GOGA4_HUMAN
ID GOGA4_HUMAN Reviewed; 2230 AA.
AC Q13439; F8W8Q7; Q13270; Q13654; Q14436; Q59EW8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Golgin subfamily A member 4;
DE AltName: Full=256 kDa golgin;
DE AltName: Full=Golgin-245;
DE AltName: Full=Protein 72.1;
DE AltName: Full=Trans-Golgi p230;
GN Name=GOLGA4;
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), AND ALTERNATIVE SPLICING.
RX PubMed=8626529; DOI=10.1074/jbc.271.14.8328;
RA Erlich R., Gleeson P.A., Campbell P., Dietzsch E., Toh B.-H.;
RT "Molecular characterization of trans-Golgi p230: a human peripheral
RT membrane protein encoded by a gene on chromosome 6p12-22 contains extensive
RT coiled-coil alpha-helical domains and a granin motif.";
RL J. Biol. Chem. 271:8328-8337(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Seelig H.P.;
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1279 (ISOFORM 5).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 131-2230.
RC TISSUE=Placenta;
RX PubMed=8537393; DOI=10.1074/jbc.270.52.31262;
RA Fritzler M.J., Lung C.-C., Hamel J.C., Griffith K.J., Chan E.K.L.;
RT "Molecular characterization of golgin-245, a novel Golgi complex protein
RT containing a granin signature.";
RL J. Biol. Chem. 270:31262-31268(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 524-672.
RC TISSUE=Gastric fundus;
RA Balague C.;
RL Thesis (1994), Instituto municipal de investigacion medica, Spain.
RN [7]
RP INTERACTION WITH RAB6A, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-2177.
RX PubMed=10209123; DOI=10.1016/s0960-9822(99)80167-5;
RA Barr F.A.;
RT "A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-
RT coil proteins.";
RL Curr. Biol. 9:381-384(1999).
RN [8]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-2177 AND TYR-2185.
RX PubMed=10209125; DOI=10.1016/s0960-9822(99)80168-7;
RA Kjer-Nielsen L., Teasdale R.D., van Vliet C., Gleeson P.A.;
RT "A novel Golgi-localisation domain shared by a class of coiled-coil
RT peripheral membrane proteins.";
RL Curr. Biol. 9:385-388(1999).
RN [9]
RP INTERACTION WITH ARL1 AND ARL3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP TYR-2177.
RX PubMed=11303027; DOI=10.1074/jbc.m102359200;
RA Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.;
RT "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific
RT and shared effectors: characterizing ARL1-binding proteins.";
RL J. Biol. Chem. 276:22826-22837(2001).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MACF1.
RX PubMed=15265687; DOI=10.1016/j.yexcr.2004.04.047;
RA Kakinuma T., Ichikawa H., Tsukada Y., Nakamura T., Toh B.H.;
RT "Interaction between p230 and MACF1 is associated with transport of a
RT glycosyl phosphatidyl inositol-anchored protein from the Golgi to the cell
RT periphery.";
RL Exp. Cell Res. 298:388-398(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-89; SER-266 AND
RP THR-2223, AND IDENTIFICATION BY 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-78 AND SER-266, 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-266, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-41; SER-71; SER-78
RP AND SER-266, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, 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 [19]
RP FUNCTION, INTERACTION WITH TBC1D23 AND FAM91A1, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF PHE-2.
RX PubMed=29084197; DOI=10.1038/ncb3627;
RA Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.;
RT "TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at
RT the trans-Golgi.";
RL Nat. Cell Biol. 19:1424-1432(2017).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2170-2221 IN COMPLEX WITH ARL1.
RX PubMed=14580338; DOI=10.1016/s1097-2765(03)00356-3;
RA Panic B., Perisic O., Veprintsev D.B., Williams R.L., Munro S.;
RT "Structural basis for Arl1-dependent targeting of homodimeric GRIP domains
RT to the Golgi apparatus.";
RL Mol. Cell 12:863-874(2003).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2172-2222 IN COMPLEX WITH ARL1,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-2181; PHE-2183; MET-2186;
RP THR-2193; MET-2194; VAL-2197; ILE-2198; LEU-2202; PHE-2204 AND ILE-2212,
RP AND HOMODIMERIZATION.
RX PubMed=14718928; DOI=10.1038/nsmb714;
RA Wu M., Lu L., Hong W., Song H.;
RT "Structural basis for recruitment of GRIP domain golgin-245 by small GTPase
RT Arl1.";
RL Nat. Struct. Mol. Biol. 11:86-94(2004).
CC -!- FUNCTION: Involved in vesicular trafficking at the Golgi apparatus
CC level. May play a role in delivery of transport vesicles containing
CC GPI-linked proteins from the trans-Golgi network through its
CC interaction with MACF1. Involved in endosome-to-Golgi trafficking
CC (PubMed:29084197). {ECO:0000269|PubMed:15265687,
CC ECO:0000269|PubMed:29084197}.
CC -!- SUBUNIT: Homodimer (PubMed:14718928). Interacts with RAB6A
CC (PubMed:10209123). Interacts with GTP-bound ARL1 and ARL3
CC (PubMed:11303027, PubMed:14580338, PubMed:14718928). Interacts with
CC MACF1 (PubMed:15265687). Directly interacts with TBC1D23
CC (PubMed:29084197). Interacts with FAM91A1; this interaction may be
CC mediated by TBC1D23 (PubMed:29084197). {ECO:0000269|PubMed:10209123,
CC ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:14580338,
CC ECO:0000269|PubMed:14718928, ECO:0000269|PubMed:15265687,
CC ECO:0000269|PubMed:29084197}.
CC -!- INTERACTION:
CC Q13439; Q96NW4: ANKRD27; NbExp=2; IntAct=EBI-1037845, EBI-6125599;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane
CC {ECO:0000269|PubMed:10209123, ECO:0000269|PubMed:10209125,
CC ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:14718928,
CC ECO:0000269|PubMed:15265687}; Peripheral membrane protein. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:29084197}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q13439-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q13439-3; Sequence=VSP_004274;
CC Name=4;
CC IsoId=Q13439-4; Sequence=VSP_004275;
CC Name=5;
CC IsoId=Q13439-5; Sequence=VSP_044819, VSP_004274, VSP_004275;
CC -!- DOMAIN: Extended rod-like protein with coiled-coil domains.
CC -!- MISCELLANEOUS: Antibodies against GOLGA4 are present in sera from
CC patients with Sjoegren syndrome. Sera from patients with Sjoegren
CC syndrome often contain antibodies that react with normal components of
CC the Golgi complex.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92930.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA58041.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U41740; AAC50434.1; -; mRNA.
DR EMBL; X82834; CAA58041.1; ALT_FRAME; mRNA.
DR EMBL; AC097359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB209693; BAD92930.1; ALT_INIT; mRNA.
DR EMBL; U31906; AAC51791.1; -; mRNA.
DR EMBL; X76942; CAA54261.1; -; mRNA.
DR CCDS; CCDS2666.1; -. [Q13439-1]
DR CCDS; CCDS54564.1; -. [Q13439-5]
DR RefSeq; NP_001166184.1; NM_001172713.1. [Q13439-5]
DR RefSeq; NP_002069.2; NM_002078.4. [Q13439-1]
DR PDB; 1R4A; X-ray; 2.30 A; E/F/G/H=2172-2222.
DR PDB; 1UPT; X-ray; 1.70 A; B/D/F/H=2170-2228.
DR PDBsum; 1R4A; -.
DR PDBsum; 1UPT; -.
DR AlphaFoldDB; Q13439; -.
DR SMR; Q13439; -.
DR BioGRID; 109065; 129.
DR IntAct; Q13439; 49.
DR MINT; Q13439; -.
DR STRING; 9606.ENSP00000349305; -.
DR GlyConnect; 690; 5 N-Linked glycans (2 sites).
DR GlyGen; Q13439; 3 sites, 10 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q13439; -.
DR MetOSite; Q13439; -.
DR PhosphoSitePlus; Q13439; -.
DR BioMuta; GOLGA4; -.
DR DMDM; 12643718; -.
DR EPD; Q13439; -.
DR jPOST; Q13439; -.
DR MassIVE; Q13439; -.
DR MaxQB; Q13439; -.
DR PaxDb; Q13439; -.
DR PeptideAtlas; Q13439; -.
DR PRIDE; Q13439; -.
DR ProteomicsDB; 30188; -.
DR ProteomicsDB; 59436; -. [Q13439-1]
DR ProteomicsDB; 59437; -. [Q13439-3]
DR ProteomicsDB; 59438; -. [Q13439-4]
DR Antibodypedia; 28305; 93 antibodies from 23 providers.
DR DNASU; 2803; -.
DR Ensembl; ENST00000356847.8; ENSP00000349305.4; ENSG00000144674.17. [Q13439-5]
DR Ensembl; ENST00000361924.7; ENSP00000354486.2; ENSG00000144674.17. [Q13439-1]
DR GeneID; 2803; -.
DR KEGG; hsa:2803; -.
DR MANE-Select; ENST00000361924.7; ENSP00000354486.2; NM_002078.5; NP_002069.2.
DR UCSC; uc003cgv.4; human. [Q13439-1]
DR CTD; 2803; -.
DR DisGeNET; 2803; -.
DR GeneCards; GOLGA4; -.
DR HGNC; HGNC:4427; GOLGA4.
DR HPA; ENSG00000144674; Low tissue specificity.
DR MIM; 602509; gene.
DR neXtProt; NX_Q13439; -.
DR OpenTargets; ENSG00000144674; -.
DR PharmGKB; PA28808; -.
DR VEuPathDB; HostDB:ENSG00000144674; -.
DR eggNOG; ENOG502QTM0; Eukaryota.
DR GeneTree; ENSGT00730000111139; -.
DR HOGENOM; CLU_001994_0_0_1; -.
DR InParanoid; Q13439; -.
DR OMA; DEFRNQG; -.
DR OrthoDB; 663248at2759; -.
DR PhylomeDB; Q13439; -.
DR TreeFam; TF325082; -.
DR PathwayCommons; Q13439; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-HSA-9673768; Signaling by membrane-tethered fusions of PDGFRA or PDGFRB.
DR SignaLink; Q13439; -.
DR BioGRID-ORCS; 2803; 14 hits in 1076 CRISPR screens.
DR ChiTaRS; GOLGA4; human.
DR EvolutionaryTrace; Q13439; -.
DR GeneWiki; GOLGA4; -.
DR GenomeRNAi; 2803; -.
DR Pharos; Q13439; Tbio.
DR PRO; PR:Q13439; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q13439; protein.
DR Bgee; ENSG00000144674; Expressed in gluteal muscle and 210 other tissues.
DR ExpressionAtlas; Q13439; baseline and differential.
DR Genevisible; Q13439; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005802; C:trans-Golgi network; TAS:ProtInc.
DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB.
DR GO; GO:0048193; P:Golgi vesicle transport; IBA:GO_Central.
DR GO; GO:0045773; P:positive regulation of axon extension; IDA:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR InterPro; IPR000237; GRIP_dom.
DR Pfam; PF01465; GRIP; 1.
DR SMART; SM00755; Grip; 1.
DR PROSITE; PS50913; GRIP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Glycoprotein;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..2230
FT /note="Golgin subfamily A member 4"
FT /id="PRO_0000190059"
FT DOMAIN 2168..2215
FT /note="GRIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00250"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..203
FT /note="Interaction with MACF1"
FT /evidence="ECO:0000269|PubMed:15265687"
FT COILED 133..2185
FT /evidence="ECO:0000255"
FT COMPBIAS 11..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q91VW5"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2223
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 54
FT /note="E -> ENASTHASKSPDSVNGSEPSIPQ (in isoform 5)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_044819"
FT VAR_SEQ 2103..2109
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_004274"
FT VAR_SEQ 2222..2230
FT /note="FTSPRSGIF -> SWLRSSS (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_004275"
FT VARIANT 1028
FT /note="Q -> K (in dbSNP:rs11718848)"
FT /id="VAR_033975"
FT VARIANT 1552
FT /note="N -> S (in dbSNP:rs9840779)"
FT /id="VAR_033976"
FT VARIANT 2058
FT /note="R -> S (in dbSNP:rs11924014)"
FT /id="VAR_049258"
FT MUTAGEN 2
FT /note="F->A: Loss of TBC1D23-binding."
FT /evidence="ECO:0000269|PubMed:29084197"
FT MUTAGEN 2177
FT /note="Y->A: Loss of localization at the Golgi apparatus.
FT Loss of ARL1-binding."
FT /evidence="ECO:0000269|PubMed:10209123,
FT ECO:0000269|PubMed:10209125, ECO:0000269|PubMed:11303027,
FT ECO:0000269|PubMed:14718928"
FT MUTAGEN 2177
FT /note="Y->F: No effect on localization at the Golgi
FT apparatus."
FT /evidence="ECO:0000269|PubMed:10209125,
FT ECO:0000269|PubMed:14718928"
FT MUTAGEN 2181
FT /note="V->A: Abolishes Golgi localization."
FT /evidence="ECO:0000269|PubMed:14718928"
FT MUTAGEN 2183
FT /note="F->A: Abolishes Golgi localization."
FT /evidence="ECO:0000269|PubMed:14718928"
FT MUTAGEN 2185
FT /note="Y->A: Loss of localization at the Golgi apparatus."
FT /evidence="ECO:0000269|PubMed:10209125"
FT MUTAGEN 2186
FT /note="M->A: Abolishes Golgi localization."
FT /evidence="ECO:0000269|PubMed:14718928"
FT MUTAGEN 2193
FT /note="T->A: Abolishes Golgi localization."
FT /evidence="ECO:0000269|PubMed:14718928"
FT MUTAGEN 2194
FT /note="M->A: Abolishes Golgi localization."
FT /evidence="ECO:0000269|PubMed:14718928"
FT MUTAGEN 2197
FT /note="V->A: Abolishes Golgi localization."
FT /evidence="ECO:0000269|PubMed:14718928"
FT MUTAGEN 2198
FT /note="I->A: Abolishes Golgi localization."
FT /evidence="ECO:0000269|PubMed:14718928"
FT MUTAGEN 2202
FT /note="L->A: Abolishes Golgi localization."
FT /evidence="ECO:0000269|PubMed:14718928"
FT MUTAGEN 2204
FT /note="F->A: Abolishes Golgi localization."
FT /evidence="ECO:0000269|PubMed:14718928"
FT MUTAGEN 2212
FT /note="I->A: Abolishes Golgi localization."
FT /evidence="ECO:0000269|PubMed:14718928"
FT CONFLICT 188
FT /note="R -> K (in Ref. 5; AAC51791)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="Y -> H (in Ref. 5; AAC51791)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="T -> A (in Ref. 5; AAC51791)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="K -> E (in Ref. 5; AAC51791)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="T -> A (in Ref. 5; AAC51791)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="K -> E (in Ref. 5; AAC51791)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="K -> N (in Ref. 5; AAC51791)"
FT /evidence="ECO:0000305"
FT HELIX 2173..2186
FT /evidence="ECO:0007829|PDB:1UPT"
FT HELIX 2191..2201
FT /evidence="ECO:0007829|PDB:1UPT"
FT HELIX 2206..2221
FT /evidence="ECO:0007829|PDB:1UPT"
SQ SEQUENCE 2230 AA; 261140 MW; 3BB733DB1EA86134 CRC64;
MFKKLKQKIS EEQQQLQQAL APAQASSNSS TPTRMRSRTS SFTEQLDEGT PNRESGDTQS
