GIPC1_HUMAN
ID GIPC1_HUMAN Reviewed; 333 AA.
AC O14908; A8K4I3; A8MZG3; Q9BTC9;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=PDZ domain-containing protein GIPC1;
DE AltName: Full=GAIP C-terminus-interacting protein;
DE AltName: Full=RGS-GAIP-interacting protein;
DE AltName: Full=RGS19-interacting protein 1;
DE AltName: Full=Synectin;
DE AltName: Full=Tax interaction protein 2;
DE Short=TIP-2;
GN Name=GIPC1; Synonyms=C19orf3, GIPC, RGS19IP1;
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] (ISOFORM 1), INTERACTION WITH RGS19, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Pituitary;
RX PubMed=9770488; DOI=10.1073/pnas.95.21.12340;
RA De Vries L., Lou X., Zhao G., Zheng B., Farquhar M.G.;
RT "GIPC, a PDZ domain containing protein, interacts specifically with the C-
RT terminus of RGS-GAIP.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12340-12345(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and 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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 78-333 (ISOFORM 1/2), AND INTERACTION WITH
RP HTLV-I TAX.
RX PubMed=9482110; DOI=10.1038/sj.onc.1201567;
RA Rousset R., Fabre S., Desbois C., Bantignies F., Jalinot P.;
RT "The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the
RT PDZ domain of cellular proteins.";
RL Oncogene 16:643-654(1998).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND SER-232, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-222; SER-225;
RP SER-232; THR-242 AND SER-247, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP INVOLVEMENT IN OPDM2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=32413282; DOI=10.1016/j.ajhg.2020.04.011;
RA Deng J., Yu J., Li P., Luan X., Cao L., Zhao J., Yu M., Zhang W., Lv H.,
RA Xie Z., Meng L., Zheng Y., Zhao Y., Gang Q., Wang Q., Liu J., Zhu M.,
RA Guo X., Su Y., Liang Y., Liang F., Hayashi T., Maeda M.H., Sato T., Ura S.,
RA Oya Y., Ogasawara M., Iida A., Nishino I., Zhou C., Yan C., Yuan Y.,
RA Hong D., Wang Z.;
RT "Expansion of GGC Repeat in GIPC1 Is Associated with Oculopharyngodistal
RT Myopathy.";
RL Am. J. Hum. Genet. 106:793-804(2020).
CC -!- FUNCTION: May be involved in G protein-linked signaling.
CC -!- SUBUNIT: Interacts with GLUT1 (C-terminus), ACTN1, KIF1B, MYO6,
CC PLEKHG5, SDC4/syndecan-4 and SEMA4C/semaphorin-4C (By similarity).
CC Interacts with RGS19 C-terminus. Interacts with HTLV-I Tax through the
CC PDZ domain. {ECO:0000250, ECO:0000269|PubMed:9482110,
CC ECO:0000269|PubMed:9770488}.
CC -!- INTERACTION:
CC O14908; Q9HB19: PLEKHA2; NbExp=3; IntAct=EBI-373132, EBI-4401947;
CC O14908; Q03167: TGFBR3; NbExp=3; IntAct=EBI-373132, EBI-2852679;
CC O14908; P17643: TYRP1; NbExp=3; IntAct=EBI-373132, EBI-7900408;
CC O14908-2; Q8NC06-3: ACBD4; NbExp=3; IntAct=EBI-25913156, EBI-12811089;
CC O14908-2; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-25913156, EBI-2875816;
CC O14908-2; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-25913156, EBI-742750;
CC O14908-2; P20849: COL9A1; NbExp=3; IntAct=EBI-25913156, EBI-2528238;
CC O14908-2; Q6NZ36-4: FAAP20; NbExp=3; IntAct=EBI-25913156, EBI-12013806;
CC O14908-2; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-25913156, EBI-11793142;
CC O14908-2; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-25913156, EBI-618189;
CC O14908-2; Q7LGA3-3: HS2ST1; NbExp=3; IntAct=EBI-25913156, EBI-25887463;
CC O14908-2; Q14005-2: IL16; NbExp=3; IntAct=EBI-25913156, EBI-17178971;
CC O14908-2; P57682: KLF3; NbExp=3; IntAct=EBI-25913156, EBI-8472267;
CC O14908-2; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-25913156, EBI-714379;
CC O14908-2; Q15759: MAPK11; NbExp=3; IntAct=EBI-25913156, EBI-298304;
CC O14908-2; Q9Y266: NUDC; NbExp=3; IntAct=EBI-25913156, EBI-357298;
CC O14908-2; Q6P4D5-2: PABIR3; NbExp=3; IntAct=EBI-25913156, EBI-9091052;
CC O14908-2; Q8WZ73-3: RFFL; NbExp=3; IntAct=EBI-25913156, EBI-25839575;
CC O14908-2; Q969K3: RNF34; NbExp=3; IntAct=EBI-25913156, EBI-2340642;
CC O14908-2; P48443: RXRG; NbExp=3; IntAct=EBI-25913156, EBI-712405;
CC O14908-2; Q8N488: RYBP; NbExp=3; IntAct=EBI-25913156, EBI-752324;
CC O14908-2; Q9BY12-3: SCAPER; NbExp=3; IntAct=EBI-25913156, EBI-25837959;
CC O14908-2; Q86SQ7-2: SDCCAG8; NbExp=3; IntAct=EBI-25913156, EBI-10696955;
CC O14908-2; Q2NKQ1-4: SGSM1; NbExp=3; IntAct=EBI-25913156, EBI-10182463;
CC O14908-2; O75558: STX11; NbExp=3; IntAct=EBI-25913156, EBI-714135;
CC O14908-2; O15273: TCAP; NbExp=3; IntAct=EBI-25913156, EBI-954089;
CC O14908-2; O60830: TIMM17B; NbExp=3; IntAct=EBI-25913156, EBI-2372529;
CC O14908-2; Q5VYS8-5: TUT7; NbExp=3; IntAct=EBI-25913156, EBI-9088812;
CC O14908-2; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-25913156, EBI-12817837;
CC O14908-2; Q96EF9: ZHX1-C8orf76; NbExp=3; IntAct=EBI-25913156, EBI-25830993;
CC O14908-2; Q8WUU4: ZNF296; NbExp=3; IntAct=EBI-25913156, EBI-8834821;
CC O14908-2; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-25913156, EBI-12010736;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32413282,
CC ECO:0000269|PubMed:9770488}. Membrane {ECO:0000269|PubMed:9770488};
CC Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14908-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14908-2; Sequence=VSP_044296;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:9770488). Expressed in
CC skeletal muscle (at protein level) (PubMed:32413282).
CC {ECO:0000269|PubMed:32413282, ECO:0000269|PubMed:9770488}.
CC -!- DISEASE: Oculopharyngodistal myopathy 2 (OPDM2) [MIM:618940]: A form of
CC oculopharyngodistal myopathy, a muscle disorder characterized by
CC progressive ptosis, external ophthalmoplegia, and weakness of the
CC masseter, facial, pharyngeal, and distal limb muscles. The
CC myopathological features are presence of rimmed vacuoles in the muscle
CC fibers and myopathic changes of differing severity. OPDM2 inheritance
CC pattern is autosomal dominant. {ECO:0000269|PubMed:32413282}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry. GGC repeat expansions in the 5'-UTR ranging from 73 to 164
CC were reported in patients, compared with a normal range from 12 to 32
CC in unaffected individuals. Patient skeletal muscle showed similar
CC protein levels to those of unaffected individuals.
CC {ECO:0000269|PubMed:32413282}.
CC -!- SIMILARITY: Belongs to the GIPC family. {ECO:0000305}.
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DR EMBL; AF089816; AAC67548.1; -; mRNA.
DR EMBL; AK290948; BAF83637.1; -; mRNA.
DR EMBL; AC008569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84423.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84425.1; -; Genomic_DNA.
DR EMBL; BC000410; AAH00410.1; -; mRNA.
DR EMBL; BC004226; AAH04226.2; -; mRNA.
DR EMBL; BC012810; AAH12810.1; -; mRNA.
DR EMBL; BC016169; AAH16169.1; -; mRNA.
DR EMBL; AF028824; AAB84249.1; -; mRNA.
DR CCDS; CCDS12310.1; -. [O14908-1]
DR CCDS; CCDS12311.1; -. [O14908-2]
DR RefSeq; NP_005707.1; NM_005716.3. [O14908-1]
DR RefSeq; NP_974197.1; NM_202468.2. [O14908-1]
DR RefSeq; NP_974198.1; NM_202469.2. [O14908-2]
DR RefSeq; NP_974199.1; NM_202470.2. [O14908-1]
DR RefSeq; NP_974223.1; NM_202494.2. [O14908-2]
DR RefSeq; XP_016881636.1; XM_017026147.1. [O14908-1]
DR RefSeq; XP_016881637.1; XM_017026148.1. [O14908-2]
DR AlphaFoldDB; O14908; -.
DR SMR; O14908; -.
DR BioGRID; 115978; 97.
DR CORUM; O14908; -.
DR DIP; DIP-31142N; -.
DR IntAct; O14908; 55.
DR MINT; O14908; -.
DR STRING; 9606.ENSP00000376753; -.
DR iPTMnet; O14908; -.
DR PhosphoSitePlus; O14908; -.
DR BioMuta; GIPC1; -.
DR EPD; O14908; -.
DR jPOST; O14908; -.
DR MassIVE; O14908; -.
DR MaxQB; O14908; -.
DR PaxDb; O14908; -.
