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Q6ZRS2 (SRCAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Helicase SRCAP

EC=3.6.4.-
Alternative name(s):
Domino homolog 2
Snf2-related CBP activator
Gene names
Name:SRCAP
Synonyms:KIAA0309
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3230 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.8 Ref.10 Ref.13 Ref.14 Ref.16

Subunit structure

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. Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14

Subcellular location

Nucleus Ref.7.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23

Sequence similarities

Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.

Contains 3 A.T hook DNA-binding domains.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 HSA domain.

Biophysicochemical properties

Kinetic parameters:

KM=66 µM for ATP Ref.6

Sequence caution

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6ZRS2-1)

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.
Isoform 2 (identifier: Q6ZRS2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1236-1298: RNVVHLVSAGGQHHLISQPAHVALIQAVAPTPGPTPVSVLPSSTPSTTPAPTGLSLPLAANQV → M
Isoform 3 (identifier: Q6ZRS2-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 32303230Helicase SRCAP
PRO_0000311236

Regions

Domain124 – 19673HSA
Domain630 – 795166Helicase ATP-binding
Domain2044 – 2197154Helicase C-terminal
Nucleotide binding643 – 6508ATP By similarity
DNA binding2857 – 286913A.T hook 1
DNA binding2936 – 294813A.T hook 2
DNA binding3004 – 301613A.T hook 3
Compositional bias275 – 2784Poly-Pro
Compositional bias293 – 563271Glu-rich
Compositional bias981 – 1883903Pro-rich
Compositional bias2227 – 2362136Glu-rich
Compositional bias2426 – 3023598Pro-rich
Compositional bias3179 – 31824Poly-Glu

Amino acid modifications

Modified residue2741Phosphoserine Ref.20
Modified residue5721Phosphothreonine Ref.20
Modified residue24301Phosphoserine Ref.18
Modified residue28691Phosphoserine Ref.15
Modified residue31481Phosphoserine Ref.15 Ref.21 Ref.22
Modified residue31611Phosphoserine Ref.20
Modified residue31721Phosphoserine Ref.20
Modified residue31771Phosphoserine Ref.20

Natural variations

Alternative sequence1085 – 118197VLPSP…ARLPS → A in isoform 3.
VSP_029441
Alternative sequence1236 – 129863RNVVH…AANQV → M in isoform 2 and isoform 3.
VSP_029442

Experimental info

Sequence conflict11471T → A in BAC87237. Ref.2
Sequence conflict14941A → Q in AAD39760. Ref.6
Sequence conflict27651R → Q in AAD39760. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 3CFB74C7BDFBEAD0

FASTA3,230343,555
        10         20         30         40         50         60 
MQSSPSPAHP QLPVLQTQMV SDGMTGSNPV SPASSSSPAS SGAGGISPQH IAQDSSLDGP 

        70         80         90        100        110        120 
PGPPDGATVP LEGFSLSQAA DLANKGPKWE KSHAEIAEQA KHEAEIETRI AELRKEGFWS 

       130        140        150        160        170        180 
LKRLPKVPEP PRPKGHWDYL CEEMQWLSAD FAQERRWKRG VARKVVRMVI RHHEEQRQKE 

       190        200        210        220        230        240 
ERARREEQAK LRRIASTMAK DVRQFWSNVE KVVQFKQQSR LEEKRKKALD LHLDFIVGQT 

       250        260        270        280        290        300 
EKYSDLLSQS LNQPLTSSKA GSSPCLGSSS AASSPPPPAS RLDDEDGDFQ PQEDEEEDDE 

       310        320        330        340        350        360 
ETIEVEEQQE GNDAEAQRRE IELLRREGEL PLEELLRSLP PQLLEGPSSP SQTPSSHDSD 

       370        380        390        400        410        420 
TRDGPEEGAE EEPPQVLEIK PPPSAVTQRN KQPWHPDEDD EEFTANEEEA EDEEDTIAAE 

       430        440        450        460        470        480 
EQLEGEVDHA MELSELAREG ELSMEELLQQ YAGAYAPGSG SSEDEDEDEV DANSSDCEPE 

       490        500        510        520        530        540 
GPVEAEEPPQ EDSSSQSDSV EDRSEDEEDE HSEEEETSGS SASEESESEE SEDAQSQSQA 

       550        560        570        580        590        600 
DEEEEDDDFG VEYLLARDEE QSEADAGSGP PTPGPTTLGP KKEITDIAAA AESLQPKGYT 

       610        620        630        640        650        660 
LATTQVKTPI PLLLRGQLRE YQHIGLDWLV TMYEKKLNGI LADEMGLGKT IQTISLLAHL 

       670        680        690        700        710        720 
ACEKGNWGPH LIIVPTSVML NWEMELKRWC PSFKILTYYG AQKERKLKRQ GWTKPNAFHV 

       730        740        750        760        770        780 
CITSYKLVLQ DHQAFRRKNW RYLILDEAQN IKNFKSQRWQ SLLNFNSQRR LLLTGTPLQN 

       790        800        810        820        830        840 
SLMELWSLMH FLMPHVFQSH REFKEWFSNP LTGMIEGSQE YNEGLVKRLH KVLRPFLLRR 

       850        860        870        880        890        900 
VKVDVEKQMP KKYEHVIRCR LSKRQRCLYD DFMAQTTTKE TLATGHFMSV INILMQLRKV 

       910        920        930        940        950        960 
CNHPNLFDPR PVTSPFITPG ICFSTASLVL RATDVHPLQR IDMGRFDLIG LEGRVSRYEA 

       970        980        990       1000       1010       1020 
DTFLPRHRLS RRVLLEVATA PDPPPRPKPV KMKVNRMLQP VPKQEGRTVV VVNNPRAPLG 

      1030       1040       1050       1060       1070       1080 
PVPVRPPPGP ELSAQPTPGP VPQVLPASLM VSASPAGPPL IPASRPPGPV LLPPLQPNSG 

      1090       1100       1110       1120       1130       1140 
SLPQVLPSPL GVLSGTSRPP TPTLSLKPTP PAPVRLSPAP PPGSSSLLKP LTVPPGYTFP 

      1150       1160       1170       1180       1190       1200 
PAAATTTSTT TATATTTAVP APTPAPQRLI LSPDMQARLP SGEVVSIGQL ASLAQRPVAN 

      1210       1220       1230       1240       1250       1260 
AGGSKPLTFQ IQGNKLTLTG AQVRQLAVGQ PRPLQRNVVH LVSAGGQHHL ISQPAHVALI 

      1270       1280       1290       1300       1310       1320 
QAVAPTPGPT PVSVLPSSTP STTPAPTGLS LPLAANQVPP TMVNNTGVVK IVVRQAPRDG 

      1330       1340       1350       1360       1370       1380 
LTPVPPLAPA PRPPSSGLPA VLNPRPTLTP GRLPTPTLGT ARAPMPTPTL VRPLLKLVHS 

      1390       1400       1410       1420       1430       1440 
PSPEVSASAP GAAPLTISSP LHVPSSLPGP ASSPMPIPNS SPLASPVSST VSVPLSSSLP 

      1450       1460       1470       1480       1490       1500 
ISVPTTLPAP ASAPLTIPIS APLTVSASGP ALLTSVTPPL APVVPAAPGP PSLAPSGASP 

      1510       1520       1530       1540       1550       1560 
SASALTLGLA TAPSLSSSQT PGHPLLLAPT SSHVPGLNST VAPACSPVLV PASALASPFP 

      1570       1580       1590       1600       1610       1620 
SAPNPAPAQA SLLAPASSAS QALATPLAPM AAPQTAILAP SPAPPLAPLP VLAPSPGAAP 

      1630       1640       1650       1660       1670       1680 
VLASSQTPVP VMAPSSTPGT SLASASPVPA PTPVLAPSST QTMLPAPVPS PLPSPASTQT 

      1690       1700       1710       1720       1730       1740 
LALAPALAPT LGGSSPSQTL SLGTGNPQGP FPTQTLSLTP ASSLVPTPAQ TLSLAPGPPL 

      1750       1760       1770       1780       1790       1800 
GPTQTLSLAP APPLAPASPV GPAPAHTLTL APASSSASLL APASVQTLTL SPAPVPTLGP 

      1810       1820       1830       1840       1850       1860 
AAAQTLALAP ASTQSPASQA SSLVVSASGA APLPVTMVSR LPVSKDEPDT LTLRSGPPSP 

      1870       1880       1890       1900       1910       1920 
PSTATSFGGP RPRRQPPPPP RSPFYLDSLE EKRKRQRSER LERIFQLSEA HGALAPVYGT 

      1930       1940       1950       1960       1970       1980 
EVLDFCTLPQ PVASPIGPRS PGPSHPTFWT YTEAAHRAVL FPQQRLDQLS EIIERFIFVM 

      1990       2000       2010       2020       2030       2040 
PPVEAPPPSL HACHPPPWLA PRQAAFQEQL ASELWPRARP LHRIVCNMRT QFPDLRLIQY 

      2050       2060       2070       2080       2090       2100 
DCGKLQTLAV LLRQLKAEGH RVLIFTQMTR MLDVLEQFLT YHGHLYLRLD GSTRVEQRQA 

      2110       2120       2130       2140       2150       2160 
LMERFNADKR IFCFILSTRS GGVGVNLTGA DTVVFYDSDW NPTMDAQAQD RCHRIGQTRD 

      2170       2180       2190       2200       2210       2220 
VHIYRLISER TVEENILKKA NQKRMLGDMA IEGGNFTTAY FKQQTIRELF DMPLEEPSSS 

      2230       2240       2250       2260       2270       2280 
SVPSAPEEEE ETVASKQTHI LEQALCRAED EEDIRAATQA KAEQVAELAE FNENDGFPAG 

      2290       2300       2310       2320       2330       2340 
EGEEAGRPGA EDEEMSRAEQ EIAALVEQLT PIERYAMKFL EASLEEVSRE ELKQAEEQVE 

      2350       2360       2370       2380       2390       2400 
AARKDLDQAK EEVFRLPQEE EEGPGAGDES SCGTGGGTHR RSKKAKAPER PGTRVSERLR 

      2410       2420       2430       2440       2450       2460 
GARAETQGAN HTPVISAHQT RSTTTPPRCS PARERVPRPA PRPRPTPASA PAAIPALVPV 

      2470       2480       2490       2500       2510       2520 
PVSAPVPISA PNPITILPVH ILPSPPPPSQ IPPCSSPACT PPPACTPPPA HTPPPAQTCL 

      2530       2540       2550       2560       2570       2580 
VTPSSPLLLG PPSVPISASV TNLPLGLRPE AELCAQALAS PESLELASVA SSETSSLSLV 

      2590       2600       2610       2620       2630       2640 
PPKDLLPVAV EILPVSEKNL SLTPSAPSLT LEAGSIPNGQ EQEAPDSAEG TTLTVLPEGE 

      2650       2660       2670       2680       2690       2700 
ELPLCVSESN GLELPPSAAS DEPLQEPLEA DRTSEELTEA KTPTSSPEKP QELVTAEVAA 

      2710       2720       2730       2740       2750       2760 
PSTSSSATSS PEGPSPARPP RRRTSADVEI RGQGTGRPGQ PPGPKVLRKL PGRLVTVVEE 

      2770       2780       2790       2800       2810       2820 
KELVRRRRQQ RGAASTLVPG VSETSASPGS PSVRSMSGPE SSPPIGGPCE AAPSSSLPTP 

      2830       2840       2850       2860       2870       2880 
PQQPFIARRH IELGVTGGGS PENGDGALLA ITPPAVKRRR GRPPKKNRSP ADAGRGVDEA 

      2890       2900       2910       2920       2930       2940 
PSSTLKGKTN GADPVPGPET LIVADPVLEP QLIPGPQPLG PQPVHRPNPL LSPVEKRRRG 

      2950       2960       2970       2980       2990       3000 
RPPKARDLPI PGTISSAGDG NSESRTQPPP HPSPLTPLPP LLVCPTATVA NTVTTVTIST 

      3010       3020       3030       3040       3050       3060 
SPPKRKRGRP PKNPPSPRPS QLPVLDRDST SVLESCGLGR RRQPQGQGES EGSSSDEDGS 

      3070       3080       3090       3100       3110       3120 
RPLTRLARLR LEAEGMRGRK SGGSMVVAVI QDDLDLADSG PGGLELTPPV VSLTPKLRST 

      3130       3140       3150       3160       3170       3180 
RLRPGSLVPP LETEKLPRKR AGAPVGGSPG LAKRGRLQPP SPLGPEGSVE ESEAEASGEE 

      3190       3200       3210       3220       3230 
EEGDGTPRRR PGPRRLVGTT NQGDQRILRS SAPPSLAGPA VSHRGRKAKT 

« Hide

Isoform 2 [UniParc].

Checksum: B9A0D36717389361
Show »

FASTA3,168337,445
Isoform 3 [UniParc].

Checksum: EA4D60708B59DC5B
Show »

FASTA3,072327,838

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-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]"Mutations in SRCAP, encoding SNF2-related CREBBP activator protein, cause Floating-Harbor syndrome."
Hood R.L., Lines M.A., Nikkel S.M., Schwartzentruber J., Beaulieu C., Nowaczyk M.J., Allanson J., Kim C.A., Wieczorek D., Moilanen J.S., Lacombe D., Gillessen-Kaesbach G., Whiteford M.L., Quaio C.R., Gomy I., Bertola D.R., Albrecht B., Platzer K. expand/collapse author list , McGillivray G., Zou R., McLeod D.R., Chudley A.E., Chodirker B.N., Marcadier J., Majewski J., Bulman D.E., White S.M., Boycott K.M.
Am. J. Hum. Genet. 90:308-313(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN FLHS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_006653.2. NM_006662.2.
UniGeneHs.620916.

3D structure databases

ProteinModelPortalQ6ZRS2.
SMRQ6ZRS2. Positions 611-930, 2023-2209.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116058. 23 interactions.
IntActQ6ZRS2. 14 interactions.
MINTMINT-123408.
STRING9606.ENSP00000262518.

PTM databases

PhosphoSiteQ6ZRS2.

Polymorphism databases

DMDM296452947.

Proteomic databases

PaxDbQ6ZRS2.
PRIDEQ6ZRS2.

Protocols and materials databases

DNASU10847.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262518; ENSP00000262518; ENSG00000080603. [Q6ZRS2-1]
ENST00000344771; ENSP00000343042; ENSG00000080603. [Q6ZRS2-3]
ENST00000380361; ENSP00000369719; ENSG00000080603.
ENST00000395059; ENSP00000378499; ENSG00000080603. [Q6ZRS2-2]
GeneID10847.
KEGGhsa:10847.
UCSCuc002dze.1. human. [Q6ZRS2-1]
uc002dzg.1. human. [Q6ZRS2-2]

Organism-specific databases

CTD10847.
GeneCardsGC16P030710.
H-InvDBHIX0012970.
HGNCHGNC:16974. SRCAP.
HPAHPA028929.
MIM136140. phenotype.
611421. gene.
neXtProtNX_Q6ZRS2.
Orphanet2044. Floating-Harbor syndrome.
PharmGKBPA162404706.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOGENOMHOG000168717.
InParanoidQ6ZRS2.
KOK11661.
OMAPSSTQTM.
OrthoDBEOG79CXXJ.
PhylomeDBQ6ZRS2.
TreeFamTF106424.

Gene expression databases

ArrayExpressQ6ZRS2.
BgeeQ6ZRS2.
CleanExHS_SRCAP.
GenevestigatorQ6ZRS2.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR020478. 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]
PfamPF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
PRINTSPR00929. ATHOOK.
SMARTSM00384. AT_hook. 3 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 4 hits.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51204. HSA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSRCAP. human.
GeneWikiSRCAP.
GenomeRNAi10847.
NextBio41182.
PROQ6ZRS2.
SOURCESearch...

Entry information

Entry nameSRCAP_HUMAN
AccessionPrimary (citable) accession number: Q6ZRS2
Secondary accession number(s): B0JZA6 expand/collapse secondary AC list , O15026, Q7Z744, Q9Y5L9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM