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Protein

Serum response factor-binding protein 1

Gene

SRFBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells (By similarity).By similarity

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Serum response factor-binding protein 1
Alternative name(s):
SRF-dependent transcription regulation-associated protein
p49/STRAP
Gene namesi
Name:SRFBP1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:26333. SRFBP1.

Subcellular locationi

  • Cytoplasmperinuclear region By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670870.

Polymorphism and mutation databases

BioMutaiSRFBP1.
DMDMi74751249.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 429428Serum response factor-binding protein 1PRO_0000320006Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei203 – 2031PhosphoserineCombined sources
Modified residuei205 – 2051PhosphoserineCombined sources
Modified residuei264 – 2641PhosphoserineCombined sources
Modified residuei279 – 2791PhosphoserineCombined sources
Modified residuei281 – 2811PhosphoserineCombined sources
Modified residuei349 – 3491PhosphoserineCombined sources
Modified residuei351 – 3511PhosphoserineCombined sources
Modified residuei367 – 3671PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8NEF9.
MaxQBiQ8NEF9.
PaxDbiQ8NEF9.
PeptideAtlasiQ8NEF9.
PRIDEiQ8NEF9.
TopDownProteomicsiQ8NEF9.

PTM databases

iPTMnetiQ8NEF9.
PhosphoSiteiQ8NEF9.

Expressioni

Tissue specificityi

Abundantly expressed in heart and skeletal muscle, and at much lower levels in brain and lung.1 Publication

Developmental stagei

Up-regulated in adult heart (at protein level).1 Publication

Gene expression databases

BgeeiQ8NEF9.
CleanExiHS_SRFBP1.
GenevisibleiQ8NEF9. HS.

Organism-specific databases

HPAiHPA042737.
HPA058150.

Interactioni

Subunit structurei

Interacts with SRF. Forms complexes with SRF and SRF cofactors ARID2, MYOCD and NKX2-5. Interacts with the N-terminus of SLC2A4 (By similarity).By similarity

Protein-protein interaction databases

BioGridi127495. 6 interactions.
IntActiQ8NEF9. 6 interactions.
MINTiMINT-4932778.
STRINGi9606.ENSP00000341324.

Structurei

3D structure databases

ProteinModelPortaliQ8NEF9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili42 – 6726Sequence analysisAdd
BLAST
Coiled coili108 – 14639Sequence analysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IEZ8. Eukaryota.
ENOG4111UG3. LUCA.
GeneTreeiENSGT00390000006478.
HOGENOMiHOG000154413.
HOVERGENiHBG056694.
InParanoidiQ8NEF9.
OMAiFKEARQN.
OrthoDBiEOG79KPG5.
PhylomeDBiQ8NEF9.
TreeFamiTF328596.

Family and domain databases

InterProiIPR015158. Bud22/SRFB1.
[Graphical view]
PfamiPF09073. BUD22. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8NEF9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQPGTLNLN NEVVKMRKEV KRIRVLVIRK LVRSVGRLKS KKGTEDALLK
60 70 80 90 100
NQRRAQRLLE EIHAMKELKP DIVTKSALGD DINFEKIFKK PDSTATERAI
110 120 130 140 150
ARLAVHPLLK KKIDVLKAAV QAFKEARQNV AEVESSKNAS EDNHSENTLY
160 170 180 190 200
SNDNGSNLQR EATVISEQKV KETKILAKKP IHNSKEKIAK MEHGPKAVTI
210 220 230 240 250
ANSPSKPSEK DSVVSLESQK TPADPKLKTL SQTKKNKGSD SSLSGNSDGG
260 270 280 290 300
EEFCEEEKEY FDDSTEERFY KQSSMSEDSD SGDDFFIGKV RRTRKKESSC
310 320 330 340 350
HSSVKEQKPL EKVFLKEDTG ETHGDTRNDK IKPSTETRKL ESVFFHSLSG
360 370 380 390 400
SKSSRRNFKE QAPKTRSLDF PQNEPQIKNQ FNKKLSGRLE NTKQQLQLPL
410 420
HPSWEASRRR KEQQSNIAVF QGKKITFDD
Length:429
Mass (Da):48,634
Last modified:October 1, 2002 - v1
Checksum:i6046C3E73C87BCF0
GO

