SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P11831

- SRF_HUMAN

UniProt

P11831 - SRF_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Serum response factor

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

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi133 – 22290Add
BLAST

GO - Molecular functioni

  1. chromatin DNA binding Source: Ensembl
  2. protein binding Source: UniProtKB
  3. protein homodimerization activity Source: BHF-UCL
  4. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  5. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: UniProtKB
  6. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: Ensembl
  7. RNA polymerase II transcription factor binding transcription factor activity Source: Ensembl
  8. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
  9. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  10. serum response element binding Source: BHF-UCL
  11. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. angiogenesis involved in wound healing Source: BHF-UCL
  2. associative learning Source: Ensembl
  3. cardiac myofibril assembly Source: Ensembl
  4. cardiac vascular smooth muscle cell differentiation Source: Ensembl
  5. cell-matrix adhesion Source: Ensembl
  6. cell migration involved in sprouting angiogenesis Source: BHF-UCL
  7. cellular response to glucose stimulus Source: Ensembl
  8. cellular senescence Source: BHF-UCL
  9. contractile actin filament bundle assembly Source: Ensembl
  10. developmental growth Source: Ensembl
  11. dorsal aorta morphogenesis Source: Ensembl
  12. epithelial cell-cell adhesion Source: Ensembl
  13. epithelial structure maintenance Source: Ensembl
  14. erythrocyte development Source: Ensembl
  15. eyelid development in camera-type eye Source: Ensembl
  16. heart development Source: BHF-UCL
  17. heart looping Source: BHF-UCL
  18. heart trabecula formation Source: Ensembl
  19. hematopoietic stem cell differentiation Source: Ensembl
  20. hippocampus development Source: Ensembl
  21. long-term memory Source: Ensembl
  22. long term synaptic depression Source: Ensembl
  23. megakaryocyte development Source: Ensembl
  24. mesoderm formation Source: Ensembl
  25. morphogenesis of an epithelial sheet Source: Ensembl
  26. mRNA transcription from RNA polymerase II promoter Source: BHF-UCL
  27. muscle cell cellular homeostasis Source: BHF-UCL
  28. negative regulation of beta-amyloid clearance Source: BHF-UCL
  29. negative regulation of cell migration Source: Ensembl
  30. negative regulation of cell proliferation Source: Ensembl
  31. neuron development Source: BHF-UCL
  32. neuron migration Source: Ensembl
  33. neuron projection development Source: Ensembl
  34. patterning of blood vessels Source: Ensembl
  35. platelet activation Source: Ensembl
  36. platelet formation Source: Ensembl
  37. positive regulation of cell differentiation Source: MGI
  38. positive regulation of filopodium assembly Source: Ensembl
  39. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  40. positive regulation of smooth muscle contraction Source: BHF-UCL
  41. positive regulation of transcription by glucose Source: Ensembl
  42. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  43. positive regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation Source: BHF-UCL
  44. positive regulation of transcription initiation from RNA polymerase II promoter Source: BHF-UCL
  45. positive regulation of transcription via serum response element binding Source: BHF-UCL
  46. positive thymic T cell selection Source: Ensembl
  47. primitive streak formation Source: Ensembl
  48. regulation of cell adhesion Source: Ensembl
  49. regulation of smooth muscle cell differentiation Source: BHF-UCL
  50. regulation of water loss via skin Source: Ensembl
  51. response to cytokine Source: BHF-UCL
  52. response to hormone Source: BHF-UCL
  53. response to hypoxia Source: BHF-UCL
  54. response to toxic substance Source: BHF-UCL
  55. sarcomere organization Source: Ensembl
  56. skin morphogenesis Source: Ensembl
  57. stress fiber assembly Source: Ensembl
  58. tangential migration from the subventricular zone to the olfactory bulb Source: Ensembl
  59. tight junction assembly Source: Ensembl
  60. transcription from RNA polymerase II promoter Source: BHF-UCL
  61. trophectodermal cell differentiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SignaLinkiP11831.

