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P11831 (SRF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serum response factor

Short name=SRF
Gene names
Name:SRF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS). Required for cardiac differentiation and maturation.

Subunit structure

Binds DNA as a multimer, probably a dimer. Interacts with MLLT7/FOXO4, NKX3A and SSRP1. Interacts with ARID2 and SRFBP1 By similarity. Forms complexes with ARID2, MYOCD, NKX2-5 and SRFBP1 By similarity. Forms a nuclear ternary complex with MKL1 and SCAI. Interacts with LPXN. Ref.9 Ref.11 Ref.13

Subcellular location

Nucleus Ref.13.

Post-translational modification

Phosphorylated by PRKDC. Ref.5 Ref.6 Ref.8

Sequence similarities

Contains 1 MADS-box domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis involved in wound healing

Traceable author statement PubMed 15180964. Source: BHF-UCL

associative learning

Inferred from electronic annotation. Source: Ensembl

cardiac myofibril assembly

Inferred from electronic annotation. Source: Ensembl

cardiac vascular smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

cell migration involved in sprouting angiogenesis

Inferred from mutant phenotype PubMed 15180964. Source: BHF-UCL

cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

cellular senescence

Inferred from mutant phenotype PubMed 15282327. Source: BHF-UCL

contractile actin filament bundle assembly

Inferred from electronic annotation. Source: Ensembl

developmental growth

Inferred from electronic annotation. Source: Ensembl

dorsal aorta morphogenesis

Inferred from electronic annotation. Source: Ensembl

epithelial cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

epithelial structure maintenance

Inferred from electronic annotation. Source: Ensembl

erythrocyte development

Inferred from electronic annotation. Source: Ensembl

eyelid development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from sequence or structural similarity. Source: BHF-UCL

heart looping

Inferred from sequence or structural similarity. Source: BHF-UCL

heart trabecula formation

Inferred from electronic annotation. Source: Ensembl

hematopoietic stem cell differentiation

Inferred from electronic annotation. Source: Ensembl

hippocampus development

Inferred from electronic annotation. Source: Ensembl

long term synaptic depression

Inferred from electronic annotation. Source: Ensembl

long-term memory

Inferred from electronic annotation. Source: Ensembl

mRNA transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: BHF-UCL

megakaryocyte development

Inferred from electronic annotation. Source: Ensembl

mesoderm formation

Inferred from electronic annotation. Source: Ensembl

morphogenesis of an epithelial sheet

Inferred from electronic annotation. Source: Ensembl

muscle cell cellular homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of beta-amyloid clearance

Inferred from mutant phenotype PubMed 19098903. Source: BHF-UCL

negative regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

neuron development

Traceable author statement PubMed 17200232. Source: BHF-UCL

neuron migration

Inferred from electronic annotation. Source: Ensembl

neuron projection development

Inferred from electronic annotation. Source: Ensembl

patterning of blood vessels

Inferred from electronic annotation. Source: Ensembl

platelet activation

Inferred from electronic annotation. Source: Ensembl

platelet formation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell differentiation

Inferred from direct assay PubMed 17576768. Source: MGI

positive regulation of filopodium assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 19098903. Source: BHF-UCL

positive regulation of smooth muscle contraction

Inferred from direct assay PubMed 17215356. Source: BHF-UCL

positive regulation of transcription by glucose

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17576768. Source: MGI

positive regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation

Inferred from genetic interaction PubMed 19783823. Source: BHF-UCL

positive regulation of transcription initiation from RNA polymerase II promoter

Inferred from direct assay PubMed 8887666. Source: BHF-UCL

positive regulation of transcription via serum response element binding

Inferred from direct assay Ref.1PubMed 8887666. Source: BHF-UCL

positive thymic T cell selection

Inferred from electronic annotation. Source: Ensembl

primitive streak formation

Inferred from electronic annotation. Source: Ensembl

regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

regulation of smooth muscle cell differentiation

Traceable author statement PubMed 17215356. Source: BHF-UCL

regulation of water loss via skin

Inferred from electronic annotation. Source: Ensembl

response to cytokine

Inferred from mutant phenotype PubMed 15180964. Source: BHF-UCL

response to hormone

Inferred from direct assay PubMed 17975004. Source: BHF-UCL

response to hypoxia

Inferred from expression pattern PubMed 19098903. Source: BHF-UCL

response to toxic substance

Traceable author statement PubMed 12660819. Source: BHF-UCL

sarcomere organization

Inferred from electronic annotation. Source: Ensembl

skin morphogenesis

Inferred from electronic annotation. Source: Ensembl

stress fiber assembly

Inferred from electronic annotation. Source: Ensembl

tangential migration from the subventricular zone to the olfactory bulb

Inferred from electronic annotation. Source: Ensembl

tight junction assembly

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: BHF-UCL

trophectodermal cell differentiation

Inferred from direct assay PubMed 17576768. Source: MGI

   Cellular_componentcytoplasm

Traceable author statement PubMed 15180964. Source: BHF-UCL

nuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 2108863. Source: BHF-UCL

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: BHF-UCL

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 20808827. Source: UniProtKB

