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Q6ZRS2

- SRCAP_HUMAN

UniProt

Q6ZRS2 - SRCAP_HUMAN

Protein

Helicase SRCAP

Gene

SRCAP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    Catalytic component of the SRCAP complex which mediates the ATP-dependent exchange of histone H2AZ/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling. Acts as a coactivator for CREB-mediated transcription, steroid receptor-mediated transcription, and Notch-mediated transcription.6 Publications

    Kineticsi

    1. KM=66 µM for ATP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi643 – 6508ATPPROSITE-ProRule annotation
    DNA bindingi2857 – 286913A.T hook 1Add
    BLAST
    DNA bindingi2936 – 294813A.T hook 2Add
    BLAST
    DNA bindingi3004 – 301613A.T hook 3Add
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. helicase activity Source: UniProtKB-KW
    4. histone acetyltransferase activity Source: ProtInc
    5. transcription coactivator activity Source: ProtInc

    GO - Biological processi

    1. histone acetylation Source: GOC
    2. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    3. transcription, DNA-templated Source: UniProtKB-KW
    4. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Helicase, Hydrolase

    Keywords - Biological processi

    Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Helicase SRCAP (EC:3.6.4.-)
    Alternative name(s):
    Domino homolog 2
    Snf2-related CBP activator
    Gene namesi
    Name:SRCAP
    Synonyms:KIAA0309
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:16974. SRCAP.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. Golgi apparatus Source: HPA
    2. nucleus Source: HPA
    3. protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Floating-Harbor syndrome (FLHS) [MIM:136140]: A rare genetic disorder characterized by proportionate short stature, delayed bone age, delayed speech development, and typical facial features. The face is triangular with deep-set eyes, long eyelashes, bulbous nose, wide columella, short philtrum, and thin lips.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi136140. phenotype.
    Orphaneti2044. Floating-Harbor syndrome.
    PharmGKBiPA162404706.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 32303230Helicase SRCAPPRO_0000311236Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei274 – 2741Phosphoserine1 Publication
    Modified residuei572 – 5721Phosphothreonine1 Publication
    Modified residuei2430 – 24301Phosphoserine1 Publication
    Modified residuei2869 – 28691Phosphoserine1 Publication
    Modified residuei3148 – 31481Phosphoserine3 Publications
    Modified residuei3161 – 31611Phosphoserine1 Publication
    Modified residuei3172 – 31721Phosphoserine1 Publication
    Modified residuei3177 – 31771Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ6ZRS2.
    PaxDbiQ6ZRS2.
    PRIDEiQ6ZRS2.

    PTM databases

    PhosphoSiteiQ6ZRS2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6ZRS2.
    BgeeiQ6ZRS2.
    CleanExiHS_SRCAP.
    GenevestigatoriQ6ZRS2.

    Organism-specific databases

    HPAiHPA028929.

    Interactioni

    Subunit structurei

    Interacts with CREBBP and EP300. May be part of a complex containing SRCAP, CREBBP, CARM1 and GRIP1. Component of the chromatin-remodeling SRCAP complex composed of at least SRCAP, DMAP1, RUVBL1, RUVBL2, ACTL6A, YEATS4, VPS72, ACTR6 and ZNHIT1. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. Interacts with hepatitis C virus (HCV) NS5A and human adenovirus 2 DBP.7 Publications

    Protein-protein interaction databases

    BioGridi116058. 23 interactions.
    IntActiQ6ZRS2. 14 interactions.
    MINTiMINT-123408.
    STRINGi9606.ENSP00000262518.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6ZRS2.
    SMRiQ6ZRS2. Positions 611-930, 2023-2209.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini124 – 19673HSAPROSITE-ProRule annotationAdd
    BLAST
    Domaini630 – 795166Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2044 – 2197154Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi275 – 2784Poly-Pro
    Compositional biasi293 – 563271Glu-richAdd
    BLAST
    Compositional biasi981 – 1883903Pro-richAdd
    BLAST
    Compositional biasi2227 – 2362136Glu-richAdd
    BLAST
    Compositional biasi2426 – 3023598Pro-richAdd
    BLAST
    Compositional biasi3179 – 31824Poly-Glu

    Sequence similaritiesi

    Contains 3 A.T hook DNA-binding domains.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 HSA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0553.
    HOGENOMiHOG000168717.
    InParanoidiQ6ZRS2.
    KOiK11661.
    OMAiPSSTQTM.
    OrthoDBiEOG79CXXJ.
    PhylomeDBiQ6ZRS2.
    TreeFamiTF106424.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR020478. AT_hook-like.
    IPR017956. AT_hook_DNA-bd_motif.
    IPR014012. Helicase/SANT-assoc_DNA-bd.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view]
    PfamiPF00271. Helicase_C. 1 hit.
    PF07529. HSA. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view]
    PRINTSiPR00929. ATHOOK.
    SMARTiSM00384. AT_hook. 3 hits.
    SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 4 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51204. HSA. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6ZRS2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MQSSPSPAHP QLPVLQTQMV SDGMTGSNPV SPASSSSPAS SGAGGISPQH     50
    IAQDSSLDGP PGPPDGATVP LEGFSLSQAA DLANKGPKWE KSHAEIAEQA 100
    KHEAEIETRI AELRKEGFWS LKRLPKVPEP PRPKGHWDYL CEEMQWLSAD 150
    FAQERRWKRG VARKVVRMVI RHHEEQRQKE ERARREEQAK LRRIASTMAK 200
    DVRQFWSNVE KVVQFKQQSR LEEKRKKALD LHLDFIVGQT EKYSDLLSQS 250
    LNQPLTSSKA GSSPCLGSSS AASSPPPPAS RLDDEDGDFQ PQEDEEEDDE 300
    ETIEVEEQQE GNDAEAQRRE IELLRREGEL PLEELLRSLP PQLLEGPSSP 350
    SQTPSSHDSD TRDGPEEGAE EEPPQVLEIK PPPSAVTQRN KQPWHPDEDD 400
    EEFTANEEEA EDEEDTIAAE EQLEGEVDHA MELSELAREG ELSMEELLQQ 450
    YAGAYAPGSG SSEDEDEDEV DANSSDCEPE GPVEAEEPPQ EDSSSQSDSV 500
    EDRSEDEEDE HSEEEETSGS SASEESESEE SEDAQSQSQA DEEEEDDDFG 550
    VEYLLARDEE QSEADAGSGP PTPGPTTLGP KKEITDIAAA AESLQPKGYT 600
    LATTQVKTPI PLLLRGQLRE YQHIGLDWLV TMYEKKLNGI LADEMGLGKT 650
    IQTISLLAHL ACEKGNWGPH LIIVPTSVML NWEMELKRWC PSFKILTYYG 700
    AQKERKLKRQ GWTKPNAFHV CITSYKLVLQ DHQAFRRKNW RYLILDEAQN 750
    IKNFKSQRWQ SLLNFNSQRR LLLTGTPLQN SLMELWSLMH FLMPHVFQSH 800
    REFKEWFSNP LTGMIEGSQE YNEGLVKRLH KVLRPFLLRR VKVDVEKQMP 850
    KKYEHVIRCR LSKRQRCLYD DFMAQTTTKE TLATGHFMSV INILMQLRKV 900
    CNHPNLFDPR PVTSPFITPG ICFSTASLVL RATDVHPLQR IDMGRFDLIG 950
    LEGRVSRYEA DTFLPRHRLS RRVLLEVATA PDPPPRPKPV KMKVNRMLQP 1000
    VPKQEGRTVV VVNNPRAPLG PVPVRPPPGP ELSAQPTPGP VPQVLPASLM 1050
    VSASPAGPPL IPASRPPGPV LLPPLQPNSG SLPQVLPSPL GVLSGTSRPP 1100
    TPTLSLKPTP PAPVRLSPAP PPGSSSLLKP LTVPPGYTFP PAAATTTSTT 1150
    TATATTTAVP APTPAPQRLI LSPDMQARLP SGEVVSIGQL ASLAQRPVAN 1200
    AGGSKPLTFQ IQGNKLTLTG AQVRQLAVGQ PRPLQRNVVH LVSAGGQHHL 1250
    ISQPAHVALI QAVAPTPGPT PVSVLPSSTP STTPAPTGLS LPLAANQVPP 1300
    TMVNNTGVVK IVVRQAPRDG LTPVPPLAPA PRPPSSGLPA VLNPRPTLTP 1350
    GRLPTPTLGT ARAPMPTPTL VRPLLKLVHS PSPEVSASAP GAAPLTISSP 1400
    LHVPSSLPGP ASSPMPIPNS SPLASPVSST VSVPLSSSLP ISVPTTLPAP 1450
    ASAPLTIPIS APLTVSASGP ALLTSVTPPL APVVPAAPGP PSLAPSGASP 1500
    SASALTLGLA TAPSLSSSQT PGHPLLLAPT SSHVPGLNST VAPACSPVLV 1550
    PASALASPFP SAPNPAPAQA SLLAPASSAS QALATPLAPM AAPQTAILAP 1600
    SPAPPLAPLP VLAPSPGAAP VLASSQTPVP VMAPSSTPGT SLASASPVPA 1650
    PTPVLAPSST QTMLPAPVPS PLPSPASTQT LALAPALAPT LGGSSPSQTL 1700
    SLGTGNPQGP FPTQTLSLTP ASSLVPTPAQ TLSLAPGPPL GPTQTLSLAP 1750
    APPLAPASPV GPAPAHTLTL APASSSASLL APASVQTLTL SPAPVPTLGP 1800
    AAAQTLALAP ASTQSPASQA SSLVVSASGA APLPVTMVSR LPVSKDEPDT 1850
    LTLRSGPPSP PSTATSFGGP RPRRQPPPPP RSPFYLDSLE EKRKRQRSER 1900
    LERIFQLSEA HGALAPVYGT EVLDFCTLPQ PVASPIGPRS PGPSHPTFWT 1950
    YTEAAHRAVL FPQQRLDQLS EIIERFIFVM PPVEAPPPSL HACHPPPWLA 2000
    PRQAAFQEQL ASELWPRARP LHRIVCNMRT QFPDLRLIQY DCGKLQTLAV 2050
    LLRQLKAEGH RVLIFTQMTR MLDVLEQFLT YHGHLYLRLD GSTRVEQRQA 2100
    LMERFNADKR IFCFILSTRS GGVGVNLTGA DTVVFYDSDW NPTMDAQAQD 2150
    RCHRIGQTRD VHIYRLISER TVEENILKKA NQKRMLGDMA IEGGNFTTAY 2200
    FKQQTIRELF DMPLEEPSSS SVPSAPEEEE ETVASKQTHI LEQALCRAED 2250
    EEDIRAATQA KAEQVAELAE FNENDGFPAG EGEEAGRPGA EDEEMSRAEQ 2300
    EIAALVEQLT PIERYAMKFL EASLEEVSRE ELKQAEEQVE AARKDLDQAK 2350
    EEVFRLPQEE EEGPGAGDES SCGTGGGTHR RSKKAKAPER PGTRVSERLR 2400
    GARAETQGAN HTPVISAHQT RSTTTPPRCS PARERVPRPA PRPRPTPASA 2450
    PAAIPALVPV PVSAPVPISA PNPITILPVH ILPSPPPPSQ IPPCSSPACT 2500
    PPPACTPPPA HTPPPAQTCL VTPSSPLLLG PPSVPISASV TNLPLGLRPE 2550
    AELCAQALAS PESLELASVA SSETSSLSLV PPKDLLPVAV EILPVSEKNL 2600
    SLTPSAPSLT LEAGSIPNGQ EQEAPDSAEG TTLTVLPEGE ELPLCVSESN 2650
    GLELPPSAAS DEPLQEPLEA DRTSEELTEA KTPTSSPEKP QELVTAEVAA 2700
    PSTSSSATSS PEGPSPARPP RRRTSADVEI RGQGTGRPGQ PPGPKVLRKL 2750
    PGRLVTVVEE KELVRRRRQQ RGAASTLVPG VSETSASPGS PSVRSMSGPE 2800
    SSPPIGGPCE AAPSSSLPTP PQQPFIARRH IELGVTGGGS PENGDGALLA 2850
    ITPPAVKRRR GRPPKKNRSP ADAGRGVDEA PSSTLKGKTN GADPVPGPET 2900
    LIVADPVLEP QLIPGPQPLG PQPVHRPNPL LSPVEKRRRG RPPKARDLPI 2950
    PGTISSAGDG NSESRTQPPP HPSPLTPLPP LLVCPTATVA NTVTTVTIST 3000
    SPPKRKRGRP PKNPPSPRPS QLPVLDRDST SVLESCGLGR RRQPQGQGES 3050
    EGSSSDEDGS RPLTRLARLR LEAEGMRGRK SGGSMVVAVI QDDLDLADSG 3100
    PGGLELTPPV VSLTPKLRST RLRPGSLVPP LETEKLPRKR AGAPVGGSPG 3150
    LAKRGRLQPP SPLGPEGSVE ESEAEASGEE EEGDGTPRRR PGPRRLVGTT 3200
    NQGDQRILRS SAPPSLAGPA VSHRGRKAKT 3230
    Length:3,230
    Mass (Da):343,555
    Last modified:May 18, 2010 - v3
    Checksum:i3CFB74C7BDFBEAD0
    GO
    Isoform 2 (identifier: Q6ZRS2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1236-1298: RNVVHLVSAGGQHHLISQPAHVALIQAVAPTPGPTPVSVLPSSTPSTTPAPTGLSLPLAANQV → M

    Show »
    Length:3,168
    Mass (Da):337,445
    Checksum:iB9A0D36717389361
    GO
    Isoform 3 (identifier: Q6ZRS2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1085-1181: VLPSPLGVLS...SPDMQARLPS → A
         1236-1298: RNVVHLVSAGGQHHLISQPAHVALIQAVAPTPGPTPVSVLPSSTPSTTPAPTGLSLPLAANQV → M

    Show »
    Length:3,072
    Mass (Da):327,838
    Checksum:iEA4D60708B59DC5B
    GO

    Sequence cautioni

    The sequence AAI59100.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1147 – 11471T → A in BAC87237. (PubMed:14702039)Curated
    Sequence conflicti1494 – 14941A → Q in AAD39760. (PubMed:10347196)Curated
    Sequence conflicti2765 – 27651R → Q in AAD39760. (PubMed:10347196)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1085 – 118197VLPSP…ARLPS → A in isoform 3. 2 PublicationsVSP_029441Add
    BLAST
    Alternative sequencei1236 – 129863RNVVH…AANQV → M in isoform 2 and isoform 3. 3 PublicationsVSP_029442Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC093249 Genomic DNA. No translation available.
    AC106886 Genomic DNA. No translation available.
    AK128030 mRNA. Translation: BAC87237.1.
    AB002307 mRNA. Translation: BAA20768.2.
    BC159099 mRNA. Translation: AAI59100.1. Different initiation.
    AF143946 mRNA. Translation: AAD39760.1.
    CCDSiCCDS10689.2. [Q6ZRS2-1]
    RefSeqiNP_006653.2. NM_006662.2. [Q6ZRS2-1]
    UniGeneiHs.620916.

    Genome annotation databases

    EnsembliENST00000262518; ENSP00000262518; ENSG00000080603. [Q6ZRS2-1]
    ENST00000380361; ENSP00000369719; ENSG00000080603.
    ENST00000395059; ENSP00000378499; ENSG00000080603. [Q6ZRS2-2]
    GeneIDi10847.
    KEGGihsa:10847.
    UCSCiuc002dze.1. human. [Q6ZRS2-1]
    uc002dzg.1. human. [Q6ZRS2-2]

    Polymorphism databases

    DMDMi296452947.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC093249 Genomic DNA. No translation available.
    AC106886 Genomic DNA. No translation available.
    AK128030 mRNA. Translation: BAC87237.1 .
    AB002307 mRNA. Translation: BAA20768.2 .
    BC159099 mRNA. Translation: AAI59100.1 . Different initiation.
    AF143946 mRNA. Translation: AAD39760.1 .
    CCDSi CCDS10689.2. [Q6ZRS2-1 ]
    RefSeqi NP_006653.2. NM_006662.2. [Q6ZRS2-1 ]
    UniGenei Hs.620916.

    3D structure databases

    ProteinModelPortali Q6ZRS2.
    SMRi Q6ZRS2. Positions 611-930, 2023-2209.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116058. 23 interactions.
    IntActi Q6ZRS2. 14 interactions.
    MINTi MINT-123408.
    STRINGi 9606.ENSP00000262518.

    PTM databases

    PhosphoSitei Q6ZRS2.

    Polymorphism databases

    DMDMi 296452947.

    Proteomic databases

    MaxQBi Q6ZRS2.
    PaxDbi Q6ZRS2.
    PRIDEi Q6ZRS2.

    Protocols and materials databases

    DNASUi 10847.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262518 ; ENSP00000262518 ; ENSG00000080603 . [Q6ZRS2-1 ]
    ENST00000380361 ; ENSP00000369719 ; ENSG00000080603 .
    ENST00000395059 ; ENSP00000378499 ; ENSG00000080603 . [Q6ZRS2-2 ]
    GeneIDi 10847.
    KEGGi hsa:10847.
    UCSCi uc002dze.1. human. [Q6ZRS2-1 ]
    uc002dzg.1. human. [Q6ZRS2-2 ]

    Organism-specific databases

    CTDi 10847.
    GeneCardsi GC16P030710.
    GeneReviewsi SRCAP.
    H-InvDB HIX0012970.
    HGNCi HGNC:16974. SRCAP.
    HPAi HPA028929.
    MIMi 136140. phenotype.
    611421. gene.
    neXtProti NX_Q6ZRS2.
    Orphaneti 2044. Floating-Harbor syndrome.
    PharmGKBi PA162404706.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0553.
    HOGENOMi HOG000168717.
    InParanoidi Q6ZRS2.
    KOi K11661.
    OMAi PSSTQTM.
    OrthoDBi EOG79CXXJ.
    PhylomeDBi Q6ZRS2.
    TreeFami TF106424.