Names & Taxonomyi

Protein namesi
Recommended name:
Serum response factor
Short name:
SRF
Gene namesi
Name:SRF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:11291. SRF.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. nuclear chromatin Source: Ensembl
  3. nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36116.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508Serum response factorPRO_0000199423Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771Phosphoserine2 Publications
Modified residuei79 – 791Phosphoserine2 Publications
Modified residuei83 – 831Phosphoserine2 Publications
Modified residuei85 – 851Phosphoserine2 Publications
Modified residuei103 – 1031Phosphoserine1 Publication
Modified residuei224 – 2241Phosphoserine3 Publications
Modified residuei253 – 2531Phosphoserine1 Publication
Glycosylationi277 – 2771O-linked (GlcNAc)1 PublicationCAR_000181
Glycosylationi307 – 3071O-linked (GlcNAc) Inferred
Glycosylationi309 – 3091O-linked (GlcNAc) Inferred
Glycosylationi316 – 3161O-linked (GlcNAc)1 PublicationCAR_000196
Glycosylationi383 – 3831O-linked (GlcNAc) Inferred
Modified residuei435 – 4351Phosphoserine; by dsDNA kinase1 Publication
Modified residuei446 – 4461Phosphoserine; by dsDNA kinase1 Publication

Post-translational modificationi

Phosphorylated by PRKDC.3 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP11831.
PaxDbiP11831.
PRIDEiP11831.

PTM databases

PhosphoSiteiP11831.
UniCarbKBiP11831.

Miscellaneous databases

PMAP-CutDBP11831.

Expressioni

Gene expression databases

ArrayExpressiP11831.
BgeeiP11831.
CleanExiHS_SRF.
GenevestigatoriP11831.

Organism-specific databases

HPAiCAB005416.
HPA001819.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MKL1Q969V62EBI-493034,EBI-493122
MKL2Q9ULH73EBI-493034,EBI-493007
MYOCDQ8IZQ82EBI-493034,EBI-493384

Protein-protein interaction databases

BioGridi112600. 60 interactions.
DIPiDIP-49N.
IntActiP11831. 6 interactions.
MINTiMINT-130058.
STRINGi9606.ENSP00000265354.

Structurei

Secondary structure

1
508
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi154 – 17926
Beta strandi182 – 1887
Beta strandi190 – 1923
Beta strandi194 – 1985
Helixi200 – 2056
Helixi209 – 22012

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HBXX-ray3.15A/B/D/E132-223[»]
1K6OX-ray3.19B/C133-235[»]
1SRSX-ray3.20A/B132-223[»]
DisProtiDP00574.
ProteinModelPortaliP11831.
SMRiP11831. Positions 135-223.

Miscellaneous databases

EvolutionaryTraceiP11831.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini141 – 20161MADS-boxAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni168 – 22255Involved in dimerizationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 142130Gly-richAdd
BLAST
Compositional biasi80 – 9011Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi242 – 25817Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Contains 1 MADS-box domain.

Phylogenomic databases

eggNOGiCOG5068.
HOGENOMiHOG000012380.
HOVERGENiHBG014968.
InParanoidiP11831.
KOiK04378.
OMAiNAFPQAP.
OrthoDBiEOG76DTVJ.
PhylomeDBiP11831.
TreeFamiTF318482.

Family and domain databases

InterProiIPR002100. TF_MADSbox.
[Graphical view]
PfamiPF00319. SRF-TF. 1 hit.
[Graphical view]
PRINTSiPR00404. MADSDOMAIN.
SMARTiSM00432. MADS. 1 hit.
[Graphical view]
SUPFAMiSSF55455. SSF55455. 1 hit.
PROSITEiPS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11831-1 [UniParc]FASTAAdd to Basket

