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GOLM2_HUMAN
ID   GOLM2_HUMAN             Reviewed;         436 AA.
AC   Q6P4E1; B4DPZ6; G5E934; Q6UY45; Q96EM1;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Protein GOLM2 {ECO:0000305};
DE   AltName: Full=Cancer susceptibility candidate gene 4 protein;
DE            Short=CASC4;
DE   AltName: Full=Golgi membrane protein 2 {ECO:0000305};
GN   Name=GOLM2 {ECO:0000312|HGNC:HGNC:24892}; Synonyms=CASC4;
GN   ORFNames=UNQ2573/PRO6308;
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).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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 MRNA] (ISOFORM 4).
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 GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Blood, and Kidney;
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP   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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332 AND SER-366, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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-233; SER-275; SER-328;
RP   SER-332 AND SER-366, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   ACETYLATION AT MET-1.
RX   PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053;
RA   Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I.,
RA   Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S.,
RA   Ziegler M., Niere M., Gevaert K., Arnesen T.;
RT   "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N
RT   termini of transmembrane proteins and maintains Golgi integrity.";
RL   Cell Rep. 10:1362-1374(2015).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=4;
CC         IsoId=Q6P4E1-4; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P4E1-2; Sequence=VSP_060181;
CC       Name=3;
CC         IsoId=Q6P4E1-3; Sequence=VSP_060179, VSP_060180;
CC       Name=5;
CC         IsoId=Q6P4E1-5; Sequence=VSP_060178;
CC   -!- SIMILARITY: Belongs to the GOLM family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH63480.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR   EMBL; AY358086; AAQ88453.1; -; mRNA.
DR   EMBL; AK298564; BAG60758.1; -; mRNA.
DR   EMBL; AL832333; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC025043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471082; EAW77258.1; -; Genomic_DNA.
DR   EMBL; BC012124; AAH12124.1; -; mRNA.
DR   EMBL; BC063480; AAH63480.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS10108.1; -. [Q6P4E1-4]
DR   CCDS; CCDS10109.1; -. [Q6P4E1-2]
DR   RefSeq; NP_612432.2; NM_138423.3. [Q6P4E1-4]
DR   RefSeq; NP_816929.1; NM_177974.2. [Q6P4E1-2]
DR   AlphaFoldDB; Q6P4E1; -.
DR   SMR; Q6P4E1; -.
DR   BioGRID; 125233; 41.
DR   IntAct; Q6P4E1; 10.
DR   MINT; Q6P4E1; -.
DR   STRING; 9606.ENSP00000299957; -.
DR   GlyConnect; 1652; 4 N-Linked glycans (1 site).
DR   GlyGen; Q6P4E1; 11 sites, 3 N-linked glycans (1 site), 3 O-linked glycans (6 sites).
DR   iPTMnet; Q6P4E1; -.
DR   PhosphoSitePlus; Q6P4E1; -.
DR   BioMuta; CASC4; -.
DR   DMDM; 74737334; -.
DR   EPD; Q6P4E1; -.
DR   jPOST; Q6P4E1; -.
DR   MassIVE; Q6P4E1; -.
DR   MaxQB; Q6P4E1; -.
DR   PaxDb; Q6P4E1; -.
DR   PeptideAtlas; Q6P4E1; -.
DR   PRIDE; Q6P4E1; -.
DR   ProteomicsDB; 33815; -.
DR   ProteomicsDB; 66964; -. [Q6P4E1-2]
DR   ProteomicsDB; 66965; -. [Q6P4E1-3]
DR   Antibodypedia; 55771; 89 antibodies from 18 providers.
DR   DNASU; 113201; -.
DR   Ensembl; ENST00000299957.11; ENSP00000299957.6; ENSG00000166734.20. [Q6P4E1-4]
DR   Ensembl; ENST00000345795.6; ENSP00000335063.4; ENSG00000166734.20. [Q6P4E1-2]
DR   Ensembl; ENST00000557945.5; ENSP00000453720.1; ENSG00000166734.20. [Q6P4E1-3]
DR   GeneID; 113201; -.
DR   KEGG; hsa:113201; -.
DR   MANE-Select; ENST00000299957.11; ENSP00000299957.6; NM_138423.4; NP_612432.2.
DR   UCSC; uc001ztp.4; human. [Q6P4E1-4]
DR   CTD; 113201; -.
DR   DisGeNET; 113201; -.
DR   GeneCards; GOLM2; -.
DR   HGNC; HGNC:24892; GOLM2.
DR   HPA; ENSG00000166734; Low tissue specificity.
DR   neXtProt; NX_Q6P4E1; -.
DR   OpenTargets; ENSG00000166734; -.
DR   VEuPathDB; HostDB:ENSG00000166734; -.
DR   eggNOG; ENOG502QTYH; Eukaryota.
DR   GeneTree; ENSGT00530000063675; -.
DR   HOGENOM; CLU_129925_0_0_1; -.
DR   InParanoid; Q6P4E1; -.
DR   OMA; ERGPGLH; -.
DR   OrthoDB; 913812at2759; -.
DR   PhylomeDB; Q6P4E1; -.
DR   TreeFam; TF331127; -.
DR   PathwayCommons; Q6P4E1; -.
DR   SignaLink; Q6P4E1; -.
DR   BioGRID-ORCS; 113201; 15 hits in 1080 CRISPR screens.
DR   ChiTaRS; CASC4; human.
DR   GenomeRNAi; 113201; -.
DR   Pharos; Q6P4E1; Tbio.
DR   PRO; PR:Q6P4E1; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q6P4E1; protein.
DR   Bgee; ENSG00000166734; Expressed in calcaneal tendon and 186 other tissues.
DR   ExpressionAtlas; Q6P4E1; baseline and differential.
DR   Genevisible; Q6P4E1; HS.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR026141; CASC4.
DR   InterPro; IPR026139; GOLM1/CASC4.
DR   PANTHER; PTHR15896; PTHR15896; 1.
DR   PANTHER; PTHR15896:SF11; PTHR15896:SF11; 1.
DR   PRINTS; PR02084; GOLM1CASC4.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Membrane; Phosphoprotein;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..436
FT                   /note="Protein GOLM2"
FT                   /id="PRO_0000291843"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..436
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          225..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          35..198
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        225..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..421
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:25732826,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         275
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         332
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         366
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         1..22
FT                   /note="MVGFGANRRAGRLPSLVLVVLL -> M (in isoform 5)"
FT                   /id="VSP_060178"
FT   VAR_SEQ         163..177
FT                   /note="FQCGQQMKELRAQHE -> KRPKRFNQMMERNWI (in isoform 3)"
FT                   /id="VSP_060179"
FT   VAR_SEQ         178..436
FT                   /note="Missing (in isoform 3)"
FT                   /id="VSP_060180"
FT   VAR_SEQ         358..414
FT                   /note="SRFFDENESPVDPQHGSKLADYNGDDGNVGEYEADKQAELAYNEEEDGDGGE
FT                   EDVQD -> N (in isoform 2)"
FT                   /id="VSP_060181"
FT   CONFLICT        429
FT                   /note="K -> E (in Ref. 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   436 AA;  49498 MW;  E11DABFDD27CF70A CRC64;
     MVGFGANRRA GRLPSLVLVV LLVVIVVLAF NYWSISSRHV LLQEEVAELQ GQVQRTEVAR
     GRLEKRNSDL LLLVDTHKKQ IDQKEADYGR LSSRLQAREG LGKRCEDDKV KLQNNISYQM
     ADIHHLKEQL AELRQEFLRQ EDQLQDYRKN NTYLVKRLEY ESFQCGQQMK ELRAQHEENI
     KKLADQFLEE QKQETQKIQS NDGKELDINN QVVPKNIPKV AENVADKNEE PSSNHIPHGK
     EQIKRGGDAG MPGIEENDLA KVDDLPPALR KPPISVSQHE SHQAISHLPT GQPLSPNMPP
     DSHINHNGNP GTSKQNPSSP LQRLIPGSNL DSEPRIQTDI LKQATKDRVS DFHKLKQSRF
     FDENESPVDP QHGSKLADYN GDDGNVGEYE ADKQAELAYN EEEDGDGGEE DVQDDEEREL
     QMDPADYGKQ HFNDVL
 
 
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