Q6ZRS2 (SRCAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 75.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Helicase SRCAP EC=3.6.4.- Alternative name(s): Domino homolog 2 Snf2-related CBP activator | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 3230 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 |
| Subcellular location | |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 |
| 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. |
Ontologies
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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 3230 | 3230 | Helicase SRCAP | PRO_0000311236 | |||||
Regions | |||||||||
| Domain | 124 – 196 | 73 | HSA | ||||||
| Domain | 630 – 795 | 166 | Helicase ATP-binding | ||||||
| Domain | 2044 – 2197 | 154 | Helicase C-terminal | ||||||
| Nucleotide binding | 643 – 650 | 8 | ATP By similarity | ||||||
| DNA binding | 2857 – 2869 | 13 | A.T hook 1 | ||||||
| DNA binding | 2936 – 2948 | 13 | A.T hook 2 | ||||||
| DNA binding | 3004 – 3016 | 13 | A.T hook 3 | ||||||
| Compositional bias | 275 – 278 | 4 | Poly-Pro | ||||||
| Compositional bias | 293 – 563 | 271 | Glu-rich | ||||||
| Compositional bias | 981 – 1883 | 903 | Pro-rich | ||||||
| Compositional bias | 2227 – 2362 | 136 | Glu-rich | ||||||
| Compositional bias | 2426 – 3023 | 598 | Pro-rich | ||||||
| Compositional bias | 3179 – 3182 | 4 | Poly-Glu | ||||||
Amino acid modifications | |||||||||
| Modified residue | 248 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 258 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 274 | 1 | Phosphoserine Ref.20 | ||||||
| Modified residue | 562 | 1 | Phosphoserine Ref.20 | ||||||
| Modified residue | 568 | 1 | Phosphoserine Ref.20 | ||||||
| Modified residue | 572 | 1 | Phosphothreonine Ref.20 | ||||||
| Modified residue | 2258 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 2425 | 1 | Phosphothreonine Ref.18 | ||||||
| Modified residue | 2430 | 1 | Phosphoserine Ref.18 | ||||||
| Modified residue | 2787 | 1 | Phosphoserine Ref.19 Ref.20 | ||||||
| Modified residue | 2790 | 1 | Phosphoserine Ref.19 Ref.20 | ||||||
| Modified residue | 2869 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 3148 | 1 | Phosphoserine Ref.15 Ref.19 Ref.20 | ||||||
| Modified residue | 3161 | 1 | Phosphoserine Ref.20 | ||||||
| Modified residue | 3168 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 3172 | 1 | Phosphoserine Ref.20 | ||||||
| Modified residue | 3177 | 1 | Phosphoserine Ref.19 Ref.20 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1085 – 1181 | 97 | VLPSP…ARLPS → A in isoform 3. | VSP_029441 | |||||
| Alternative sequence | 1236 – 1298 | 63 | RNVVH…AANQV → M in isoform 2 and isoform 3. | VSP_029442 | |||||
Experimental info | |||||||||
| Sequence conflict | 1147 | 1 | T → A in BAC87237. Ref.2 | ||||||
| Sequence conflict | 1494 | 1 | A → Q in AAD39760. Ref.6 | ||||||
| Sequence conflict | 2765 | 1 | R → Q in AAD39760. Ref.6 | ||||||
Sequences
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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. Pennacchio L.A.Nature 432:988-994(2004) [PubMed: 15616553] [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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [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: 9205841] [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: 15489334] [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: 10347196] [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: 10702287] [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: 11522779] [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: 11581372] [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: 14500758] [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: 14966270] [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: 15647280] [Abstract] Cited for: IDENTIFICATION IN THE SRCAP COMPLEX, 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: 16024792] [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: 16634648] [Abstract] Cited for: IDENTIFICATION IN THE SRCAP COMPLEX, FUNCTION, 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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2869 AND SER-3148, MASS SPECTROMETRY. 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: 17617668] [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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248 AND THR-2258, MASS SPECTROMETRY. 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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2425 AND SER-2430, MASS SPECTROMETRY. 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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-2787; SER-2790; SER-3148; SER-3168 AND SER-3177, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-562; SER-568; THR-572; SER-2787; SER-2790; SER-3148; SER-3161; SER-3172 AND SER-3177, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| + | 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. |
| IPI | IPI00009101. IPI00444046. IPI00550342. |
| RefSeq | NP_006653.2. NM_006662.2. |
| UniGene | Hs.647334. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1Z63 based on UniProtKB Q97XQ5. |
| ProteinModelPortal | Q6ZRS2. |
| SMR | Q6ZRS2. Positions 611-910. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q6ZRS2. 12 interactions. |
| MINT | MINT-123408. |
| STRING | Q6ZRS2. |
PTM databases | |
| PhosphoSite | Q6ZRS2. |
Polymorphism databases | |
| DMDM | 296452947. |
Proteomic databases | |
| PRIDE | Q6ZRS2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000262518; ENSP00000262518; ENSG00000080603. ENST00000344771; ENSP00000343042; ENSG00000080603. ENST00000380361; ENSP00000369719; ENSG00000080603. |
| GeneID | 10847. |
| KEGG | hsa:10847. |
| UCSC | uc002dze.1. human. uc002dzg.1. human. |
Organism-specific databases | |
| CTD | 10847. |
| GeneCards | GC16P030710. |
| H-InvDB | HIX0012970. |
| HGNC | HGNC:16974. SRCAP. |
| HPA | HPA028929. |
| MIM | 611421. gene. |
| neXtProt | NX_Q6ZRS2. |
| PharmGKB | PA162404706. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| GeneTree | ENSGT00530000063427. |
| HOGENOM | HBG281654. |
| InParanoid | Q6ZRS2. |
| OMA | GSHRRSK. |
| OrthoDB | EOG4B2SWB. |
| PhylomeDB | Q6ZRS2. |
Gene expression databases | |
| ArrayExpress | Q6ZRS2. |
| Bgee | Q6ZRS2. |
| CleanEx | HS_SRCAP. |
| Genevestigator | Q6ZRS2. |
Family and domain databases | |
| InterPro | IPR020478. AT_hook-like. IPR017956. AT_hook_DNA-bd_motif. IPR014001. DEAD-like_helicase. IPR014012. Helicase/SANT-assoc_DNA-bd. IPR001650. Helicase_C. IPR006562. HSA. IPR000330. SNF2_N. [Graphical view] |
| KO | K11661. |
| Pfam | PF00271. Helicase_C. 1 hit. PF07529. HSA. 1 hit. PF00176. SNF2_N. 1 hit. [Graphical view] |
| PRINTS | PR00929. ATHOOK. |
| SMART | SM00384. AT_hook. 3 hits. SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view] |
| PROSITE | PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS51204. HSA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 41182. |
| SOURCE | Search... |
Entry information
| Entry name | SRCAP_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q6ZRS2 Secondary accession number(s): B0JZA6 Q9Y5L9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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
| Human chromosome 16 Human chromosome 16: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with