« Hide

MLPTQAGAAA ALGRGSALGG SLNRTPTGRP GGGGGTRGAN GGRVPGNGAG    50
LGPGRLEREA AAAAATTPAP TAGALYSGSE GDSESGEEEE LGAERRGLKR 100
SLSEMEIGMV VGGPEASAAA TGGYGPVSGA VSGAKPGKKT RGRVKIKMEF 150
IDNKLRRYTT FSKRKTGIMK KAYELSTLTG TQVLLLVASE TGHVYTFATR 200
KLQPMITSET GKALIQTCLN SPDSPPRSDP TTDQRMSATG FEETDLTYQV 250
SESDSSGETK DTLKPAFTVT NLPGTTSTIQ TAPSTSTTMQ VSSGPSFPIT 300
NYLAPVSASV SPSAVSSANG TVLKSTGSGP VSSGGLMQLP TSFTLMPGGA 350
VAQQVPVQAI QVHQAPQQAS PSRDSSTDLT QTSSSGTVTL PATIMTSSVP 400
TTVGGHMMYP SPHAVMYAPT SGLGDGSLTV LNAFSQAPST MQVSHSQVQE 450
PGGVPQVFLT ASSGTVQIPV SAVQLHQMAV IGQQAGSSSN LTELQVVNLD 500
TAHSTKSE 508
Length:508
Mass (Da):51,593
Last modified:October 1, 1989 - v1
Checksum:i25505828D3276F44
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4889.1.
PIRiA31637.
RefSeqiNP_003122.1. NM_003131.3.
UniGeneiHs.520140.

Genome annotation databases

EnsembliENST00000265354; ENSP00000265354; ENSG00000112658.
GeneIDi6722.
KEGGihsa:6722.
UCSCiuc003oui.3. human.

Polymorphism databases

DMDMi134876.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4889.1.
PIRi A31637.
RefSeqi NP_003122.1. NM_003131.3.
UniGenei Hs.520140.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HBX X-ray 3.15 A/B/D/E 132-223 [» ]
1K6O X-ray 3.19 B/C 133-235 [» ]
1SRS X-ray 3.20 A/B 132-223 [» ]
DisProti DP00574.
ProteinModelPortali P11831.
SMRi P11831. Positions 135-223.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112600. 60 interactions.
DIPi DIP-49N.
IntActi P11831. 6 interactions.
MINTi MINT-130058.
STRINGi 9606.ENSP00000265354.

PTM databases

PhosphoSitei P11831.
UniCarbKBi P11831.

Polymorphism databases

DMDMi 134876.

Proteomic databases

MaxQBi P11831.
PaxDbi P11831.
PRIDEi P11831.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265354 ; ENSP00000265354 ; ENSG00000112658 .
GeneIDi 6722.
KEGGi hsa:6722.
UCSCi uc003oui.3. human.

Organism-specific databases

CTDi 6722.
GeneCardsi GC06P043138.
HGNCi HGNC:11291. SRF.
HPAi CAB005416.
HPA001819.
MIMi 600589. gene.
neXtProti NX_P11831.
PharmGKBi PA36116.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5068.
HOGENOMi HOG000012380.
HOVERGENi HBG014968.
InParanoidi P11831.
KOi K04378.
OMAi NAFPQAP.
OrthoDBi EOG76DTVJ.
PhylomeDBi P11831.
TreeFami TF318482.

Enzyme and pathway databases

SignaLinki P11831.

Miscellaneous databases

EvolutionaryTracei P11831.
GeneWikii Serum_response_factor.
GenomeRNAii 6722.
NextBioi 26222.
PMAP-CutDB P11831.
PROi P11831.
SOURCEi Search...

Gene expression databases

ArrayExpressi P11831.
Bgeei P11831.
CleanExi HS_SRF.
Genevestigatori P11831.

Family and domain databases

InterProi IPR002100. TF_MADSbox.
[Graphical view ]
Pfami PF00319. SRF-TF. 1 hit.
[Graphical view ]
PRINTSi PR00404. MADSDOMAIN.
SMARTi SM00432. MADS. 1 hit.
[Graphical view ]
SUPFAMi SSF55455. SSF55455. 1 hit.
PROSITEi PS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiSRF_HUMAN
AccessioniPrimary (citable) accession number: P11831
Secondary accession number(s): Q5T648
Entry historyi
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 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi