SRCAP_HUMAN
ID SRCAP_HUMAN Reviewed; 3230 AA.
AC Q6ZRS2; B0JZA6; O15026; Q7Z744; Q9Y5L9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Helicase SRCAP;
DE EC=3.6.4.-;
DE AltName: Full=Domino homolog 2;
DE AltName: Full=Snf2-related CBP activator;
GN Name=SRCAP; Synonyms=KIAA0309;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-2427 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-3230 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-3230 (ISOFORM 3).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 128-3230 (ISOFORM 2), INTERACTION WITH
RP CREBBP, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=10347196; DOI=10.1074/jbc.274.23.16370;
RA Johnston H., Kneer J., Chackalaparampil I., Yaciuk P., Chrivia J.;
RT "Identification of a novel SNF2/SWI2 protein family member, SRCAP, which
RT interacts with CREB-binding protein.";
RL J. Biol. Chem. 274:16370-16376(1999).
RN [7]
RP INTERACTION WITH HCV NS5A (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=10702287; DOI=10.1074/jbc.275.10.7184;
RA Ghosh A.K., Majumder M., Steele R., Yaciuk P., Chrivia J., Ray R.,
RA Ray R.B.;
RT "Hepatitis C virus NS5A protein modulates transcription through a novel
RT cellular transcription factor SRCAP.";
RL J. Biol. Chem. 275:7184-7188(2000).
RN [8]
RP FUNCTION.
RX PubMed=11522779; DOI=10.1074/jbc.m103615200;
RA Monroy M.A., Ruhl D.D., Xu X., Granner D.K., Yaciuk P., Chrivia J.C.;
RT "Regulation of cAMP-responsive element-binding protein-mediated
RT transcription by the SNF2/SWI-related protein, SRCAP.";
RL J. Biol. Chem. 276:40721-40726(2001).
RN [9]
RP INTERACTION WITH EP300 AND HADV-2 DBP (MICROBIAL INFECTION).
RX PubMed=11581372; DOI=10.1128/jvi.75.21.10033-10040.2001;
RA Xu X., Chackalaparampil I., Monroy M.A., Cannella M.T., Pesek E.,
RA Chrivia J., Yaciuk P.;
RT "Adenovirus DNA binding protein interacts with the SNF2-related CBP
RT activator protein (SrCap) and inhibits SrCap-mediated transcription.";
RL J. Virol. 75:10033-10040(2001).
RN [10]
RP FUNCTION, AND IDENTIFICATION IN COMPLEX WITH CREBBP; CARM1 AND GRIP1.
RX PubMed=14500758; DOI=10.1210/me.2003-0208;
RA Monroy M.A., Schott N.M., Cox L., Chen J.D., Ruh M., Chrivia J.C.;
RT "SNF2-related CBP activator protein (SRCAP) functions as a coactivator of
RT steroid receptor-mediated transcription through synergistic interactions
RT with CARM-1 and GRIP-1.";
RL Mol. Endocrinol. 17:2519-2528(2003).
RN [11]
RP IDENTIFICATION IN A NUA4-RELATED COMPLEX.
RX PubMed=14966270; DOI=10.1128/mcb.24.5.1884-1896.2004;
RA Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
RT "Structural and functional conservation of the NuA4 histone
RT acetyltransferase complex from yeast to humans.";
RL Mol. Cell. Biol. 24:1884-1896(2004).
RN [12]
RP IDENTIFICATION IN THE SRCAP COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15647280; DOI=10.1074/jbc.m500001200;
RA Cai Y., Jin J., Florens L., Swanson S.K., Kusch T., Li B., Workman J.L.,
RA Washburn M.P., Conaway R.C., Conaway J.W.;
RT "The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone
RT acetyltransferase and SRCAP complexes.";
RL J. Biol. Chem. 280:13665-13670(2005).
RN [13]
RP FUNCTION.
RX PubMed=16024792; DOI=10.1128/mcb.25.15.6559-6569.2005;
RA Eissenberg J.C., Wong M., Chrivia J.C.;
RT "Human SRCAP and Drosophila melanogaster DOM are homologs that function in
RT the notch signaling pathway.";
RL Mol. Cell. Biol. 25:6559-6569(2005).
RN [14]
RP IDENTIFICATION IN THE SRCAP COMPLEX, FUNCTION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16634648; DOI=10.1021/bi060043d;
RA Ruhl D.D., Jin J., Cai Y., Swanson S., Florens L., Washburn M.P.,
RA Conaway R.C., Conaway J.W., Chrivia J.C.;
RT "Purification of a human SRCAP complex that remodels chromatin by
RT incorporating the histone variant H2A.Z into nucleosomes.";
RL Biochemistry 45:5671-5677(2006).
RN [15]
RP FUNCTION.
RX PubMed=17617668; DOI=10.1074/jbc.m703418200;
RA Wong M.M., Cox L.K., Chrivia J.C.;
RT "The chromatin remodeling protein, SRCAP, is critical for deposition of the
RT histone variant H2A.Z at promoters.";
RL J. Biol. Chem. 282:26132-26139(2007).
RN [16]
RP INVOLVEMENT IN FLHS, AND VARIANTS FLHS 2435-ARG--THR-3230 DEL AND
RP 2444-ARG--THR-3230 DEL.
RX PubMed=22265015; DOI=10.1016/j.ajhg.2011.12.001;
RA Hood R.L., Lines M.A., Nikkel S.M., Schwartzentruber J., Beaulieu C.,
RA Nowaczyk M.J., Allanson J., Kim C.A., Wieczorek D., Moilanen J.S.,
RA Lacombe D., Gillessen-Kaesbach G., Whiteford M.L., Quaio C.R., Gomy I.,
RA Bertola D.R., Albrecht B., Platzer K., McGillivray G., Zou R., McLeod D.R.,
RA Chudley A.E., Chodirker B.N., Marcadier J., Majewski J., Bulman D.E.,
RA White S.M., Boycott K.M.;
RT "Mutations in SRCAP, encoding SNF2-related CREBBP activator protein, cause
RT Floating-Harbor syndrome.";
RL Am. J. Hum. Genet. 90:308-313(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1172, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP VARIANTS DEHMBA 392-GLN--THR-3230 DEL; 840-ARG--THR-3230 DEL;
RP 1278-SER--THR-3230 DEL; 1642-LEU--THR-3230 DEL AND 2070-ARG--THR-3230 DEL,
RP AND INVOLVEMENT IN DEHMBA.
RX PubMed=33909990; DOI=10.1016/j.ajhg.2021.04.008;
RA Rots D., Chater-Diehl E., Dingemans A.J.M., Goodman S.J., Siu M.T.,
RA Cytrynbaum C., Choufani S., Hoang N., Walker S., Awamleh Z., Charkow J.,
RA Meyn S., Pfundt R., Rinne T., Gardeitchik T., de Vries B.B.A., Deden A.C.,
RA Leenders E., Kwint M., Stumpel C.T.R.M., Stevens S.J.C., Vermeulen J.R.,
RA van Harssel J.V.T., Bosch D.G.M., van Gassen K.L.I., van Binsbergen E.,
RA de Geus C.M., Brackel H., Hempel M., Lessel D., Denecke J., Slavotinek A.,
RA Strober J., Crunk A., Folk L., Wentzensen I.M., Yang H., Zou F., Millan F.,
RA Person R., Xie Y., Liu S., Ousager L.B., Larsen M., Schultz-Rogers L.,
RA Morava E., Klee E.W., Berry I.R., Campbell J., Lindstrom K., Pruniski B.,
RA Neumeyer A.M., Radley J.A., Phornphutkul C., Schmidt B., Wilson W.G.,
RA Ounap K., Reinson K., Pajusalu S., van Haeringen A., Ruivenkamp C.,
RA Cuperus R., Santos-Simarro F., Palomares-Bralo M., Pacio-Miguez M.,
RA Ritter A., Bhoj E., Toenne E., Tveten K., Cappuccio G., Brunetti-Pierri N.,
RA Rowe L., Bunn J., Saenz M., Platzer K., Mertens M., Caluseriu O.,
RA Nowaczyk M.J.M., Cohn R.D., Kannu P., Alkhunaizi E., Chitayat D.,
RA Scherer S.W., Brunner H.G., Vissers L.E.L.M., Kleefstra T., Koolen D.A.,
RA Weksberg R.;
RT "Truncating SRCAP variants outside the Floating-Harbor syndrome locus cause
RT a distinct neurodevelopmental disorder with a specific DNA methylation
RT signature.";
RL Am. J. Hum. Genet. 108:1053-1068(2021).
