GPTC1_HUMAN
ID GPTC1_HUMAN Reviewed; 931 AA.
AC Q9BRR8; Q8IZV6; Q8N3B7; Q9NW94;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=G patch domain-containing protein 1;
DE AltName: Full=Evolutionarily conserved G-patch domain-containing protein;
GN Name=GPATCH1; Synonyms=ECGP, GPATC1;
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 [MRNA].
RC TISSUE=Urinary bladder;
RA Luallen R.J., Sargeant R., Geng Y.;
RT "Cloning of an evolutionarily conserved G-patch domain containing
RT protein.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-931, AND VARIANTS PRO-476;
RP ARG-724 AND SER-728.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 434-931, AND VARIANT SER-728.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6 AND SER-8, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6 AND SER-8, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-357; SER-477 AND
RP SER-715, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-312, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- SIMILARITY: Belongs to the GPATCH1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91489.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD39124.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF434677; AAN63596.1; -; mRNA.
DR EMBL; BC006108; AAH06108.1; -; mRNA.
DR EMBL; AL834465; CAD39124.1; ALT_INIT; mRNA.
DR EMBL; AK001068; BAA91489.1; ALT_INIT; mRNA.
DR CCDS; CCDS12428.1; -.
DR RefSeq; NP_060495.2; NM_018025.2.
DR AlphaFoldDB; Q9BRR8; -.
DR BioGRID; 120406; 83.
DR CORUM; Q9BRR8; -.
DR IntAct; Q9BRR8; 46.
DR MINT; Q9BRR8; -.
DR STRING; 9606.ENSP00000170564; -.
DR GlyGen; Q9BRR8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BRR8; -.
DR PhosphoSitePlus; Q9BRR8; -.
DR BioMuta; GPATCH1; -.
DR DMDM; 74732921; -.
DR EPD; Q9BRR8; -.
DR jPOST; Q9BRR8; -.
DR MassIVE; Q9BRR8; -.
DR MaxQB; Q9BRR8; -.
DR PaxDb; Q9BRR8; -.
DR PeptideAtlas; Q9BRR8; -.
DR PRIDE; Q9BRR8; -.
DR ProteomicsDB; 78818; -.
DR Antibodypedia; 28992; 21 antibodies from 8 providers.
DR DNASU; 55094; -.
DR Ensembl; ENST00000170564.7; ENSP00000170564.1; ENSG00000076650.7.
DR GeneID; 55094; -.
DR KEGG; hsa:55094; -.
DR MANE-Select; ENST00000170564.7; ENSP00000170564.1; NM_018025.3; NP_060495.2.
DR UCSC; uc002nug.2; human.
DR CTD; 55094; -.
DR DisGeNET; 55094; -.
DR GeneCards; GPATCH1; -.
DR HGNC; HGNC:24658; GPATCH1.
DR HPA; ENSG00000076650; Low tissue specificity.
DR neXtProt; NX_Q9BRR8; -.
DR OpenTargets; ENSG00000076650; -.
DR PharmGKB; PA162390063; -.
DR VEuPathDB; HostDB:ENSG00000076650; -.
DR eggNOG; KOG2138; Eukaryota.
DR GeneTree; ENSGT00390000007074; -.
DR HOGENOM; CLU_008613_2_0_1; -.
DR InParanoid; Q9BRR8; -.
DR OMA; QLWQQHA; -.
DR OrthoDB; 1175081at2759; -.
DR PhylomeDB; Q9BRR8; -.
DR TreeFam; TF314717; -.
DR PathwayCommons; Q9BRR8; -.
DR SignaLink; Q9BRR8; -.
DR BioGRID-ORCS; 55094; 199 hits in 1091 CRISPR screens.
DR ChiTaRS; GPATCH1; human.
DR GenomeRNAi; 55094; -.
DR Pharos; Q9BRR8; Tdark.
DR PRO; PR:Q9BRR8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BRR8; protein.
DR Bgee; ENSG00000076650; Expressed in calcaneal tendon and 170 other tissues.
DR ExpressionAtlas; Q9BRR8; baseline and differential.
DR Genevisible; Q9BRR8; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR InterPro; IPR011666; DUF1604.
DR InterPro; IPR000467; G_patch_dom.
DR Pfam; PF07713; DUF1604; 1.
DR Pfam; PF01585; G-patch; 1.
DR PROSITE; PS50174; G_PATCH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CHAIN 2..931
FT /note="G patch domain-containing protein 1"
FT /id="PRO_0000287457"
FT DOMAIN 152..198
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..889
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 312
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 476
FT /note="L -> P (in dbSNP:rs2287679)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_032303"
FT VARIANT 520
FT /note="L -> S (in dbSNP:rs16967805)"
FT /id="VAR_051014"
FT VARIANT 631
FT /note="D -> E (in dbSNP:rs35389599)"
FT /id="VAR_059657"
FT VARIANT 724
FT /note="H -> R (in dbSNP:rs10416265)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_032304"
FT VARIANT 728
FT /note="L -> S (in dbSNP:rs10421769)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_032305"
FT VARIANT 909
FT /note="E -> K (in dbSNP:rs16967824)"
FT /id="VAR_032306"
FT CONFLICT 484
FT /note="H -> Y (in Ref. 4; BAA91489)"
FT /evidence="ECO:0000305"
FT CONFLICT 748
FT /note="R -> P (in Ref. 1; AAN63596)"
FT /evidence="ECO:0000305"
FT CONFLICT 800
FT /note="S -> L (in Ref. 3; CAD39124)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 931 AA; 103345 MW; 407082BEC44904F4 CRC64;
MAARDSDSEE DLVSYGTGLE PLEEGERPKK PIPLQDQTVR DEKGRYKRFH GAFSGGFSAG
YFNTVGSKEG WTPSTFVSSR QNRADKSVLG PEDFMDEEDL SEFGIAPKAI VTTDDFASKT
KDRIREKARQ LAAATAPIPG ATLLDDLITP AKLSVGFELL RKMGWKEGQG VGPRVKRRPR
RQKPDPGVKI YGCALPPGSS EGSEGEDDDY LPDNVTFAPK DVTPVDFTPK DNVHGLAYKG
LDPHQALFGT SGEHFNLFSG GSERAGDLGE IGLNKGRKLG ISGQAFGVGA LEEEDDDIYA
TETLSKYDTV LKDEEPGDGL YGWTAPRQYK NQKESEKDLR YVGKILDGFS LASKPLSSKK
IYPPPELPRD YRPVHYFRPM VAATSENSHL LQVLSESAGK ATPDPGTHSK HQLNASKRAE
LLGETPIQGS ATSVLEFLSQ KDKERIKEMK QATDLKAAQL KARSLAQNAQ SSRAQLSPAA
AAGHCSWNMA LGGGTATLKA SNFKPFAKDP EKQKRYDEFL VHMKQGQKDA LERCLDPSMT
EWERGRERDE FARAALLYAS SHSTLSSRFT HAKEEDDSDQ VEVPRDQEND VGDKQSAVKM
KMFGKLTRDT FEWHPDKLLC KRFNVPDPYP DSTLVGLPRV KRDKYSVFNF LTLPETASLP
TTQASSEKVS QHRGPDKSRK PSRWDTSKHE KKEDSISEFL SLARSKAEPP KQQSSPLVNK
EEEHAPELSA NQTVNKDVDA QAEGEGSRPS MDLFRAIFAS SSDEKSSSSE DEQGDSEDDQ
AGSGEANFQS SQDTDLGETS SVAHALVPAP QEPPPSFPIQ KMQIDEREEF GPRLPPVFCP
NARQTLEVPQ KEKHKKNKDK HKAKKEHRRK KEKKKKHRKH KHKGKQKNKK PEKSSSSESS
DSSDSQSDEE TADVSPQELL RRLKSLPLRR Q