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II transcription factor binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from sequence or structural similarity. Source: BHF-UCL

chromatin DNA binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 14565952PubMed 18296735Ref.11Ref.13. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.1. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.1. Source: BHF-UCL

serum response element binding

Inferred from direct assay Ref.1. Source: BHF-UCL

transcription factor binding

Inferred from physical interaction Ref.9PubMed 18296735. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 508508Serum response factor
PRO_0000199423

Regions

Domain141 – 20161MADS-box
DNA binding133 – 22290
Region168 – 22255Involved in dimerization
Compositional bias13 – 142130Gly-rich
Compositional bias80 – 9011Asp/Glu-rich (acidic)
Compositional bias242 – 25817Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue771Phosphoserine Ref.6 Ref.12
Modified residue791Phosphoserine Ref.6 Ref.12
Modified residue831Phosphoserine Ref.6 Ref.12
Modified residue851Phosphoserine Ref.6 Ref.12
Modified residue1031Phosphoserine Ref.6
Modified residue2241Phosphoserine Ref.10 Ref.12 Ref.14
Modified residue2531Phosphoserine Ref.5
Modified residue4351Phosphoserine; by dsDNA kinase Ref.8
Modified residue4461Phosphoserine; by dsDNA kinase Ref.8
Glycosylation2771O-linked (GlcNAc) Ref.7
CAR_000181
Glycosylation3071O-linked (GlcNAc) Probable
Glycosylation3091O-linked (GlcNAc) Probable
Glycosylation3161O-linked (GlcNAc) Ref.7
CAR_000196
Glycosylation3831O-linked (GlcNAc) Probable

Secondary structure

............. 508
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11831 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 25505828D3276F44

FASTA50851,593
        10         20         30         40         50         60 
MLPTQAGAAA ALGRGSALGG SLNRTPTGRP GGGGGTRGAN GGRVPGNGAG LGPGRLEREA 

        70         80         90        100        110        120 
AAAAATTPAP TAGALYSGSE GDSESGEEEE LGAERRGLKR SLSEMEIGMV VGGPEASAAA 

       130        140        150        160        170        180 
TGGYGPVSGA VSGAKPGKKT RGRVKIKMEF IDNKLRRYTT FSKRKTGIMK KAYELSTLTG 

       190        200        210        220        230        240 
TQVLLLVASE TGHVYTFATR KLQPMITSET GKALIQTCLN SPDSPPRSDP TTDQRMSATG 

       250        260        270        280        290        300 
FEETDLTYQV SESDSSGETK DTLKPAFTVT NLPGTTSTIQ TAPSTSTTMQ VSSGPSFPIT 

       310        320        330        340        350        360 
NYLAPVSASV SPSAVSSANG TVLKSTGSGP VSSGGLMQLP TSFTLMPGGA VAQQVPVQAI 

       370        380        390        400        410        420 
QVHQAPQQAS PSRDSSTDLT QTSSSGTVTL PATIMTSSVP TTVGGHMMYP SPHAVMYAPT 

       430        440        450        460        470        480 
SGLGDGSLTV LNAFSQAPST MQVSHSQVQE PGGVPQVFLT ASSGTVQIPV SAVQLHQMAV 