FAQKLQLRVP SVESLFRSPI KESLFRSSSK ESLVRTSSRE SLNRLDLDSS TASFDPPSDM
DSEAEDLVGN SDSLNKEQLI QRLRRMERSL SSYRGKYSEL VTAYQMLQRE KKKLQGILSQ
SQDKSLRRIA ELREELQMDQ QAKKHLQEEF DASLEEKDQY ISVLQTQVSL LKQRLRNGPM
NVDVLKPLPQ LEPQAEVFTK EENPESDGEP VVEDGTSVKT LETLQQRVKR QENLLKRCKE
TIQSHKEQCT LLTSEKEALQ EQLDERLQEL EKIKDLHMAE KTKLITQLRD AKNLIEQLEQ
DKGMVIAETK RQMHETLEMK EEEIAQLRSR IKQMTTQGEE LREQKEKSER AAFEELEKAL
STAQKTEEAR RKLKAEMDEQ IKTIEKTSEE ERISLQQELS RVKQEVVDVM KKSSEEQIAK
LQKLHEKELA RKEQELTKKL QTREREFQEQ MKVALEKSQS EYLKISQEKE QQESLALEEL
ELQKKAILTE SENKLRDLQQ EAETYRTRIL ELESSLEKSL QENKNQSKDL AVHLEAEKNK
HNKEITVMVE KHKTELESLK HQQDALWTEK LQVLKQQYQT EMEKLREKCE QEKETLLKDK
EIIFQAHIEE MNEKTLEKLD VKQTELESLS SELSEVLKAR HKLEEELSVL KDQTDKMKQE
LEAKMDEQKN HHQQQVDSII KEHEVSIQRT EKALKDQINQ LELLLKERDK HLKEHQAHVE
NLEADIKRSE GELQQASAKL DVFQSYQSAT HEQTKAYEEQ LAQLQQKLLD LETERILLTK
QVAEVEAQKK DVCTELDAHK IQVQDLMQQL EKQNSEMEQK VKSLTQVYES KLEDGNKEQE
QTKQILVEKE NMILQMREGQ KKEIEILTQK LSAKEDSIHI LNEEYETKFK NQEKKMEKVK
QKAKEMQETL KKKLLDQEAK LKKELENTAL ELSQKEKQFN AKMLEMAQAN SAGISDAVSR
LETNQKEQIE SLTEVHRREL NDVISIWEKK LNQQAEELQE IHEIQLQEKE QEVAELKQKI
LLFGCEKEEM NKEITWLKEE GVKQDTTLNE LQEQLKQKSA HVNSLAQDET KLKAHLEKLE
VDLNKSLKEN TFLQEQLVEL KMLAEEDKRK VSELTSKLKT TDEEFQSLKS SHEKSNKSLE
DKSLEFKKLS EELAIQLDIC CKKTEALLEA KTNELINISS SKTNAILSRI SHCQHRTTKV
KEALLIKTCT VSELEAQLRQ LTEEQNTLNI SFQQATHQLE EKENQIKSMK ADIESLVTEK
EALQKEGGNQ QQAASEKESC ITQLKKELSE NINAVTLMKE ELKEKKVEIS SLSKQLTDLN
VQLQNSISLS EKEAAISSLR KQYDEEKCEL LDQVQDLSFK VDTLSKEKIS ALEQVDDWSN
KFSEWKKKAQ SRFTQHQNTV KELQIQLELK SKEAYEKDEQ INLLKEELDQ QNKRFDCLKG
EMEDDKSKME KKESNLETEL KSQTARIMEL EDHITQKTIE IESLNEVLKN YNQQKDIEHK
ELVQKLQHFQ ELGEEKDNRV KEAEEKILTL ENQVYSMKAE LETKKKELEH VNLSVKSKEE
ELKALEDRLE SESAAKLAEL KRKAEQKIAA IKKQLLSQME EKEEQYKKGT ESHLSELNTK
LQEREREVHI LEEKLKSVES SQSETLIVPR SAKNVAAYTE QEEADSQGCV QKTYEEKISV
LQRNLTEKEK LLQRVGQEKE ETVSSHFEMR CQYQERLIKL EHAEAKQHED QSMIGHLQEE
LEEKNKKYSL IVAQHVEKEG GKNNIQAKQN LENVFDDVQK TLQEKELTCQ ILEQKIKELD
SCLVRQKEVH RVEMEELTSK YEKLQALQQM DGRNKPTELL EENTEEKSKS HLVQPKLLSN
MEAQHNDLEF KLAGAEREKQ KLGKEIVRLQ KDLRMLRKEH QQELEILKKE YDQEREEKIK
QEQEDLELKH NSTLKQLMRE FNTQLAQKEQ ELEMTIKETI NKAQEVEAEL LESHQEETNQ
LLKKIAEKDD DLKRTAKRYE EILDAREEEM TAKVRDLQTQ LEELQKKYQQ KLEQEENPGN
DNVTIMELQT QLAQKTTLIS DSKLKEQEFR EQIHNLEDRL KKYEKNVYAT TVGTPYKGGN
LYHTDVSLFG EPTEFEYLRK VLFEYMMGRE TKTMAKVITT VLKFPDDQTQ KILEREDARL
MFTSPRSGIF