CC -!- FUNCTION: Catalytic component of the SRCAP complex which mediates the
CC ATP-dependent exchange of histone H2AZ/H2B dimers for nucleosomal
CC H2A/H2B, leading to transcriptional regulation of selected genes by
CC chromatin remodeling. Acts as a coactivator for CREB-mediated
CC transcription, steroid receptor-mediated transcription, and Notch-
CC mediated transcription. {ECO:0000269|PubMed:10347196,
CC ECO:0000269|PubMed:11522779, ECO:0000269|PubMed:14500758,
CC ECO:0000269|PubMed:16024792, ECO:0000269|PubMed:16634648,
CC ECO:0000269|PubMed:17617668}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=66 uM for ATP {ECO:0000269|PubMed:10347196};
CC -!- SUBUNIT: Interacts with CREBBP and EP300. May be part of a complex
CC containing SRCAP, CREBBP, CARM1 and GRIP1. Component of the chromatin-
CC remodeling SRCAP complex composed of at least SRCAP, DMAP1, RUVBL1,
CC RUVBL2, ACTL6A, YEATS4, VPS72, ACTR6 and ZNHIT1. Component of a NuA4-
CC related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP,
CC EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72
CC and YEATS4/GAS41. {ECO:0000269|PubMed:10347196,
CC ECO:0000269|PubMed:11581372, ECO:0000269|PubMed:14500758,
CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:15647280,
CC ECO:0000269|PubMed:16634648}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis C virus (HCV)
CC NS5A. {ECO:0000269|PubMed:10702287}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus 2 DBP.
CC {ECO:0000269|PubMed:11581372}.
CC -!- INTERACTION:
CC Q6ZRS2-3; X5D778: ANKRD11; NbExp=3; IntAct=EBI-12029182, EBI-17183751;
CC Q6ZRS2-3; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-12029182, EBI-11519926;
CC Q6ZRS2-3; P24863: CCNC; NbExp=3; IntAct=EBI-12029182, EBI-395261;
CC Q6ZRS2-3; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-12029182, EBI-739624;
CC Q6ZRS2-3; Q9H944: MED20; NbExp=3; IntAct=EBI-12029182, EBI-394644;
CC Q6ZRS2-3; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-12029182, EBI-2548751;
CC Q6ZRS2-3; P26045: PTPN3; NbExp=3; IntAct=EBI-12029182, EBI-1047946;
CC Q6ZRS2-3; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-12029182, EBI-748621;
CC Q6ZRS2-3; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-12029182, EBI-2130429;
CC Q6ZRS2-3; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-12029182, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549,
CC ECO:0000269|PubMed:10702287}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6ZRS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZRS2-2; Sequence=VSP_029442;
CC Name=3;
CC IsoId=Q6ZRS2-3; Sequence=VSP_029441, VSP_029442;
CC -!- DISEASE: Floating-Harbor syndrome (FLHS) [MIM:136140]: A rare genetic
CC disorder characterized by proportionate short stature, delayed bone
CC age, delayed speech development, and typical facial features. The face
CC is triangular with deep-set eyes, long eyelashes, bulbous nose, wide
CC columella, short philtrum, and thin lips.
CC {ECO:0000269|PubMed:22265015}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Developmental delay, hypotonia, musculoskeletal defects, and
CC behavioral abnormalities (DEHMBA) [MIM:619595]: An autosomal dominant
CC disorder characterized by developmental delay, speech delay, mild to
CC severe intellectual disability, hypotonia, musculoskeletal features,
CC and behavioral abnormalities including autistic features. Skeletal
CC anomalies include joint hypermobility, chronic musculoskeletal pain,
CC scoliosis, and pectus defects. Affected individuals also have non-
CC specific and variable dysmorphic facial features.
CC {ECO:0000269|PubMed:33909990}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI59100.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC093249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK128030; BAC87237.1; -; mRNA.
DR EMBL; AB002307; BAA20768.2; -; mRNA.
DR EMBL; BC159099; AAI59100.1; ALT_INIT; mRNA.
DR EMBL; AF143946; AAD39760.1; -; mRNA.
DR CCDS; CCDS10689.2; -. [Q6ZRS2-1]
DR RefSeq; NP_006653.2; NM_006662.2. [Q6ZRS2-1]
DR PDB; 6IGM; EM; 4.00 A; H=1-3230.
DR PDBsum; 6IGM; -.
DR SMR; Q6ZRS2; -.
DR BioGRID; 116058; 111.
DR ComplexPortal; CPX-974; SRCAP chromatin remodeling complex.
DR CORUM; Q6ZRS2; -.
DR DIP; DIP-45191N; -.
DR IntAct; Q6ZRS2; 62.
DR MINT; Q6ZRS2; -.
DR STRING; 9606.ENSP00000262518; -.
DR GlyGen; Q6ZRS2; 12 sites, 2 O-linked glycans (12 sites).
DR iPTMnet; Q6ZRS2; -.
DR PhosphoSitePlus; Q6ZRS2; -.
DR BioMuta; SRCAP; -.
DR DMDM; 296452947; -.
DR EPD; Q6ZRS2; -.
DR jPOST; Q6ZRS2; -.
DR MassIVE; Q6ZRS2; -.
DR MaxQB; Q6ZRS2; -.
DR PaxDb; Q6ZRS2; -.
DR PeptideAtlas; Q6ZRS2; -.
DR PRIDE; Q6ZRS2; -.
DR ProteomicsDB; 68161; -. [Q6ZRS2-1]
DR ProteomicsDB; 68162; -. [Q6ZRS2-2]
DR ProteomicsDB; 68163; -. [Q6ZRS2-3]
DR Antibodypedia; 27413; 84 antibodies from 22 providers.
DR DNASU; 10847; -.
DR Ensembl; ENST00000262518.9; ENSP00000262518.4; ENSG00000080603.17. [Q6ZRS2-1]
DR GeneID; 10847; -.
DR KEGG; hsa:10847; -.
DR MANE-Select; ENST00000262518.9; ENSP00000262518.4; NM_006662.3; NP_006653.2.
DR UCSC; uc002dze.2; human. [Q6ZRS2-1]
DR CTD; 10847; -.
DR DisGeNET; 10847; -.
DR GeneCards; SRCAP; -.
DR GeneReviews; SRCAP; -.
DR HGNC; HGNC:16974; SRCAP.
DR HPA; ENSG00000080603; Low tissue specificity.
DR MalaCards; SRCAP; -.
DR MIM; 136140; phenotype.
DR MIM; 611421; gene.
DR MIM; 619595; phenotype.
DR neXtProt; NX_Q6ZRS2; -.
DR OpenTargets; ENSG00000080603; -.
DR Orphanet; 2044; Floating-Harbor syndrome.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA162404706; -.
DR VEuPathDB; HostDB:ENSG00000080603; -.
DR eggNOG; KOG0391; Eukaryota.
DR GeneTree; ENSGT00940000157457; -.
DR HOGENOM; CLU_000315_12_2_1; -.
DR InParanoid; Q6ZRS2; -.
DR OMA; FWTFTEA; -.
DR OrthoDB; 188211at2759; -.
DR PhylomeDB; Q6ZRS2; -.
DR TreeFam; TF106424; -.
DR PathwayCommons; Q6ZRS2; -.
DR SABIO-RK; Q6ZRS2; -.
DR SignaLink; Q6ZRS2; -.
DR SIGNOR; Q6ZRS2; -.
DR BioGRID-ORCS; 10847; 705 hits in 1106 CRISPR screens.
DR ChiTaRS; SRCAP; human.
DR GeneWiki; SRCAP; -.
DR GenomeRNAi; 10847; -.
DR Pharos; Q6ZRS2; Tbio.
DR PRO; PR:Q6ZRS2; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6ZRS2; protein.
DR Bgee; ENSG00000080603; Expressed in sural nerve and 95 other tissues.
DR ExpressionAtlas; Q6ZRS2; baseline and differential.
DR Genevisible; Q6ZRS2; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0004402; F:histone acetyltransferase activity; TAS:ProtInc.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00929; ATHOOK.
DR SMART; SM00384; AT_hook; 3.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SUPFAM; SSF52540; SSF52540; 3.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; ATP-binding;
KW Chromatin regulator; Disease variant; DNA-binding; Helicase;
KW Host-virus interaction; Hydrolase; Intellectual disability;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..3230
FT /note="Helicase SRCAP"
FT /id="PRO_0000311236"
FT DOMAIN 124..196
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 630..795
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 2044..2197
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DNA_BIND 2857..2869
FT /note="A.T hook 1"
FT DNA_BIND 2936..2948
FT /note="A.T hook 2"
FT DNA_BIND 3004..3016
FT /note="A.T hook 3"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1629..1760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1839..1893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2214..2233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2271..2298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2327..2453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2564..2583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2598..3081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3095..3230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..310
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..421
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..487
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..547
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1043
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1076
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1421
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2327..2362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2409..2429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2565..2579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2598..2629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2679..2712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2754..2769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2775..2799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2911..2928
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2931..2945
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2967..2981
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2987..3002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3054..3077
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 643..650
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 1172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1085..1181
FT /note="VLPSPLGVLSGTSRPPTPTLSLKPTPPAPVRLSPAPPPGSSSLLKPLTVPPG
FT YTFPPAAATTTSTTTATATTTAVPAPTPAPQRLILSPDMQARLPS -> A (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9205841"
FT /id="VSP_029441"
FT VAR_SEQ 1236..1298
FT /note="RNVVHLVSAGGQHHLISQPAHVALIQAVAPTPGPTPVSVLPSSTPSTTPAPT
FT GLSLPLAANQV -> M (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10347196,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9205841"
FT /id="VSP_029442"
FT VARIANT 392..3230
FT /note="Missing (in DEHMBA)"
FT /evidence="ECO:0000269|PubMed:33909990"
FT /id="VAR_086403"
FT VARIANT 840..3230
FT /note="Missing (in DEHMBA)"
FT /evidence="ECO:0000269|PubMed:33909990"
FT /id="VAR_086404"
FT VARIANT 1278..3230
FT /note="Missing (in DEHMBA)"
FT /evidence="ECO:0000269|PubMed:33909990"
FT /id="VAR_086405"
FT VARIANT 1642..3230
FT /note="Missing (in DEHMBA)"
FT /evidence="ECO:0000269|PubMed:33909990"
FT /id="VAR_086406"
FT VARIANT 2070..3230
FT /note="Missing (in DEHMBA)"
FT /evidence="ECO:0000269|PubMed:33909990"
FT /id="VAR_086407"
FT VARIANT 2435..3230
FT /note="Missing (in FLHS)"
FT /evidence="ECO:0000269|PubMed:22265015"
FT /id="VAR_086408"
FT VARIANT 2444..3230
FT /note="Missing (in FLHS)"
FT /evidence="ECO:0000269|PubMed:22265015"
FT /id="VAR_086409"
FT CONFLICT 1147
FT /note="T -> A (in Ref. 2; BAC87237)"
FT /evidence="ECO:0000305"
FT CONFLICT 1494
FT /note="A -> Q (in Ref. 6; AAD39760)"
FT /evidence="ECO:0000305"
FT CONFLICT 2765
FT /note="R -> Q (in Ref. 6; AAD39760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3230 AA; 343555 MW; 3CFB74C7BDFBEAD0 CRC64;
MQSSPSPAHP QLPVLQTQMV SDGMTGSNPV SPASSSSPAS SGAGGISPQH IAQDSSLDGP
PGPPDGATVP LEGFSLSQAA DLANKGPKWE KSHAEIAEQA KHEAEIETRI AELRKEGFWS
LKRLPKVPEP PRPKGHWDYL CEEMQWLSAD FAQERRWKRG VARKVVRMVI RHHEEQRQKE
ERARREEQAK LRRIASTMAK DVRQFWSNVE KVVQFKQQSR LEEKRKKALD LHLDFIVGQT
EKYSDLLSQS LNQPLTSSKA GSSPCLGSSS AASSPPPPAS RLDDEDGDFQ PQEDEEEDDE
ETIEVEEQQE GNDAEAQRRE IELLRREGEL PLEELLRSLP PQLLEGPSSP SQTPSSHDSD
TRDGPEEGAE EEPPQVLEIK PPPSAVTQRN KQPWHPDEDD EEFTANEEEA EDEEDTIAAE
EQLEGEVDHA MELSELAREG ELSMEELLQQ YAGAYAPGSG SSEDEDEDEV DANSSDCEPE
GPVEAEEPPQ EDSSSQSDSV EDRSEDEEDE HSEEEETSGS SASEESESEE SEDAQSQSQA
DEEEEDDDFG VEYLLARDEE QSEADAGSGP PTPGPTTLGP KKEITDIAAA AESLQPKGYT
LATTQVKTPI PLLLRGQLRE YQHIGLDWLV TMYEKKLNGI LADEMGLGKT IQTISLLAHL
ACEKGNWGPH LIIVPTSVML NWEMELKRWC PSFKILTYYG AQKERKLKRQ GWTKPNAFHV
CITSYKLVLQ DHQAFRRKNW RYLILDEAQN IKNFKSQRWQ SLLNFNSQRR LLLTGTPLQN
SLMELWSLMH FLMPHVFQSH REFKEWFSNP LTGMIEGSQE YNEGLVKRLH KVLRPFLLRR
VKVDVEKQMP KKYEHVIRCR LSKRQRCLYD DFMAQTTTKE TLATGHFMSV INILMQLRKV
CNHPNLFDPR PVTSPFITPG ICFSTASLVL RATDVHPLQR IDMGRFDLIG LEGRVSRYEA
DTFLPRHRLS RRVLLEVATA PDPPPRPKPV KMKVNRMLQP VPKQEGRTVV VVNNPRAPLG
PVPVRPPPGP ELSAQPTPGP VPQVLPASLM VSASPAGPPL IPASRPPGPV LLPPLQPNSG
SLPQVLPSPL GVLSGTSRPP TPTLSLKPTP PAPVRLSPAP PPGSSSLLKP LTVPPGYTFP
PAAATTTSTT TATATTTAVP APTPAPQRLI LSPDMQARLP SGEVVSIGQL ASLAQRPVAN
AGGSKPLTFQ IQGNKLTLTG AQVRQLAVGQ PRPLQRNVVH LVSAGGQHHL ISQPAHVALI
QAVAPTPGPT PVSVLPSSTP STTPAPTGLS LPLAANQVPP TMVNNTGVVK IVVRQAPRDG
LTPVPPLAPA PRPPSSGLPA VLNPRPTLTP GRLPTPTLGT ARAPMPTPTL VRPLLKLVHS
PSPEVSASAP GAAPLTISSP LHVPSSLPGP ASSPMPIPNS SPLASPVSST VSVPLSSSLP
ISVPTTLPAP ASAPLTIPIS APLTVSASGP ALLTSVTPPL APVVPAAPGP PSLAPSGASP
SASALTLGLA TAPSLSSSQT PGHPLLLAPT SSHVPGLNST VAPACSPVLV PASALASPFP
SAPNPAPAQA SLLAPASSAS QALATPLAPM AAPQTAILAP SPAPPLAPLP VLAPSPGAAP
VLASSQTPVP VMAPSSTPGT SLASASPVPA PTPVLAPSST QTMLPAPVPS PLPSPASTQT
LALAPALAPT LGGSSPSQTL SLGTGNPQGP FPTQTLSLTP ASSLVPTPAQ TLSLAPGPPL
GPTQTLSLAP APPLAPASPV GPAPAHTLTL APASSSASLL APASVQTLTL SPAPVPTLGP
AAAQTLALAP ASTQSPASQA SSLVVSASGA APLPVTMVSR LPVSKDEPDT LTLRSGPPSP
PSTATSFGGP RPRRQPPPPP RSPFYLDSLE EKRKRQRSER LERIFQLSEA HGALAPVYGT
EVLDFCTLPQ PVASPIGPRS PGPSHPTFWT YTEAAHRAVL FPQQRLDQLS EIIERFIFVM
PPVEAPPPSL HACHPPPWLA PRQAAFQEQL ASELWPRARP LHRIVCNMRT QFPDLRLIQY
DCGKLQTLAV LLRQLKAEGH RVLIFTQMTR MLDVLEQFLT YHGHLYLRLD GSTRVEQRQA
LMERFNADKR IFCFILSTRS GGVGVNLTGA DTVVFYDSDW NPTMDAQAQD RCHRIGQTRD
VHIYRLISER TVEENILKKA NQKRMLGDMA IEGGNFTTAY FKQQTIRELF DMPLEEPSSS
SVPSAPEEEE ETVASKQTHI LEQALCRAED EEDIRAATQA KAEQVAELAE FNENDGFPAG
EGEEAGRPGA EDEEMSRAEQ EIAALVEQLT PIERYAMKFL EASLEEVSRE ELKQAEEQVE
AARKDLDQAK EEVFRLPQEE EEGPGAGDES SCGTGGGTHR RSKKAKAPER PGTRVSERLR
GARAETQGAN HTPVISAHQT RSTTTPPRCS PARERVPRPA PRPRPTPASA PAAIPALVPV
PVSAPVPISA PNPITILPVH ILPSPPPPSQ IPPCSSPACT PPPACTPPPA HTPPPAQTCL
VTPSSPLLLG PPSVPISASV TNLPLGLRPE AELCAQALAS PESLELASVA SSETSSLSLV
PPKDLLPVAV EILPVSEKNL SLTPSAPSLT LEAGSIPNGQ EQEAPDSAEG TTLTVLPEGE
ELPLCVSESN GLELPPSAAS DEPLQEPLEA DRTSEELTEA KTPTSSPEKP QELVTAEVAA
PSTSSSATSS PEGPSPARPP RRRTSADVEI RGQGTGRPGQ PPGPKVLRKL PGRLVTVVEE
KELVRRRRQQ RGAASTLVPG VSETSASPGS PSVRSMSGPE SSPPIGGPCE AAPSSSLPTP
PQQPFIARRH IELGVTGGGS PENGDGALLA ITPPAVKRRR GRPPKKNRSP ADAGRGVDEA
PSSTLKGKTN GADPVPGPET LIVADPVLEP QLIPGPQPLG PQPVHRPNPL LSPVEKRRRG
RPPKARDLPI PGTISSAGDG NSESRTQPPP HPSPLTPLPP LLVCPTATVA NTVTTVTIST
SPPKRKRGRP PKNPPSPRPS QLPVLDRDST SVLESCGLGR RRQPQGQGES EGSSSDEDGS
RPLTRLARLR LEAEGMRGRK SGGSMVVAVI QDDLDLADSG PGGLELTPPV VSLTPKLRST
RLRPGSLVPP LETEKLPRKR AGAPVGGSPG LAKRGRLQPP SPLGPEGSVE ESEAEASGEE
EEGDGTPRRR PGPRRLVGTT NQGDQRILRS SAPPSLAGPA VSHRGRKAKT
