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Protein

Helicase SRCAP

Gene

SRCAP

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

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

    • ATP binding Source: UniProtKB-KW
    • DNA binding Source: UniProtKB-KW
    • helicase activity Source: UniProtKB-KW
    • histone acetyltransferase activity Source: ProtInc
    • transcription coactivator activity Source: ProtInc

    GO - Biological processi

    • histone acetylation Source: GOC
    • regulation of transcription from RNA polymerase II promoter Source: ProtInc
    • transcription, DNA-templated Source: UniProtKB-KW
    • viral process Source: UniProtKB-KW
    Complete GO annotation...

    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 Componenti: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:16974. SRCAP.

    Subcellular locationi

    • Nucleus PROSITE-ProRule annotation1 Publication

    GO - Cellular componenti

    • Golgi apparatus Source: HPA
    • nucleoplasm Source: HPA
    • nucleus Source: AgBase
    • perinuclear region of cytoplasm Source: AgBase
    • protein complex Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Floating-Harbor syndrome (FLHS)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA 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.

    See also OMIM:136140

    Organism-specific databases

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

    Polymorphism and mutation databases

    BioMutaiSRCAP.
    DMDMi296452947.

    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

    BgeeiQ6ZRS2.
    CleanExiHS_SRCAP.
    ExpressionAtlasiQ6ZRS2. baseline and differential.
    GenevisibleiQ6ZRS2. HS.

    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. 31 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.
    GeneTreeiENSGT00530000063427.
    HOGENOMiHOG000168717.
    InParanoidiQ6ZRS2.
    KOiK11661.
    OMAiENDGFPA.
    OrthoDBiEOG79CXXJ.
    PhylomeDBiQ6ZRS2.
    TreeFamiTF106424.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR020478. AT_hook-like.
    IPR017956. AT_hook_DNA-bd_motif.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR014012. HSA_dom.
    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. AlignAdd to basket

    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

            10         20         30         40         50
    MQSSPSPAHP QLPVLQTQMV SDGMTGSNPV SPASSSSPAS SGAGGISPQH
    60 70 80 90 100
    IAQDSSLDGP PGPPDGATVP LEGFSLSQAA DLANKGPKWE KSHAEIAEQA
    110 120 130 140 150
    KHEAEIETRI AELRKEGFWS LKRLPKVPEP PRPKGHWDYL CEEMQWLSAD
    160 170 180 190 200
    FAQERRWKRG VARKVVRMVI RHHEEQRQKE ERARREEQAK LRRIASTMAK
    210 220 230 240 250
    DVRQFWSNVE KVVQFKQQSR LEEKRKKALD LHLDFIVGQT EKYSDLLSQS
    260 270 280 290 300
    LNQPLTSSKA GSSPCLGSSS AASSPPPPAS RLDDEDGDFQ PQEDEEEDDE
    310 320 330 340 350
    ETIEVEEQQE GNDAEAQRRE IELLRREGEL PLEELLRSLP PQLLEGPSSP
    360 370 380 390 400
    SQTPSSHDSD TRDGPEEGAE EEPPQVLEIK PPPSAVTQRN KQPWHPDEDD
    410 420 430 440 450
    EEFTANEEEA EDEEDTIAAE EQLEGEVDHA MELSELAREG ELSMEELLQQ
    460 470 480 490 500
    YAGAYAPGSG SSEDEDEDEV DANSSDCEPE GPVEAEEPPQ EDSSSQSDSV
    510 520 530 540 550
    EDRSEDEEDE HSEEEETSGS SASEESESEE SEDAQSQSQA DEEEEDDDFG
    560 570 580 590 600
    VEYLLARDEE QSEADAGSGP PTPGPTTLGP KKEITDIAAA AESLQPKGYT
    610 620 630 640 650
    LATTQVKTPI PLLLRGQLRE YQHIGLDWLV TMYEKKLNGI LADEMGLGKT
    660 670 680 690 700
    IQTISLLAHL ACEKGNWGPH LIIVPTSVML NWEMELKRWC PSFKILTYYG
    710 720 730 740 750
    AQKERKLKRQ GWTKPNAFHV CITSYKLVLQ DHQAFRRKNW RYLILDEAQN
    760 770 780 790 800
    IKNFKSQRWQ SLLNFNSQRR LLLTGTPLQN SLMELWSLMH FLMPHVFQSH
    810 820 830 840 850
    REFKEWFSNP LTGMIEGSQE YNEGLVKRLH KVLRPFLLRR VKVDVEKQMP
    860 870 880 890 900
    KKYEHVIRCR LSKRQRCLYD DFMAQTTTKE TLATGHFMSV INILMQLRKV
    910 920 930 940 950
    CNHPNLFDPR PVTSPFITPG ICFSTASLVL RATDVHPLQR IDMGRFDLIG
    960 970 980 990 1000
    LEGRVSRYEA DTFLPRHRLS RRVLLEVATA PDPPPRPKPV KMKVNRMLQP
    1010 1020 1030 1040 1050
    VPKQEGRTVV VVNNPRAPLG PVPVRPPPGP ELSAQPTPGP VPQVLPASLM
    1060 1070 1080 1090 1100
    VSASPAGPPL IPASRPPGPV LLPPLQPNSG SLPQVLPSPL GVLSGTSRPP
    1110 1120 1130 1140 1150
    TPTLSLKPTP PAPVRLSPAP PPGSSSLLKP LTVPPGYTFP PAAATTTSTT
    1160 1170 1180 1190 1200
    TATATTTAVP APTPAPQRLI LSPDMQARLP SGEVVSIGQL ASLAQRPVAN
    1210 1220 1230 1240 1250
    AGGSKPLTFQ IQGNKLTLTG AQVRQLAVGQ PRPLQRNVVH LVSAGGQHHL
    1260 1270 1280 1290 1300
    ISQPAHVALI QAVAPTPGPT PVSVLPSSTP STTPAPTGLS LPLAANQVPP
    1310 1320 1330 1340 1350
    TMVNNTGVVK IVVRQAPRDG LTPVPPLAPA PRPPSSGLPA VLNPRPTLTP
    1360 1370 1380 1390 1400
    GRLPTPTLGT ARAPMPTPTL VRPLLKLVHS PSPEVSASAP GAAPLTISSP
    1410 1420 1430 1440 1450
    LHVPSSLPGP ASSPMPIPNS SPLASPVSST VSVPLSSSLP ISVPTTLPAP
    1460 1470 1480 1490 1500
    ASAPLTIPIS APLTVSASGP ALLTSVTPPL APVVPAAPGP PSLAPSGASP
    1510 1520 1530 1540 1550
    SASALTLGLA TAPSLSSSQT PGHPLLLAPT SSHVPGLNST VAPACSPVLV
    1560 1570 1580 1590 1600
    PASALASPFP SAPNPAPAQA SLLAPASSAS QALATPLAPM AAPQTAILAP
    1610 1620 1630 1640 1650
    SPAPPLAPLP VLAPSPGAAP VLASSQTPVP VMAPSSTPGT SLASASPVPA
    1660 1670 1680 1690 1700
    PTPVLAPSST QTMLPAPVPS PLPSPASTQT LALAPALAPT LGGSSPSQTL
    1710 1720 1730 1740 1750
    SLGTGNPQGP FPTQTLSLTP ASSLVPTPAQ TLSLAPGPPL GPTQTLSLAP
    1760 1770 1780 1790 1800
    APPLAPASPV GPAPAHTLTL APASSSASLL APASVQTLTL SPAPVPTLGP
    1810 1820 1830 1840 1850
    AAAQTLALAP ASTQSPASQA SSLVVSASGA APLPVTMVSR LPVSKDEPDT
    1860 1870 1880 1890 1900
    LTLRSGPPSP PSTATSFGGP RPRRQPPPPP RSPFYLDSLE EKRKRQRSER
    1910 1920 1930 1940 1950
    LERIFQLSEA HGALAPVYGT EVLDFCTLPQ PVASPIGPRS PGPSHPTFWT
    1960 1970 1980 1990 2000
    YTEAAHRAVL FPQQRLDQLS EIIERFIFVM PPVEAPPPSL HACHPPPWLA
    2010 2020 2030 2040 2050
    PRQAAFQEQL ASELWPRARP LHRIVCNMRT QFPDLRLIQY DCGKLQTLAV
    2060 2070 2080 2090 2100
    LLRQLKAEGH RVLIFTQMTR MLDVLEQFLT YHGHLYLRLD GSTRVEQRQA
    2110 2120 2130 2140 2150
    LMERFNADKR IFCFILSTRS GGVGVNLTGA DTVVFYDSDW NPTMDAQAQD
    2160 2170 2180 2190 2200
    RCHRIGQTRD VHIYRLISER TVEENILKKA NQKRMLGDMA IEGGNFTTAY
    2210 2220 2230 2240 2250
    FKQQTIRELF DMPLEEPSSS SVPSAPEEEE ETVASKQTHI LEQALCRAED
    2260 2270 2280 2290 2300
    EEDIRAATQA KAEQVAELAE FNENDGFPAG EGEEAGRPGA EDEEMSRAEQ
    2310 2320 2330 2340 2350
    EIAALVEQLT PIERYAMKFL EASLEEVSRE ELKQAEEQVE AARKDLDQAK
    2360 2370 2380 2390 2400
    EEVFRLPQEE EEGPGAGDES SCGTGGGTHR RSKKAKAPER PGTRVSERLR
    2410 2420 2430 2440 2450
    GARAETQGAN HTPVISAHQT RSTTTPPRCS PARERVPRPA PRPRPTPASA
    2460 2470 2480 2490 2500
    PAAIPALVPV PVSAPVPISA PNPITILPVH ILPSPPPPSQ IPPCSSPACT
    2510 2520 2530 2540 2550
    PPPACTPPPA HTPPPAQTCL VTPSSPLLLG PPSVPISASV TNLPLGLRPE
    2560 2570 2580 2590 2600
    AELCAQALAS PESLELASVA SSETSSLSLV PPKDLLPVAV EILPVSEKNL
    2610 2620 2630 2640 2650
    SLTPSAPSLT LEAGSIPNGQ EQEAPDSAEG TTLTVLPEGE ELPLCVSESN
    2660 2670 2680 2690 2700
    GLELPPSAAS DEPLQEPLEA DRTSEELTEA KTPTSSPEKP QELVTAEVAA
    2710 2720 2730 2740 2750
    PSTSSSATSS PEGPSPARPP RRRTSADVEI RGQGTGRPGQ PPGPKVLRKL
    2760 2770 2780 2790 2800
    PGRLVTVVEE KELVRRRRQQ RGAASTLVPG VSETSASPGS PSVRSMSGPE
    2810 2820 2830 2840 2850
    SSPPIGGPCE AAPSSSLPTP PQQPFIARRH IELGVTGGGS PENGDGALLA
    2860 2870 2880 2890 2900
    ITPPAVKRRR GRPPKKNRSP ADAGRGVDEA PSSTLKGKTN GADPVPGPET
    2910 2920 2930 2940 2950
    LIVADPVLEP QLIPGPQPLG PQPVHRPNPL LSPVEKRRRG RPPKARDLPI
    2960 2970 2980 2990 3000
    PGTISSAGDG NSESRTQPPP HPSPLTPLPP LLVCPTATVA NTVTTVTIST
    3010 3020 3030 3040 3050
    SPPKRKRGRP PKNPPSPRPS QLPVLDRDST SVLESCGLGR RRQPQGQGES
    3060 3070 3080 3090 3100
    EGSSSDEDGS RPLTRLARLR LEAEGMRGRK SGGSMVVAVI QDDLDLADSG
    3110 3120 3130 3140 3150
    PGGLELTPPV VSLTPKLRST RLRPGSLVPP LETEKLPRKR AGAPVGGSPG
    3160 3170 3180 3190 3200
    LAKRGRLQPP SPLGPEGSVE ESEAEASGEE EEGDGTPRRR PGPRRLVGTT
    3210 3220 3230
    NQGDQRILRS SAPPSLAGPA VSHRGRKAKT
    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.Curated

    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:
    EMBLi
    GenBanki
    DDBJi
    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.
    GeneIDi10847.
    KEGGihsa:10847.
    UCSCiuc002dze.1. human. [Q6ZRS2-1]
    uc002dzg.1. human. [Q6ZRS2-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi116058. 31 interactions.
    IntActiQ6ZRS2. 14 interactions.
    MINTiMINT-123408.
    STRINGi9606.ENSP00000262518.

    PTM databases

    PhosphoSiteiQ6ZRS2.

    Polymorphism and mutation databases

    BioMutaiSRCAP.
    DMDMi296452947.

    Proteomic databases

    MaxQBiQ6ZRS2.
    PaxDbiQ6ZRS2.
    PRIDEiQ6ZRS2.

    Protocols and materials databases

    DNASUi10847.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi10847.
    GeneCardsiGC16P030710.
    GeneReviewsiSRCAP.
    H-InvDBHIX0012970.
    HGNCiHGNC:16974. SRCAP.
    HPAiHPA028929.
    MIMi136140. phenotype.
    611421. gene.
    neXtProtiNX_Q6ZRS2.
    Orphaneti2044. Floating-Harbor syndrome.
    PharmGKBiPA162404706.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0553.
    GeneTreeiENSGT00530000063427.
    HOGENOMiHOG000168717.
    InParanoidiQ6ZRS2.
    KOiK11661.
    OMAiENDGFPA.
    OrthoDBiEOG79CXXJ.
    PhylomeDBiQ6ZRS2.
    TreeFamiTF106424.

    Miscellaneous databases

    ChiTaRSiSRCAP. human.
    GeneWikiiSRCAP.
    GenomeRNAii10847.
    NextBioi41182.
    PROiQ6ZRS2.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ6ZRS2.
    CleanExiHS_SRCAP.
    ExpressionAtlasiQ6ZRS2. baseline and differential.
    GenevisibleiQ6ZRS2. HS.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR020478. AT_hook-like.
    IPR017956. AT_hook_DNA-bd_motif.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR014012. HSA_dom.
    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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.
    24. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    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: July 22, 2015
    This is version 108 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

    Similar proteinsi

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