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GPTC2_HUMAN
ID   GPTC2_HUMAN             Reviewed;         528 AA.
AC   Q9NW75; Q5VYK7; Q5VYK8; Q86YE7;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=G patch domain-containing protein 2;
GN   Name=GPATCH2; Synonyms=GPATC2;
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 MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Lung, and Uterus;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   FUNCTION, INTERACTION WITH DHX15, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=19432882; DOI=10.1111/j.1349-7006.2009.01185.x;
RA   Lin M.L., Fukukawa C., Park J.H., Naito K., Kijima K., Shimo A., Ajiro M.,
RA   Nishidate T., Nakamura Y., Katagiri T.;
RT   "Involvement of G-patch domain containing 2 overexpression in breast
RT   carcinogenesis.";
RL   Cancer Sci. 100:1443-1450(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115 AND SER-195, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115 AND SER-117, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115 AND SER-117, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 AND SER-195, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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).
CC   -!- FUNCTION: Enhances the ATPase activity of DHX15 in vitro.
CC       {ECO:0000269|PubMed:19432882}.
CC   -!- SUBUNIT: Interacts with DHX15. {ECO:0000269|PubMed:19432882}.
CC   -!- INTERACTION:
CC       Q9NW75-2; P68400: CSNK2A1; NbExp=3; IntAct=EBI-12068108, EBI-347804;
CC       Q9NW75-2; Q9C005: DPY30; NbExp=3; IntAct=EBI-12068108, EBI-744973;
CC       Q9NW75-2; O15481: MAGEB4; NbExp=3; IntAct=EBI-12068108, EBI-751857;
CC       Q9NW75-2; Q9NRD5: PICK1; NbExp=4; IntAct=EBI-12068108, EBI-79165;
CC       Q9NW75-2; Q99598: TSNAX; NbExp=3; IntAct=EBI-12068108, EBI-742638;
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:19432882}.
CC       Nucleus, nucleolus {ECO:0000269|PubMed:19432882}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NW75-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NW75-2; Sequence=VSP_010527, VSP_010528;
CC   -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:19432882}.
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DR   EMBL; AK001114; BAA91509.1; -; mRNA.
DR   EMBL; AC096641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL354659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471100; EAW93333.1; -; Genomic_DNA.
DR   EMBL; BC042193; AAH42193.1; -; mRNA.
DR   EMBL; BC063474; AAH63474.1; -; mRNA.
DR   CCDS; CCDS1518.1; -. [Q9NW75-1]
DR   CCDS; CCDS73031.1; -. [Q9NW75-2]
DR   RefSeq; NP_001284683.1; NM_001297754.2. [Q9NW75-2]
DR   RefSeq; NP_060510.1; NM_018040.4. [Q9NW75-1]
DR   AlphaFoldDB; Q9NW75; -.
DR   BioGRID; 120415; 23.
DR   IntAct; Q9NW75; 10.
DR   STRING; 9606.ENSP00000355902; -.
DR   iPTMnet; Q9NW75; -.
DR   PhosphoSitePlus; Q9NW75; -.
DR   BioMuta; GPATCH2; -.
DR   DMDM; 48428171; -.
DR   EPD; Q9NW75; -.
DR   jPOST; Q9NW75; -.
DR   MassIVE; Q9NW75; -.
DR   MaxQB; Q9NW75; -.
DR   PaxDb; Q9NW75; -.
DR   PeptideAtlas; Q9NW75; -.
DR   PRIDE; Q9NW75; -.
DR   ProteomicsDB; 82908; -. [Q9NW75-1]
DR   ProteomicsDB; 82909; -. [Q9NW75-2]
DR   Antibodypedia; 20729; 55 antibodies from 13 providers.
DR   DNASU; 55105; -.
DR   Ensembl; ENST00000366934.3; ENSP00000355901.3; ENSG00000092978.11. [Q9NW75-2]
DR   Ensembl; ENST00000366935.8; ENSP00000355902.3; ENSG00000092978.11. [Q9NW75-1]
DR   GeneID; 55105; -.
DR   KEGG; hsa:55105; -.
DR   MANE-Select; ENST00000366935.8; ENSP00000355902.3; NM_018040.5; NP_060510.1.
DR   UCSC; uc001hlf.2; human. [Q9NW75-1]
DR   CTD; 55105; -.
DR   DisGeNET; 55105; -.
DR   GeneCards; GPATCH2; -.
DR   HGNC; HGNC:25499; GPATCH2.
DR   HPA; ENSG00000092978; Low tissue specificity.
DR   neXtProt; NX_Q9NW75; -.
DR   OpenTargets; ENSG00000092978; -.
DR   PharmGKB; PA162390064; -.
DR   VEuPathDB; HostDB:ENSG00000092978; -.
DR   eggNOG; KOG0154; Eukaryota.
DR   GeneTree; ENSGT00410000025698; -.
DR   HOGENOM; CLU_041240_2_0_1; -.
DR   InParanoid; Q9NW75; -.
DR   OMA; DQEMDNN; -.
DR   OrthoDB; 606839at2759; -.
DR   PhylomeDB; Q9NW75; -.
DR   TreeFam; TF331954; -.
DR   PathwayCommons; Q9NW75; -.
DR   SignaLink; Q9NW75; -.
DR   BioGRID-ORCS; 55105; 12 hits in 1079 CRISPR screens.
DR   ChiTaRS; GPATCH2; human.
DR   GenomeRNAi; 55105; -.
DR   Pharos; Q9NW75; Tdark.
DR   PRO; PR:Q9NW75; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9NW75; protein.
DR   Bgee; ENSG00000092978; Expressed in buccal mucosa cell and 154 other tissues.
DR   Genevisible; Q9NW75; HS.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR026291; Gpatch2.
DR   PANTHER; PTHR14195:SF4; PTHR14195:SF4; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   SMART; SM00443; G_patch; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..528
FT                   /note="G patch domain-containing protein 2"
FT                   /id="PRO_0000087566"
FT   DOMAIN          467..513
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   REGION          36..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..76
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..119
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   MOD_RES         117
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         195
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         367..376
FT                   /note="VPIPGPVGNK -> ATNWTSEIPL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010527"
FT   VAR_SEQ         377..528
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010528"
FT   CONFLICT        220
FT                   /note="G -> A (in Ref. 4; AAH63474)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="D -> N (in Ref. 4; AAH42193)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   528 AA;  58944 MW;  472143144700DC26 CRC64;
     MFGAAGRQPI GAPAAGNSWH FSRTMEELVH DLVSALEESS EQARGGFAET GDHSRSISCP
     LKRQARKRRG RKRRSYNVHH PWETGHCLSE GSDSSLEEPS KDYRENHNNN KKDHSDSDDQ
     MLVAKRRPSS NLNNNVRGKR PLWHESDFAV DNVGNRTLRR RRKVKRMAVD LPQDISNKRT
     MTQPPEGCRD QDMDSDRAYQ YQEFTKNKVK KRKLKIIRQG PKIQDEGVVL ESEETNQTNK
     DKMECEEQKV SDELMSESDS SSLSSTDAGL FTNDEGRQGD DEQSDWFYEK ESGGACGITG
     VVPWWEKEDP TELDKNVPDP VFESILTGSF PLMSHPSRRG FQARLSRLHG MSSKNIKKSG
     GTPTSMVPIP GPVGNKRMVH FSPDSHHHDH WFSPGARTEH DQHQLLRDNR AERGHKKNCS
     VRTASRQTSM HLGSLCTGDI KRRRKAAPLP GPTTAGFVGE NAQPILENNI GNRMLQNMGW
     TPGSGLGRDG KGISEPIQAM QRPKGLGLGF PLPKSTSATT TPNAGKSA
 
 
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