Sequence cautioni

The sequence BAB71631.1 differs from that shown. Reason: Frameshift at position 425. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti345 – 3451F → S in BAB71631 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY611630 mRNA. Translation: AAU25829.2.
AK058015 mRNA. Translation: BAB71631.1. Frameshift.
CH471086 Genomic DNA. Translation: EAW48900.1.
BC017102 mRNA. Translation: AAH17102.1.
BC031222 mRNA. Translation: AAH31222.1.
CCDSiCCDS43354.1.
RefSeqiNP_689759.2. NM_152546.2.
UniGeneiHs.107622.

Genome annotation databases

EnsembliENST00000339397; ENSP00000341324; ENSG00000151304.
GeneIDi153443.
KEGGihsa:153443.
UCSCiuc003kst.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY611630 mRNA. Translation: AAU25829.2.
AK058015 mRNA. Translation: BAB71631.1. Frameshift.
CH471086 Genomic DNA. Translation: EAW48900.1.
BC017102 mRNA. Translation: AAH17102.1.
BC031222 mRNA. Translation: AAH31222.1.
CCDSiCCDS43354.1.
RefSeqiNP_689759.2. NM_152546.2.
UniGeneiHs.107622.

3D structure databases

ProteinModelPortaliQ8NEF9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127495. 6 interactions.
IntActiQ8NEF9. 6 interactions.
MINTiMINT-4932778.
STRINGi9606.ENSP00000341324.

PTM databases

iPTMnetiQ8NEF9.
PhosphoSiteiQ8NEF9.

Polymorphism and mutation databases

BioMutaiSRFBP1.
DMDMi74751249.

Proteomic databases

EPDiQ8NEF9.
MaxQBiQ8NEF9.
PaxDbiQ8NEF9.
PeptideAtlasiQ8NEF9.
PRIDEiQ8NEF9.
TopDownProteomicsiQ8NEF9.

Protocols and materials databases

DNASUi153443.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000339397; ENSP00000341324; ENSG00000151304.
GeneIDi153443.
KEGGihsa:153443.
UCSCiuc003kst.2. human.

Organism-specific databases

CTDi153443.
GeneCardsiSRFBP1.
H-InvDBHIX0005119.
HGNCiHGNC:26333. SRFBP1.
HPAiHPA042737.
HPA058150.
MIMi610479. gene.
neXtProtiNX_Q8NEF9.
PharmGKBiPA142670870.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEZ8. Eukaryota.
ENOG4111UG3. LUCA.
GeneTreeiENSGT00390000006478.
HOGENOMiHOG000154413.
HOVERGENiHBG056694.
InParanoidiQ8NEF9.
OMAiFKEARQN.
OrthoDBiEOG79KPG5.
PhylomeDBiQ8NEF9.
TreeFamiTF328596.

Miscellaneous databases

ChiTaRSiSRFBP1. human.
GenomeRNAii153443.
PROiQ8NEF9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NEF9.
CleanExiHS_SRFBP1.
GenevisibleiQ8NEF9. HS.

Family and domain databases

InterProiIPR015158. Bud22/SRFB1.
[Graphical view]
PfamiPF09073. BUD22. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel serum response factor cofactor in cardiac gene regulation."
    Zhang X., Azhar G., Zhong Y., Wei J.Y.
    J. Biol. Chem. 279:55626-55632(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: HeartImported.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Gastric mucosaImported.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: RetinoblastomaImported and TestisImported.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279 AND SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-205 AND SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-264; SER-349; SER-351 AND SER-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSRFB1_HUMAN
AccessioniPrimary (citable) accession number: Q8NEF9
Secondary accession number(s): Q5QFI2, Q96AH4, Q96DK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 1, 2002
Last modified: July 6, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.