E291 (= E9) mutation to A: No effect on DNA-binding, no effect on repression of E2F1:TFDP1-mediated transcription and no effect on adipogenesis and granulopoiesis; when associated with A-288.
I295 (= I13) mutation to A: No effect on DNA-binding, represses E2F1:TFDP1-mediated transcription and causes adipose hypoplasia and myeloid dysplasia; when associated with A-298.
R298 (= R16) mutation to A: No effect on DNA-binding, represses E2F1:TFDP1-mediated transcription and causes adipose hypoplasia and myeloid dysplasia; when associated with A-295.

Sites not aligning to the query:

1:14 modified: Variant sequence, Missing (in isoform 2)
1:117 modified: Variant sequence, Missing (in isoform 3)
180:194 Required to functionally cooperate with SREBF1 in promoter activation
182:188 PPPPPPP→APPPAPA: No effect on DNA-binding or interaction with CDK2 and CDK4. No effect on cell cycle inhibition.
184:186 PPP→AAA: No effect on DNA-binding or interaction with CDK2 and CDK4. No effect on cell cycle inhibition.
193 modified: Phosphoserine; S→A: No effect on DNA-binding. Loss of interaction with CDK2 and CDK4 as well as cell cycle inhibition.
222 modified: Phosphothreonine; by GSK3
222:230 TPPPTPVPS→APPPAPVPA: Decreases phosphorylated form. Deregulation of hepatic glucose metabolism.
226 modified: Phosphothreonine; by GSK3
240:359 Interaction with FOXO1

8k8cA Crystal structure of c/ebpalpha bzip domain bound to a high affinity DNA (see paper)
79% identity, 94% coverage: 1:58/62 of query aligns to 2:59/60 of 8k8cA

query
sites
8k8cA

S

S

D

N

E

E

Y
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Y

K
x
R

I

V

R

R

R
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R

E

E

R

R

N

N

N
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N

I

I

A
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A

V
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V

R
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R

K
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K

S
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S

R
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R

D

D

K

K

A

A

K

K

M

Q

R

R

N

N

L

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E

E

T

T

Q

Q

H

Q

K

K

V

V

L

L

E

E

L

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T

A

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N

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D

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K

K

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V

E

E

Q

Q

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L

S

S

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R

E

E

L

L

S

D

T

T

L

L

R

R

binding : Y5 (= Y4), R6 (≠ K5), R9 (= R8), N13 (= N12), A15 (= A14), V16 (= V15), R17 (= R16), K18 (= K17), S19 (= S18), R20 (= R19)

P49716 CCAAT/enhancer-binding protein delta; C/EBP delta; Nuclear factor NF-IL6-beta; NF-IL6-beta from Homo sapiens (Human) (see paper)
68% identity, 100% coverage: 1:62/62 of query aligns to 191:252/269 of P49716

query
sites
P49716

S

S

D

P

E

E

Y

Y

K

R

I

Q

R

R

E

E

R

R

N

N

I

I

A

A

V

V

R

R

K

K

S

S

R

R

D

D

K

K

A

A

K

K

M

R

R

R

N

N

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Q

E

E

T

M

Q

Q

H

Q

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K

V

L

L

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E

E

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T

S

A

A

E

E

N

N

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V

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E

D

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T

G

L

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N

Q

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F

F

F

K

K

Sites not aligning to the query:

120 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); K→A: Loss of sumoylation.

Q8IG69 CCAAT/enhancer-binding protein homolog 2 from Caenorhabditis elegans (see paper)
48% identity, 97% coverage: 2:61/62 of query aligns to 18:77/100 of Q8IG69

query
sites
Q8IG69

D

D

E

D

Y

Y

K

S

I

T

R

K

R

R

E

K

R

R

N

N

I

E

A

A

V

V

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R

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D

Q

K

K

A

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K
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R

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E

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E

L

N

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T

T

Q

A

H

E

K

K

V

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E

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L

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T

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A

K

E

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N

N

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F

F

R39 (≠ K23) mutation to C: In gk509377; low-fat phenotype. Increases expression of ech-1.1 mRNA and decreases fat-5 mRNA.

Sites not aligning to the query:

78 M→I: In gk112657; low-fat phenotype.
79 A→T: In gk112658; low-fat phenotype.
85 G→E: In gk112659; low-fat phenotype.

Query Sequence

>62 a.a. (SDEYKIRRER...)
SDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNL
FK

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory