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P11831

- SRF_HUMAN

UniProt

P11831 - SRF_HUMAN

Protein

Serum response factor

Gene

SRF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    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

    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 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

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

    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)1 Publication
    Glycosylationi309 – 3091O-linked (GlcNAc)1 Publication
    Glycosylationi316 – 3161O-linked (GlcNAc)1 PublicationCAR_000196
    Glycosylationi383 – 3831O-linked (GlcNAc)1 Publication
    Modified residuei435 – 4351Phosphoserine; by dsDNA kinase1 Publication
    Modified residuei446 – 4461Phosphoserine; by dsDNA kinase1 Publication

    Post-translational modificationi

    Phosphorylated by PRKDC.6 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.By similarity3 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11831.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini141 – 20161MADS-boxPROSITE-ProRule annotationAdd
    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.PROSITE-ProRule annotation

    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

    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: October 1, 2014
    This is version 167 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