GCC2_HUMAN
ID GCC2_HUMAN Reviewed; 1684 AA.
AC Q8IWJ2; A6H8X8; O15045; Q4ZG46; Q8TDH3; Q9H2G8;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=GRIP and coiled-coil domain-containing protein 2;
DE AltName: Full=185 kDa Golgi coiled-coil protein;
DE Short=GCC185;
DE AltName: Full=CLL-associated antigen KW-11;
DE AltName: Full=CTCL tumor antigen se1-1;
DE AltName: Full=Ran-binding protein 2-like 4;
DE Short=RanBP2L4;
DE AltName: Full=Renal carcinoma antigen NY-REN-53;
GN Name=GCC2; Synonyms=KIAA0336, RANBP2L4;
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 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-1134.
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=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-448 (ISOFORM 1).
RX PubMed=12200376; DOI=10.1182/blood-2002-02-0513;
RA Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M.,
RA Barrett P., Gribben J.G.;
RT "Identification of tumor-associated antigens in chronic lymphocytic
RT leukemia by SEREX.";
RL Blood 100:2123-2131(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 161-946 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11149944; DOI=10.1073/pnas.98.2.629;
RA Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.;
RT "Serological detection of cutaneous T-cell lymphoma-associated antigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001).
RN [7]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12446665; DOI=10.1074/jbc.m210387200;
RA Luke M.R., Kjer-Nielsen L., Brown D.L., Stow J.L., Gleeson P.A.;
RT "GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and
RT GCC185, to subcompartments of the trans-Golgi network.";
RL J. Biol. Chem. 278:4216-4226(2003).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB9A, AND MUTAGENESIS OF
RP TYR-1618.
RX PubMed=16885419; DOI=10.1091/mbc.e06-02-0153;
RA Reddy J.V., Burguete A.S., Sridevi K., Ganley I.G., Nottingham R.M.,
RA Pfeffer S.R.;
RT "A functional role for the GCC185 golgin in mannose 6-phosphate receptor
RT recycling.";
RL Mol. Biol. Cell 17:4353-4363(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1483, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP FUNCTION, AND INTERACTION WITH CLASP1 AND CLASP2.
RX PubMed=17543864; DOI=10.1016/j.devcel.2007.04.002;
RA Efimov A., Kharitonov A., Efimova N., Loncarek J., Miller P.M.,
RA Andreyeva N., Gleeson P., Galjart N., Maia A.R., McLeod I.X.,
RA Yates J.R. III, Maiato H., Khodjakov A., Akhmanova A., Kaverina I.;
RT "Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules at
RT the trans-Golgi network.";
RL Dev. Cell 12:917-930(2007).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17488291; DOI=10.1111/j.1600-0854.2007.00563.x;
RA Derby M.C., Lieu Z.Z., Brown D., Stow J.L., Goud B., Gleeson P.A.;
RT "The trans-Golgi network golgin, GCC185, is required for endosome-to-Golgi
RT transport and maintenance of Golgi structure.";
RL Traffic 8:758-773(2007).
RN [13]
RP INTERACTION WITH STX16.
RX PubMed=18195106; DOI=10.1083/jcb.200707136;
RA Ganley I.G., Espinosa E., Pfeffer S.R.;
RT "A syntaxin 10-SNARE complex distinguishes two distinct transport routes
RT from endosomes to the trans-Golgi in human cells.";
RL J. Cell Biol. 180:159-172(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1483, 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 [15]
RP INTERACTION WITH RAB6A, AND SUBCELLULAR LOCATION.
RX PubMed=19703403; DOI=10.1016/j.cell.2009.05.048;
RA Houghton F.J., Chew P.L., Lodeho S., Goud B., Gleeson P.A.;
RT "The localization of the Golgin GCC185 is independent of Rab6A/A' and
RT Arl1.";
RL Cell 138:787-794(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-11 AND THR-14, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND IDENTIFICATION BY
RP 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1483 AND SER-1487, AND
RP IDENTIFICATION BY 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 [20]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1557-1612, SUBCELLULAR LOCATION,
RP INTERACTION WITH ARL1; RAB6A AND RAB9A, AND MUTAGENESIS OF ILE-1588;
RP LEU-1595 AND TYR-1618.
RX PubMed=18243103; DOI=10.1016/j.cell.2007.11.048;
RA Burguete A.S., Fenn T.D., Brunger A.T., Pfeffer S.R.;
RT "Rab and Arl GTPase family members cooperate in the localization of the
RT golgin GCC185.";
RL Cell 132:286-298(2008).
CC -!- FUNCTION: Golgin which probably tethers transport vesicles to the
CC trans-Golgi network (TGN) and regulates vesicular transport between the
CC endosomes and the Golgi. As a RAB9A effector it is involved in
CC recycling of the mannose 6-phosphate receptor from the late endosomes
CC to the TGN. May also play a role in transport between the recycling
CC endosomes and the Golgi. Required for maintenance of the Golgi
CC structure, it is involved in the biogenesis of noncentrosomal, Golgi-
CC associated microtubules through recruitment of CLASP1 and CLASP2.
CC {ECO:0000269|PubMed:16885419, ECO:0000269|PubMed:17488291,
CC ECO:0000269|PubMed:17543864}.
CC -!- SUBUNIT: Homodimer. Interacts (via GRIP domain) with RAB6A
CC (preferentially in its GTP-bound form). May interact (RAB6A-dependent)
CC with ARL1; according to PubMed:19703403, RAB6A and ARL1 are not
CC involved in GCC2 Golgi localization as proposed by PubMed:18243103.
CC Interacts (probably via GRIP domain) with RAB9A (preferentially in its
CC GTP-bound form). Interacts with CLASP1 and CLASP2; recruits both
CC proteins to membranes of the TGN. Interacts with STX16.
CC {ECO:0000269|PubMed:16885419, ECO:0000269|PubMed:17543864,
CC ECO:0000269|PubMed:18195106, ECO:0000269|PubMed:18243103,
CC ECO:0000269|PubMed:19703403}.
CC -!- INTERACTION:
CC Q8IWJ2; Q8IWJ2: GCC2; NbExp=2; IntAct=EBI-1645320, EBI-1645320;
CC Q8IWJ2; P20340: RAB6A; NbExp=4; IntAct=EBI-1645320, EBI-1052826;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, trans-Golgi network
CC membrane; Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IWJ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IWJ2-3; Sequence=VSP_040106, VSP_040107;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11149944}.
CC -!- DOMAIN: Extended rod-like protein with coiled-coil domains.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG34902.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH37774.1; Type=Miscellaneous discrepancy; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=AAI46790.1; Type=Miscellaneous discrepancy; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=AAL99918.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAX88838.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA20794.2; Type=Miscellaneous discrepancy; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=EAW53882.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB002334; BAA20794.2; ALT_SEQ; mRNA.
DR EMBL; AC012487; AAX88838.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC068941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471182; EAW53882.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC037774; AAH37774.1; ALT_SEQ; mRNA.
DR EMBL; BC146789; AAI46790.1; ALT_SEQ; mRNA.
DR EMBL; AF432211; AAL99918.1; ALT_INIT; mRNA.
DR EMBL; AF273042; AAG34902.1; ALT_FRAME; mRNA.
DR CCDS; CCDS33268.1; -. [Q8IWJ2-1]
DR RefSeq; NP_852118.1; NM_181453.3. [Q8IWJ2-1]
DR RefSeq; XP_006712934.1; XM_006712871.1.
DR PDB; 3BBP; X-ray; 3.00 A; D/E/F=1547-1612.
DR PDBsum; 3BBP; -.
DR AlphaFoldDB; Q8IWJ2; -.
DR SMR; Q8IWJ2; -.
DR BioGRID; 115006; 103.
DR IntAct; Q8IWJ2; 41.
DR STRING; 9606.ENSP00000307939; -.
DR iPTMnet; Q8IWJ2; -.
DR MetOSite; Q8IWJ2; -.
DR PhosphoSitePlus; Q8IWJ2; -.
DR BioMuta; GCC2; -.
DR DMDM; 313104307; -.
DR EPD; Q8IWJ2; -.
DR jPOST; Q8IWJ2; -.
DR MassIVE; Q8IWJ2; -.
DR MaxQB; Q8IWJ2; -.
DR PaxDb; Q8IWJ2; -.
DR PeptideAtlas; Q8IWJ2; -.
DR PRIDE; Q8IWJ2; -.
DR ProteomicsDB; 70862; -. [Q8IWJ2-1]
DR ProteomicsDB; 70863; -. [Q8IWJ2-3]
DR Antibodypedia; 33069; 178 antibodies from 30 providers.
DR DNASU; 9648; -.
DR Ensembl; ENST00000309863.11; ENSP00000307939.5; ENSG00000135968.22. [Q8IWJ2-1]
DR Ensembl; ENST00000482325.5; ENSP00000419969.1; ENSG00000135968.22. [Q8IWJ2-3]
DR GeneID; 9648; -.
DR KEGG; hsa:9648; -.
DR MANE-Select; ENST00000309863.11; ENSP00000307939.5; NM_181453.4; NP_852118.2.
DR UCSC; uc002tec.4; human. [Q8IWJ2-1]
DR CTD; 9648; -.
DR DisGeNET; 9648; -.
DR GeneCards; GCC2; -.
DR HGNC; HGNC:23218; GCC2.
DR HPA; ENSG00000135968; Low tissue specificity.
DR MIM; 612711; gene.
DR neXtProt; NX_Q8IWJ2; -.
DR OpenTargets; ENSG00000135968; -.
DR PharmGKB; PA134876902; -.
DR VEuPathDB; HostDB:ENSG00000135968; -.
DR eggNOG; KOG0864; Eukaryota.
DR GeneTree; ENSGT00950000183078; -.
DR HOGENOM; CLU_002922_0_0_1; -.
DR InParanoid; Q8IWJ2; -.
DR OMA; YKDCVSR; -.
DR OrthoDB; 200498at2759; -.
DR PhylomeDB; Q8IWJ2; -.
DR TreeFam; TF332907; -.
DR PathwayCommons; Q8IWJ2; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR SignaLink; Q8IWJ2; -.
DR SIGNOR; Q8IWJ2; -.
DR BioGRID-ORCS; 9648; 12 hits in 1091 CRISPR screens.
DR ChiTaRS; GCC2; human.
DR EvolutionaryTrace; Q8IWJ2; -.
DR GeneWiki; GCC2; -.
DR GenomeRNAi; 9648; -.
DR Pharos; Q8IWJ2; Tbio.
DR PRO; PR:Q8IWJ2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8IWJ2; protein.
DR Bgee; ENSG00000135968; Expressed in calcaneal tendon and 202 other tissues.
DR ExpressionAtlas; Q8IWJ2; baseline and differential.
DR Genevisible; Q8IWJ2; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031267; F:small GTPase binding; ISS:FlyBase.
DR GO; GO:0090161; P:Golgi ribbon formation; IMP:UniProtKB.
DR GO; GO:0034499; P:late endosome to Golgi transport; IMP:UniProtKB.
DR GO; GO:0034453; P:microtubule anchoring; IMP:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:UniProtKB.
DR GO; GO:0006622; P:protein targeting to lysosome; IMP:UniProtKB.
DR GO; GO:0071955; P:recycling endosome to Golgi transport; IMP:UniProtKB.
DR GO; GO:0070861; P:regulation of protein exit from endoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR InterPro; IPR032023; GCC2_Rab_bind.
DR InterPro; IPR000237; GRIP_dom.
DR Pfam; PF01465; GRIP; 1.
DR Pfam; PF16704; Rab_bind; 1.
DR SMART; SM00755; Grip; 1.
DR PROSITE; PS50913; GRIP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1684
FT /note="GRIP and coiled-coil domain-containing protein 2"
FT /id="PRO_0000190074"
FT DOMAIN 1609..1659
FT /note="GRIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00250"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1475..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1684
FT /note="Mediates interaction with RAB9A"
FT REGION 1574..1613
FT /note="Mediates interaction with RAB6A"
FT COILED 110..1618
FT /evidence="ECO:0000255"
FT COMPBIAS 1475..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 1487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 22..45
FT /note="LETLPKEDLIKFAKKQMMLIQKAK -> NWRKKLKNSDQNLLLKELVILLRH
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9205841"
FT /id="VSP_040106"
FT VAR_SEQ 46..1684
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9205841"
FT /id="VSP_040107"
FT VARIANT 1134
FT /note="Q -> E (in dbSNP:rs2718698)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_046635"
FT VARIANT 1298
FT /note="R -> G (in dbSNP:rs1061202)"
FT /id="VAR_016101"
FT MUTAGEN 1588
FT /note="I->A: Slightly decreases RAB6A binding affinity.
FT Decreases RAB9A binding affinity by 2-fold. Strongly
FT decreases RAB6A or RAB9A binding affinity and abolishes
FT Golgi localization; when associated with A-1595."
FT /evidence="ECO:0000269|PubMed:18243103"
FT MUTAGEN 1595
FT /note="L->A: Decreases RAB6A binding affinity by 2-fold.
FT Strongly decreases RAB9A binding affinity. Strongly
FT decreases RAB6A or RAB9A binding affinity and abolishes
FT Golgi localization; when associated with A-1588."
FT /evidence="ECO:0000269|PubMed:18243103"
FT MUTAGEN 1618
FT /note="Y->A: No effect on interaction with RAB6A and
FT RAB9A."
FT /evidence="ECO:0000269|PubMed:16885419,
FT ECO:0000269|PubMed:18243103"
FT HELIX 1574..1605
FT /evidence="ECO:0007829|PDB:3BBP"
SQ SEQUENCE 1684 AA; 195910 MW; 83B6135D9EB9440D CRC64;
MEDLVQDGVA SPATPGTGKS KLETLPKEDL IKFAKKQMML IQKAKSRCTE LEKEIEELRS
KPVTEGTGDI IKALTERLDA LLLEKAETEQ QCLSLKKENI KMKQEVEDSV TKMGDAHKEL
EQSHINYVKE IENLKNELMA VRSKYSEDKA NLQKQLEEAM NTQLELSEQL KFQNNSEDNV
KKLQEEIEKI RPGFEEQILY LQKQLDATTD EKKETVTQLQ NIIEANSQHY QKNINSLQEE
LLQLKAIHQE EVKELMCQIE ASAKEHEAEI NKLNELKENL VKQCEASEKN IQKKYECELE
NLRKATSNAN QDNQICSILL QENTFVEQVV NEKVKHLEDT LKELESQHSI LKDEVTYMNN
LKLKLEMDAQ HIKDEFFHER EDLEFKINEL LLAKEEQGCV IEKLKSELAG LNKQFCYTVE
QHNREVQSLK EQHQKEISEL NETFLSDSEK EKLTLMFEIQ GLKEQCENLQ QEKQEAILNY
ESLREIMEIL QTELGESAGK ISQEFESMKQ QQASDVHELQ QKLRTAFTEK DALLETVNRL
QGENEKLLSQ QELVPELENT IKNLQEKNGV YLLSLSQRDT MLKELEGKIN SLTEEKDDFI
NKLKNSHEEM DNFHKKCERE ERLILELGKK VEQTIQYNSE LEQKVNELTG GLEETLKEKD
QNDQKLEKLM VQMKVLSEDK EVLSAEVKSL YEENNKLSSE KKQLSRDLEV FLSQKEDVIL
KEHITQLEKK LQLMVEEQDN LNKLLENEQV QKLFVKTQLY GFLKEMGSEV SEDSEEKDVV
NVLQAVGESL AKINEEKCNL AFQRDEKVLE LEKEIKCLQE ESVVQCEELK SLLRDYEQEK
VLLRKELEEI QSEKEALQSD LLEMKNANEK TRLENQNLLI QVEEVSQTCS KSEIHNEKEK
CFIKEHENLK PLLEQKELRD RRAELILLKD SLAKSPSVKN DPLSSVKELE EKIENLEKEC
KEKEEKINKI KLVAVKAKKE LDSSRKETQT VKEELESLRS EKDQLSASMR DLIQGAESYK
NLLLEYEKQS EQLDVEKERA NNFEHRIEDL TRQLRNSTLQ CETINSDNED LLARIETLQS
NAKLLEVQIL EVQRAKAMVD KELEAEKLQK EQKIKEHATT VNELEELQVQ LQKQKKQLQK
TMQELELVKK DAQQTTLMNM EIADYERLMK ELNQKLTNKN NKIEDLEQEI KIQKQKQETL
QEEITSLQSS VQQYEEKNTK IKQLLVKTKK ELADSKQAET DHLILQASLK GELEASQQQV
EVYKIQLAEI TSEKHKIHEH LKTSAEQHQR TLSAYQQRVT ALQEECRAAK AEQATVTSEF
ESYKVRVHNV LKQQKNKSMS QAETEGAKQE REHLEMLIDQ LKIKLQDSQN NLQINVSELQ
TLQSEHDTLL ERHNKMLQET VSKEAELREK LCSIQSENMM MKSEHTQTVS QLTSQNEVLR
NSFRDQVRHL QEEHRKTVET LQQQLSKMEA QLFQLKNEPT TRSPVSSQQS LKNLRERRNT
DLPLLDMHTV TREEGEGMET TDTESVSSAS TYTQSLEQLL NSPETKLEPP LWHAEFTKEE
LVQKLSSTTK SADHLNGLLR ETEATNAILM EQIKLLKSEI RRLERNQERE KSAANLEYLK
NVLLQFIFLK PGSERERLLP VINTMLQLSP EEKGKLAAVA QGEEENASRS SGWASYLHSW
SGLR
