GOLI4_HUMAN
ID GOLI4_HUMAN Reviewed; 696 AA.
AC O00461;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Golgi integral membrane protein 4;
DE AltName: Full=Golgi integral membrane protein, cis;
DE Short=GIMPc;
DE AltName: Full=Golgi phosphoprotein 4;
DE AltName: Full=Golgi-localized phosphoprotein of 130 kDa;
DE Short=Golgi phosphoprotein of 130 kDa;
GN Name=GOLIM4; Synonyms=GIMPC, GOLPH4, GPP130;
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], SUBCELLULAR LOCATION, PHOSPHORYLATION,
RP GLYCOSYLATION, AND TOPOLOGY.
RC TISSUE=Small intestine;
RX PubMed=9201717; DOI=10.1091/mbc.8.6.1073;
RA Linstedt A.D., Mehta A., Suhan J., Reggio H., Hauri H.-P.;
RT "Sequence and overexpression of GPP130/GIMPc: evidence for saturable pH-
RT sensitive targeting of a type II early Golgi membrane protein.";
RL Mol. Biol. Cell 8:1073-1087(1997).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=11598199; DOI=10.1091/mbc.12.10.3152;
RA Bachert C., Lee T.H., Linstedt A.D.;
RT "Lumenal endosomal and Golgi-retrieval determinants involved in pH-
RT sensitive targeting of an early Golgi protein.";
RL Mol. Biol. Cell 12:3152-3160(2001).
RN [3]
RP FUNCTION.
RX PubMed=15331763; DOI=10.1091/mbc.e04-05-0366;
RA Natarajan R., Linstedt A.D.;
RT "A cycling cis-Golgi protein mediates endosome-to-Golgi traffic.";
RL Mol. Biol. Cell 15:4798-4806(2004).
RN [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364; SER-538; TYR-613 AND
RP THR-626, AND IDENTIFICATION BY 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 [7]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-312.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Plays a role in endosome to Golgi protein trafficking;
CC mediates protein transport along the late endosome-bypass pathway from
CC the early endosome to the Golgi. {ECO:0000269|PubMed:15331763}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC pass type II membrane protein. Endosome membrane; Single-pass type II
CC membrane protein. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC Note=Localizes to cis and medial Golgi cisternae. Probably cycles
CC between early Golgi and distal compartments like endosome.
CC -!- PTM: Phosphorylated probably by c-AMP-dependent kinases in its lumenal
CC part. {ECO:0000269|PubMed:9201717}.
CC -!- PTM: O-glycosylated; modified by sialic acid residues. {ECO:0000250}.
CC -!- PTM: N-glycosylated; N-glycans are probably of the complex type and
CC modified by sialic acid residues. {ECO:0000269|PubMed:9201717}.
CC -!- SIMILARITY: Belongs to the GOLIM4 family. {ECO:0000305}.
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DR EMBL; U55853; AAB58419.1; -; mRNA.
DR CCDS; CCDS3204.1; -.
DR RefSeq; NP_055313.1; NM_014498.4.
DR AlphaFoldDB; O00461; -.
DR SMR; O00461; -.
DR BioGRID; 118146; 94.
DR DIP; DIP-61898N; -.
DR IntAct; O00461; 58.
DR MINT; O00461; -.
DR STRING; 9606.ENSP00000417354; -.
DR GlyGen; O00461; 7 sites, 3 O-linked glycans (6 sites).
DR iPTMnet; O00461; -.
DR PhosphoSitePlus; O00461; -.
DR SwissPalm; O00461; -.
DR BioMuta; GOLIM4; -.
DR EPD; O00461; -.
DR jPOST; O00461; -.
DR MassIVE; O00461; -.
DR MaxQB; O00461; -.
DR PaxDb; O00461; -.
DR PeptideAtlas; O00461; -.
DR PRIDE; O00461; -.
DR ProteomicsDB; 47911; -.
DR Antibodypedia; 952; 126 antibodies from 20 providers.
DR DNASU; 27333; -.
DR Ensembl; ENST00000470487.6; ENSP00000417354.1; ENSG00000173905.9.
DR GeneID; 27333; -.
DR KEGG; hsa:27333; -.
DR MANE-Select; ENST00000470487.6; ENSP00000417354.1; NM_014498.5; NP_055313.1.
DR UCSC; uc003ffe.3; human.
DR CTD; 27333; -.
DR DisGeNET; 27333; -.
DR GeneCards; GOLIM4; -.
DR HGNC; HGNC:15448; GOLIM4.
DR HPA; ENSG00000173905; Low tissue specificity.
DR MIM; 606805; gene.
DR neXtProt; NX_O00461; -.
DR OpenTargets; ENSG00000173905; -.
DR PharmGKB; PA162390001; -.
DR VEuPathDB; HostDB:ENSG00000173905; -.
DR eggNOG; ENOG502R4Q5; Eukaryota.
DR GeneTree; ENSGT00390000004096; -.
DR HOGENOM; CLU_030773_0_0_1; -.
DR InParanoid; O00461; -.
DR OMA; GDHRNDA; -.
DR OrthoDB; 619770at2759; -.
DR PhylomeDB; O00461; -.
DR TreeFam; TF333101; -.
DR PathwayCommons; O00461; -.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR SignaLink; O00461; -.
DR BioGRID-ORCS; 27333; 10 hits in 1072 CRISPR screens.
DR ChiTaRS; GOLIM4; human.
DR GenomeRNAi; 27333; -.
DR Pharos; O00461; Tbio.
DR PRO; PR:O00461; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O00461; protein.
DR Bgee; ENSG00000173905; Expressed in tendon of biceps brachii and 198 other tissues.
DR ExpressionAtlas; O00461; baseline and differential.
DR Genevisible; O00461; HS.
DR GO; GO:0005801; C:cis-Golgi network; TAS:ProtInc.
DR GO; GO:0030139; C:endocytic vesicle; TAS:ProtInc.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005796; C:Golgi lumen; TAS:ProtInc.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR InterPro; IPR042336; GOLIM4.
DR PANTHER; PTHR22909; PTHR22909; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endosome; Glycoprotein; Golgi apparatus; Lipoprotein;
KW Membrane; Myristate; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..696
FT /note="Golgi integral membrane protein 4"
FT /id="PRO_0000285097"
FT TOPO_DOM 2..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..696
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 38..107
FT /note="Golgi targeting"
FT REGION 80..175
FT /note="Endosome targeting"
FT REGION 122..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..248
FT /note="Golgi targeting"
FT REGION 244..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 35..244
FT /evidence="ECO:0000255"
FT COMPBIAS 252..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..573
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..623
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 613
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 626
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 673
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BXA1"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 312
FT /note="A -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036611"
SQ SEQUENCE 696 AA; 81880 MW; A3BA9AE3D52F7174 CRC64;
MGNGMCSRKQ KRIFQTLLLL TVVFGFLYGA MLYYELQTQL RKAEAVALKY QQHQESLSAQ
LQVVYEHRSR LEKSLQKERL EHKKAKEDFL VYKLEAQETL NKGRQDSNSR YSALNVQHQM
LKSQHEELKK QHSDLEEEHR KQGEDFSRTF NDHKQKYLQL QQEKEQELSK LKETVYNLRE
ENRQLRKAHQ DIHTQLQDVK QQHKNLLSEH EQLVVTLEDH KSALAAAQTQ VAEYKQLKDT
LNRIPSLRKP DPAEQQNVTQ VAHSPQGYNT AREKPTREVQ EVSRNNDVWQ NHEAVPGRAE
DTKLYAPTHK EAEFQAPPEP IQQEVERREP EEHQVEEEHR KALEEEEMEQ VGQAEHLEEE
HDPSPEEQDR EWKEQHEQRE AANLLEGHAR AEVYPSAKPM IKFQSPYEEQ LEQQRLAVQQ
VEEAQQLREH QEALHQQRLQ GHLLRQQEQQ QQQVAREMAL QRQAELEEGR PQHQEQLRQQ
AHYDAMDNDI VQGAEDQGIQ GEEGAYERDN QHQDEAEGDP GNRHEPREQG PREADPESEA
DRAAVEDINP ADDPNNQGED EFEEAEQVRE ENLPDENEEQ KQSNQKQENT EVEEHLVMAG
NPDQQEDNVD EQYQEEAEEE VQEDLTEEKK RELEHNAEET YGENDENTDD KNNDGEEQEV
RDDNRPKGRE EHYEEEEEEE EDGAAVAEKS HRRAEM