    Miscellaneous databases

    ChiTaRSi SRCAP. human.
    GeneWikii SRCAP.
    GenomeRNAii 10847.
    NextBioi 41182.
    PROi Q6ZRS2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6ZRS2.
    Bgeei Q6ZRS2.
    CleanExi HS_SRCAP.
    Genevestigatori Q6ZRS2.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR020478. AT_hook-like.
    IPR017956. AT_hook_DNA-bd_motif.
    IPR014012. Helicase/SANT-assoc_DNA-bd.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view ]
    Pfami PF00271. Helicase_C. 1 hit.
    PF07529. HSA. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00929. ATHOOK.
    SMARTi SM00384. AT_hook. 3 hits.
    SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 4 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51204. HSA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] OF 1-2427 (ISOFORM 1).
      Tissue: Testis.
    3. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-3230 (ISOFORM 3).
      Tissue: Brain.
    4. Ohara O., Nagase T., Kikuno R., Nomura N.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    5. "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] OF 20-3230 (ISOFORM 3).
    6. "Identification of a novel SNF2/SWI2 protein family member, SRCAP, which interacts with CREB-binding protein."
      Johnston H., Kneer J., Chackalaparampil I., Yaciuk P., Chrivia J.
      J. Biol. Chem. 274:16370-16376(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 128-3230 (ISOFORM 2), INTERACTION WITH CREBBP, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION.
    7. "Hepatitis C virus NS5A protein modulates transcription through a novel cellular transcription factor SRCAP."
      Ghosh A.K., Majumder M., Steele R., Yaciuk P., Chrivia J., Ray R., Ray R.B.
      J. Biol. Chem. 275:7184-7188(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCV NS5A, SUBCELLULAR LOCATION.
    8. "Regulation of cAMP-responsive element-binding protein-mediated transcription by the SNF2/SWI-related protein, SRCAP."
      Monroy M.A., Ruhl D.D., Xu X., Granner D.K., Yaciuk P., Chrivia J.C.
      J. Biol. Chem. 276:40721-40726(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Adenovirus DNA binding protein interacts with the SNF2-related CBP activator protein (SrCap) and inhibits SrCap-mediated transcription."
      Xu X., Chackalaparampil I., Monroy M.A., Cannella M.T., Pesek E., Chrivia J., Yaciuk P.
      J. Virol. 75:10033-10040(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EP300 AND HADV-2 DBP.
    10. "SNF2-related CBP activator protein (SRCAP) functions as a coactivator of steroid receptor-mediated transcription through synergistic interactions with CARM-1 and GRIP-1."
      Monroy M.A., Schott N.M., Cox L., Chen J.D., Ruh M., Chrivia J.C.
      Mol. Endocrinol. 17:2519-2528(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH CREBBP; CARM1 AND GRIP1.
    11. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
      Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
      Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A NUA4-RELATED COMPLEX.
    12. "The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes."
      Cai Y., Jin J., Florens L., Swanson S.K., Kusch T., Li B., Workman J.L., Washburn M.P., Conaway R.C., Conaway J.W.
      J. Biol. Chem. 280:13665-13670(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SRCAP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "Human SRCAP and Drosophila melanogaster DOM are homologs that function in the notch signaling pathway."
      Eissenberg J.C., Wong M., Chrivia J.C.
      Mol. Cell. Biol. 25:6559-6569(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Purification of a human SRCAP complex that remodels chromatin by incorporating the histone variant H2A.Z into nucleosomes."
      Ruhl D.D., Jin J., Cai Y., Swanson S., Florens L., Washburn M.P., Conaway R.C., Conaway J.W., Chrivia J.C.
      Biochemistry 45:5671-5677(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SRCAP COMPLEX, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "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-2869 AND SER-3148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "The chromatin remodeling protein, SRCAP, is critical for deposition of the histone variant H2A.Z at promoters."
      Wong M.M., Cox L.K., Chrivia J.C.
      J. Biol. Chem. 282:26132-26139(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2430, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; THR-572; SER-3161; SER-3172 AND SER-3177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    21. "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-3148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "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-3148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: INVOLVEMENT IN FLHS.

    Entry informationi

    Entry nameiSRCAP_HUMAN
    AccessioniPrimary (citable) accession number: Q6ZRS2
    Secondary accession number(s): B0JZA6
    , O15026, Q7Z744, Q9Y5L9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 101 of the entry and version 3 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 16
      Human chromosome 16: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3