F189B_HUMAN
ID F189B_HUMAN Reviewed; 668 AA.
AC P81408; B1AVS5; Q8IXL3; Q9BR66;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein FAM189B;
DE AltName: Full=Protein COTE1;
GN Name=FAM189B; Synonyms=C1orf2, COTE1;
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 [GENOMIC DNA] (ISOFORM 3).
RC TISSUE=Hippocampus;
RX PubMed=9331372; DOI=10.1101/gr.7.10.1020;
RA Winfield S.L., Tayebi N., Martin B.M., Ginns E.I., Sidransky E.;
RT "Identification of three additional genes contiguous to the
RT glucocerebrosidase locus on chromosome 1q21: implications for Gaucher
RT disease.";
RL Genome Res. 7:1020-1026(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; B AND 2).
RC TISSUE=Brain, Lymph, and Pancreas;
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 INTERACTION WITH WWOX.
RX PubMed=15064722; DOI=10.1038/sj.onc.1207680;
RA Ludes-Meyers J.H., Kil H., Bednarek A.K., Drake J., Bedford M.T.,
RA Aldaz C.M.;
RT "WWOX binds the specific proline-rich ligand PPXY: identification of
RT candidate interacting proteins.";
RL Oncogene 23:5049-5055(2004).
RN [6]
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-389; SER-493 AND
RP SER-574, AND 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 [8]
RP 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 [9]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-358.
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 -!- SUBUNIT: May interact with WWOX.
CC -!- INTERACTION:
CC P81408; Q9NZC7: WWOX; NbExp=2; IntAct=EBI-6366314, EBI-4320739;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A;
CC IsoId=P81408-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P81408-2; Sequence=VSP_038926;
CC Name=2;
CC IsoId=P81408-3; Sequence=VSP_046728, VSP_046729;
CC Name=3;
CC IsoId=P81408-4; Sequence=VSP_046729;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the FAM189 family. {ECO:0000305}.
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DR EMBL; AF023268; AAC51822.1; -; Genomic_DNA.
DR EMBL; AL713999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53094.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53097.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53098.1; -; Genomic_DNA.
DR EMBL; BC040136; AAH40136.2; -; mRNA.
DR EMBL; BC006493; AAH06493.1; -; mRNA.
DR EMBL; BC007444; AAH07444.1; -; mRNA.
DR EMBL; BC010471; AAH10471.1; -; mRNA.
DR EMBL; BC033707; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS1103.1; -. [P81408-1]
DR CCDS; CCDS1104.1; -. [P81408-2]
DR CCDS; CCDS58035.1; -. [P81408-3]
DR PIR; T08827; T08827.
DR RefSeq; NP_001254537.1; NM_001267608.1. [P81408-3]
DR RefSeq; NP_006580.2; NM_006589.2. [P81408-1]
DR RefSeq; NP_937995.1; NM_198264.1. [P81408-2]
DR RefSeq; XP_005244902.1; XM_005244845.1. [P81408-4]
DR AlphaFoldDB; P81408; -.
DR BioGRID; 115938; 127.
DR IntAct; P81408; 76.
DR MINT; P81408; -.
DR STRING; 9606.ENSP00000354958; -.
DR GlyGen; P81408; 1 site.
DR iPTMnet; P81408; -.
DR PhosphoSitePlus; P81408; -.
DR BioMuta; FAM189B; -.
DR DMDM; 294862432; -.
DR jPOST; P81408; -.
DR MassIVE; P81408; -.
DR MaxQB; P81408; -.
DR PaxDb; P81408; -.
DR PeptideAtlas; P81408; -.
DR PRIDE; P81408; -.
DR ProteomicsDB; 3358; -.
DR ProteomicsDB; 57695; -. [P81408-1]
DR ProteomicsDB; 57696; -. [P81408-2]
DR Antibodypedia; 1675; 81 antibodies from 15 providers.
DR DNASU; 10712; -.
DR Ensembl; ENST00000350210.6; ENSP00000307128.4; ENSG00000160767.22. [P81408-2]
DR Ensembl; ENST00000361361.7; ENSP00000354958.2; ENSG00000160767.22. [P81408-1]
DR Ensembl; ENST00000368368.7; ENSP00000357352.3; ENSG00000160767.22. [P81408-3]
DR Ensembl; ENST00000572488.5; ENSP00000458501.1; ENSG00000262666.5. [P81408-3]
DR Ensembl; ENST00000574749.5; ENSP00000460960.1; ENSG00000262666.5. [P81408-2]
DR Ensembl; ENST00000575430.5; ENSP00000461152.1; ENSG00000262666.5. [P81408-1]
DR GeneID; 10712; -.
DR KEGG; hsa:10712; -.
DR MANE-Select; ENST00000361361.7; ENSP00000354958.2; NM_006589.3; NP_006580.2.
DR UCSC; uc001fjm.4; human. [P81408-1]
DR CTD; 10712; -.
DR DisGeNET; 10712; -.
DR GeneCards; FAM189B; -.
DR HGNC; HGNC:1233; FAM189B.
DR HPA; ENSG00000160767; Low tissue specificity.
DR MIM; 619447; gene.
DR neXtProt; NX_P81408; -.
DR OpenTargets; ENSG00000160767; -.
DR PharmGKB; PA25608; -.
DR VEuPathDB; HostDB:ENSG00000160767; -.
DR eggNOG; ENOG502RB7D; Eukaryota.
DR GeneTree; ENSGT00530000063335; -.
DR HOGENOM; CLU_025607_0_0_1; -.
DR InParanoid; P81408; -.
DR OMA; TARSCHR; -.
DR OrthoDB; 608892at2759; -.
DR PhylomeDB; P81408; -.
DR TreeFam; TF332736; -.
DR PathwayCommons; P81408; -.
DR SignaLink; P81408; -.
DR BioGRID-ORCS; 10712; 19 hits in 1084 CRISPR screens.
DR ChiTaRS; FAM189B; human.
DR GenomeRNAi; 10712; -.
DR Pharos; P81408; Tbio.
DR PRO; PR:P81408; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P81408; protein.
DR Bgee; ENSG00000160767; Expressed in right hemisphere of cerebellum and 96 other tissues.
DR ExpressionAtlas; P81408; baseline and differential.
DR Genevisible; P81408; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050699; F:WW domain binding; IPI:UniProtKB.
DR InterPro; IPR007237; CD20-like.
DR InterPro; IPR030431; FAM189.
DR PANTHER; PTHR17615; PTHR17615; 1.
DR Pfam; PF04103; CD20; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..668
FT /note="Protein FAM189B"
FT /id="PRO_0000079261"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 386..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..490
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 76..171
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038926"
FT VAR_SEQ 76..94
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046728"
FT VAR_SEQ 207
FT /note="T -> TQ (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046729"
FT VARIANT 358
FT /note="S -> F (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035684"
FT VARIANT 549
FT /note="R -> H (in dbSNP:rs2072648)"
FT /id="VAR_037876"
FT VARIANT 646
FT /note="R -> H (in dbSNP:rs2072648)"
FT /id="VAR_056842"
SQ SEQUENCE 668 AA; 71355 MW; E22EED90923826BD CRC64;
MMPSPSDSSR SLTSRPSTRG LTHLRLHRPW LQALLTLGLV QVLLGILVVT FSMVASSVTT
TESIKRSCPS WAGFSLAFSG VVGIVSWKRP FTLVISFFSL LSVLCVMLSM AGSVLSCKNA
QLARDFQQCS LEGKVCVCCP SVPLLRPCPE SGQELKVAPN STCDEARGAL KNLLFSVCGL
TICAAIICTL SAIVCCIQIF SLDLVHTLAP ERSVSGPLGP LGCTSPPPAP LLHTMLDLEE
FVPPVPPPPY YPPEYTCSSE TDAQSITYNG SMDSPVPLYP TDCPPSYEAV MGLRGDSQAT
LFDPQLHDGS CICERVASIV DVSMDSGSLV LSAIGDLPGG SSPSEDSCLL ELQGSVRSVD
YVLFRSIQRS RAGYCLSLDC GLRGPFEESP LPRRPPRAAR SYSCSAPEAP PPLGAPTAAR
SCHRLEGWPP WVGPCFPELR RRVPRGGGRP AAAPPTRAPT RRFSDSSGSL TPPGHRPPHP
ASPPPLLLPR SHSDPGITTS SDTADFRDLY TKVLEEEAAS VSSADTGLCS EACLFRLARC
PSPKLLRARS AEKRRPVPTF QKVPLPSGPA PAHSLGDLKG SWPGRGLVTR FLQISRKAPD
PSGTGAHGHK QVPRSLWGRP GRESLHLRSC GDLSSSSSLR RLLSGRRLER GTRPHSLSLN
GGSRETGL