DR PeptideAtlas; O14908; -.
DR PRIDE; O14908; -.
DR ProteomicsDB; 1863; -.
DR ProteomicsDB; 48292; -. [O14908-1]
DR Antibodypedia; 13703; 297 antibodies from 34 providers.
DR DNASU; 10755; -.
DR Ensembl; ENST00000345425.6; ENSP00000340698.1; ENSG00000123159.16. [O14908-1]
DR Ensembl; ENST00000393028.5; ENSP00000376748.1; ENSG00000123159.16. [O14908-2]
DR Ensembl; ENST00000393033.9; ENSP00000376753.3; ENSG00000123159.16. [O14908-1]
DR Ensembl; ENST00000586027.5; ENSP00000466747.1; ENSG00000123159.16. [O14908-1]
DR Ensembl; ENST00000591349.5; ENSP00000467077.1; ENSG00000123159.16. [O14908-2]
DR GeneID; 10755; -.
DR KEGG; hsa:10755; -.
DR MANE-Select; ENST00000393033.9; ENSP00000376753.3; NM_005716.4; NP_005707.1.
DR UCSC; uc002myt.5; human. [O14908-1]
DR CTD; 10755; -.
DR DisGeNET; 10755; -.
DR GeneCards; GIPC1; -.
DR HGNC; HGNC:1226; GIPC1.
DR HPA; ENSG00000123159; Tissue enhanced (esophagus).
DR MalaCards; GIPC1; -.
DR MIM; 605072; gene.
DR MIM; 618940; phenotype.
DR neXtProt; NX_O14908; -.
DR OpenTargets; ENSG00000123159; -.
DR Orphanet; 98897; Oculopharyngodistal myopathy.
DR PharmGKB; PA34371; -.
DR VEuPathDB; HostDB:ENSG00000123159; -.
DR eggNOG; KOG3938; Eukaryota.
DR GeneTree; ENSGT00390000003420; -.
DR HOGENOM; CLU_044527_1_0_1; -.
DR InParanoid; O14908; -.
DR OMA; QIEPQFD; -.
DR PhylomeDB; O14908; -.
DR TreeFam; TF313878; -.
DR PathwayCommons; O14908; -.
DR SignaLink; O14908; -.
DR BioGRID-ORCS; 10755; 15 hits in 1077 CRISPR screens.
DR ChiTaRS; GIPC1; human.
DR GeneWiki; GIPC1; -.
DR GenomeRNAi; 10755; -.
DR Pharos; O14908; Tbio.
DR PRO; PR:O14908; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O14908; protein.
DR Bgee; ENSG00000123159; Expressed in lower esophagus mucosa and 209 other tissues.
DR ExpressionAtlas; O14908; baseline and differential.
DR Genevisible; O14908; HS.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; ISS:BHF-UCL.
DR GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; ISS:BHF-UCL.
DR GO; GO:0012506; C:vesicle membrane; ISS:BHF-UCL.
DR GO; GO:0003779; F:actin binding; ISS:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
DR GO; GO:0017022; F:myosin binding; ISS:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0098761; P:cellular response to interleukin-7; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; ISS:BHF-UCL.
DR GO; GO:0043542; P:endothelial cell migration; ISS:BHF-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0014047; P:glutamate secretion; ISS:BHF-UCL.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:BHF-UCL.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0006605; P:protein targeting; ISS:BHF-UCL.
DR GO; GO:0031647; P:regulation of protein stability; ISS:BHF-UCL.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:BHF-UCL.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR017379; GIPC1/2/3.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR12259; PTHR12259; 1.
DR Pfam; PF00595; PDZ; 1.
DR PIRSF; PIRSF038083; UCP038083_GIPC; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Congenital muscular dystrophy; Cytoplasm;
KW Dystroglycanopathy; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..333
FT /note="PDZ domain-containing protein GIPC1"
FT /id="PRO_0000087492"
FT DOMAIN 133..213
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..97
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044296"
SQ SEQUENCE 333 AA; 36049 MW; AA980A4B907E3FD9 CRC64;
MPLGLGRRKK APPLVENEEA EPGRGGLGVG EPGPLGGGGS GGPQMGLPPP PPALRPRLVF
HTQLAHGSPT GRIEGFTNVK ELYGKIAEAF RLPTAEVMFC TLNTHKVDMD KLLGGQIGLE
DFIFAHVKGQ RKEVEVFKSE DALGLTITDN GAGYAFIKRI KEGSVIDHIH LISVGDMIEA
INGQSLLGCR HYEVARLLKE LPRGRTFTLK LTEPRKAFDM ISQRSAGGRP GSGPQLGTGR
GTLRLRSRGP ATVEDLPSAF EEKAIEKVDD LLESYMGIRD TELAATMVEL GKDKRNPDEL
AEALDERLGD FAFPDEFVFD VWGAIGDAKV GRY