       490        500 
IGQQAGSSSN LTELQVVNLD TAHSTKSE 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element."
Norman C., Runswick M., Pollock R., Treisman R.
Cell 55:989-1003(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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: Lung and Lymph.
[5]"C-terminal phosphorylation of the serum-response factor."
Janknecht R., Ernst W.H., Houthaeve T., Nordheim A.
Eur. J. Biochem. 216:469-475(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 210-221 AND 253-264, PHOSPHORYLATION AT SER-253.
[6]"Identification of multiple SRF N-terminal phosphorylation sites affecting DNA binding properties."
Janknecht R., Hipskind R.A., Houthaeve T., Nordheim A., Stunnenberg H.G.
EMBO J. 11:1045-1054(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-77; SER-79; SER-83; SER-85 AND SER-103.
[7]"Localization of O-GlcNAc modification on the serum response transcription factor."
Reason A.J., Morris H.R., Panico M., Marais R., Treisman R.H., Haltiwanger R.S., Hart G.W., Kelly W.G., Dell A.
J. Biol. Chem. 267:16911-16921(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-277; SER-307; SER-309; SER-316 AND SER-383.
[8]"The carboxyl-terminal transactivation domain of human serum response factor contains DNA-activated protein kinase phosphorylation sites."
Liu S.-H., Ma J.-T., Yueh A.Y., Lees-Miller S.P., Anderson C.W., Ng S.-Y.
J. Biol. Chem. 268:21147-21154(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-435 AND SER-446.
[9]"Phenotypic modulation of smooth muscle cells through interaction of Foxo4 and myocardin."
Liu Z.-P., Wang Z., Yanagisawa H., Olson E.N.
Dev. Cell 9:261-270(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MLLT7.
[10]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"The LIM protein leupaxin is enriched in smooth muscle and functions as an serum response factor cofactor to induce smooth muscle cell gene transcription."
Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P., Taylor J.M.
Circ. Res. 102:1502-1511(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LPXN.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-79; SER-83; SER-85 AND SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"SCAI acts as a suppressor of cancer cell invasion through the transcriptional control of beta1-integrin."
Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J., Nollau P., Grosse R.
Nat. Cell Biol. 11:557-568(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MKL1 AND SCAI, SUBCELLULAR LOCATION.
[14]"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-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Structure of serum response factor core bound to DNA."
Pellegrini L., Tan S., Richmond T.J.
Nature 376:490-498(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 132-223.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03161 mRNA. Translation: AAA36647.1.
AL133375, AL355385 Genomic DNA. Translation: CAI20207.1.
AL355385, AL133375 Genomic DNA. Translation: CAI13785.1.
CH471081 Genomic DNA. Translation: EAX04161.1.
BC048211 mRNA. Translation: AAH48211.1.
BC052572 mRNA. Translation: AAH52572.1.
CCDSCCDS4889.1.
PIRA31637.
RefSeqNP_003122.1. NM_003131.3.
UniGeneHs.520140.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HBXX-ray3.15A/B/D/E132-223[»]
1K6OX-ray3.19B/C133-235[»]
1SRSX-ray3.20A/B132-223[»]
DisProtDP00574.
ProteinModelPortalP11831.
SMRP11831. Positions 135-223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112600. 60 interactions.
DIPDIP-49N.
IntActP11831. 6 interactions.
MINTMINT-130058.
STRING9606.ENSP00000265354.

PTM databases

PhosphoSiteP11831.
UniCarbKBP11831.

Polymorphism databases

DMDM134876.

Proteomic databases

MaxQBP11831.
PaxDbP11831.
PRIDEP11831.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265354; ENSP00000265354; ENSG00000112658.
GeneID6722.
KEGGhsa:6722.
UCSCuc003oui.3. human.

Organism-specific databases

CTD6722.
GeneCardsGC06P043138.
HGNCHGNC:11291. SRF.
HPACAB005416.
HPA001819.
MIM600589. gene.
neXtProtNX_P11831.
PharmGKBPA36116.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5068.
HOGENOMHOG000012380.
HOVERGENHBG014968.
InParanoidP11831.
KOK04378.
OMANAFPQAP.
OrthoDBEOG76DTVJ.
PhylomeDBP11831.
TreeFamTF318482.

Enzyme and pathway databases

SignaLinkP11831.

Gene expression databases

ArrayExpressP11831.
BgeeP11831.
CleanExHS_SRF.
GenevestigatorP11831.

Family and domain databases

InterProIPR002100. TF_MADSbox.
[Graphical view]
PfamPF00319. SRF-TF. 1 hit.
[Graphical view]
PRINTSPR00404. MADSDOMAIN.
SMARTSM00432. MADS. 1 hit.
[Graphical view]
SUPFAMSSF55455. SSF55455. 1 hit.
PROSITEPS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11831.
GeneWikiSerum_response_factor.
GenomeRNAi6722.
NextBio26222.
PMAP-CutDBP11831.
PROP11831.
SOURCESearch...

Entry information

Entry nameSRF_HUMAN
AccessionPrimary (citable) accession number: P11831
Secondary accession number(s): Q5T648
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM