CE162_HUMAN
ID CE162_HUMAN Reviewed; 1403 AA.
AC Q5TB80; A6PVL7; A6PVL8; Q6P475; Q9Y2L2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Centrosomal protein of 162 kDa;
DE Short=Cep162;
DE AltName: Full=Protein QN1 homolog;
GN Name=CEP162; Synonyms=C6orf84, KIAA1009, QN1;
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=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11521196; DOI=10.1038/sj.onc.1204650;
RA Munnia A., Schuetz N., Romeike B.F.M., Maldener E., Glass B., Maas R.,
RA Nastainczyk W., Feiden W., Fischer U., Meese E.;
RT "Expression, cellular distribution and protein binding of the glioma
RT amplified sequence (GAS41), a highly conserved putative transcription
RT factor.";
RL Oncogene 20:4853-4863(2001).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16302001; DOI=10.1038/sj.onc.1209215;
RA Leon A., Omri B., Gely A., Klein C., Crisanti P.;
RT "QN1/KIAA1009: a new essential protein for chromosome segregation and
RT mitotic spindle assembly.";
RL Oncogene 25:1887-1895(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474 AND SER-475, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CEP290.
RX PubMed=23644468; DOI=10.1038/ncb2739;
RA Wang W.J., Tay H.G., Soni R., Perumal G.S., Goll M.G., Macaluso F.P.,
RA Asara J.M., Amack J.D., Bryan Tsou M.F.;
RT "CEP162 is an axoneme-recognition protein promoting ciliary transition zone
RT assembly at the cilia base.";
RL Nat. Cell Biol. 15:591-601(2013).
CC -!- FUNCTION: Required to promote assembly of the transition zone in
CC primary cilia. Acts by specifically recognizing and binding the
CC axonemal microtubule. Localizes to the distal ends of centrioles before
CC ciliogenesis and directly binds to axonemal microtubule, thereby
CC promoting and restricting transition zone formation specifically at the
CC cilia base. Required to mediate CEP290 association with microtubules.
CC {ECO:0000269|PubMed:23644468}.
CC -!- SUBUNIT: Interacts with CEP290 (PubMed:23644468). Interacts with CPNE4
CC (By similarity). Interacts with alpha-tubulin (By similarity).
CC {ECO:0000250|UniProtKB:Q4KLH6, ECO:0000250|UniProtKB:Q6ZQ06,
CC ECO:0000269|PubMed:23644468}.
CC -!- INTERACTION:
CC Q5TB80; Q8N960: CEP120; NbExp=6; IntAct=EBI-1059012, EBI-2563015;
CC Q5TB80; Q66GS9: CEP135; NbExp=3; IntAct=EBI-1059012, EBI-1046993;
CC Q5TB80; O15078: CEP290; NbExp=7; IntAct=EBI-1059012, EBI-1811944;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole. Cytoplasm, cytoskeleton, spindle.
CC Nucleus. Note=Localizes to the distal end of centrioles throughout the
CC cell cycle. During ciliogenesis, found at the cilia base. Localizes to
CC spindle microtubules during mitosis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5TB80-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5TB80-2; Sequence=VSP_026953;
CC -!- MISCELLANEOUS: Promotes ectopic assembly of transition zone components
CC at cilia tips when targeted outside distal ends of centrioles,
CC generating extra-long cilia with strikingly swollen tips.
CC {ECO:0000305|PubMed:23644468}.
CC -!- SIMILARITY: Belongs to the CEP162 family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to regulate chromosome segregation and
CC mitotic spindle assembly (PubMed:16302001). However, it was later shown
CC that its absence neither affect mitosis nor centriole duplication
CC (PubMed:23644468). {ECO:0000305|PubMed:16302001,
CC ECO:0000305|PubMed:23644468}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76853.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB023226; BAA76853.2; ALT_INIT; mRNA.
DR EMBL; AL138742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS34494.2; -. [Q5TB80-1]
DR CCDS; CCDS69149.1; -. [Q5TB80-2]
DR RefSeq; NP_001273135.1; NM_001286206.1. [Q5TB80-2]
DR RefSeq; NP_055710.2; NM_014895.3. [Q5TB80-1]
DR RefSeq; XP_006715443.1; XM_006715380.2. [Q5TB80-2]
DR RefSeq; XP_016865973.1; XM_017010484.1. [Q5TB80-2]
DR AlphaFoldDB; Q5TB80; -.
DR SMR; Q5TB80; -.
DR BioGRID; 116506; 162.
DR DIP; DIP-50714N; -.
DR IntAct; Q5TB80; 151.
DR MINT; Q5TB80; -.
DR STRING; 9606.ENSP00000385215; -.
DR CarbonylDB; Q5TB80; -.
DR GlyGen; Q5TB80; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5TB80; -.
DR PhosphoSitePlus; Q5TB80; -.
DR BioMuta; CEP162; -.
DR DMDM; 156630849; -.
DR EPD; Q5TB80; -.
DR jPOST; Q5TB80; -.
DR MassIVE; Q5TB80; -.
DR MaxQB; Q5TB80; -.
DR PaxDb; Q5TB80; -.
DR PeptideAtlas; Q5TB80; -.
DR PRIDE; Q5TB80; -.
DR ProteomicsDB; 64890; -. [Q5TB80-1]
DR ProteomicsDB; 64891; -. [Q5TB80-2]
DR Antibodypedia; 31712; 31 antibodies from 7 providers.
DR DNASU; 22832; -.
DR Ensembl; ENST00000257766.8; ENSP00000257766.4; ENSG00000135315.12. [Q5TB80-2]
DR Ensembl; ENST00000403245.8; ENSP00000385215.3; ENSG00000135315.12. [Q5TB80-1]
DR Ensembl; ENST00000617909.1; ENSP00000481760.1; ENSG00000135315.12. [Q5TB80-2]
DR GeneID; 22832; -.
DR KEGG; hsa:22832; -.
DR MANE-Select; ENST00000403245.8; ENSP00000385215.3; NM_014895.4; NP_055710.2.
DR UCSC; uc003pkj.6; human. [Q5TB80-1]
DR CTD; 22832; -.
DR GeneCards; CEP162; -.
DR HGNC; HGNC:21107; CEP162.
DR HPA; ENSG00000135315; Low tissue specificity.
DR MIM; 610201; gene.
DR neXtProt; NX_Q5TB80; -.
DR OpenTargets; ENSG00000135315; -.
DR PharmGKB; PA134972331; -.
DR VEuPathDB; HostDB:ENSG00000135315; -.
DR eggNOG; ENOG502QSPF; Eukaryota.
DR GeneTree; ENSGT00390000009631; -.
DR HOGENOM; CLU_005179_0_0_1; -.
DR InParanoid; Q5TB80; -.
DR OMA; NESRGFD; -.
DR OrthoDB; 520583at2759; -.
DR PhylomeDB; Q5TB80; -.
DR TreeFam; TF330884; -.
DR PathwayCommons; Q5TB80; -.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR SignaLink; Q5TB80; -.
DR BioGRID-ORCS; 22832; 12 hits in 1082 CRISPR screens.
DR ChiTaRS; CEP162; human.
DR GenomeRNAi; 22832; -.
DR Pharos; Q5TB80; Tdark.
DR PRO; PR:Q5TB80; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5TB80; protein.
DR Bgee; ENSG00000135315; Expressed in calcaneal tendon and 164 other tissues.
DR ExpressionAtlas; Q5TB80; baseline and differential.
DR Genevisible; Q5TB80; HS.
DR GO; GO:0005879; C:axonemal microtubule; IDA:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR InterPro; IPR038774; CEP162-like.
DR PANTHER; PTHR34031; PTHR34031; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1403
FT /note="Centrosomal protein of 162 kDa"
FT /id="PRO_0000295628"
FT REGION 18..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 617..670
FT /evidence="ECO:0000255"
FT COILED 698..1121
FT /evidence="ECO:0000255"
FT COILED 1171..1206
FT /evidence="ECO:0000255"
FT COILED 1235..1386
FT /evidence="ECO:0000255"
FT COMPBIAS 173..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQ06"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KLH6"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..76
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032"
FT /id="VSP_026953"
FT VARIANT 266
FT /note="C -> S (in dbSNP:rs17790493)"
FT /id="VAR_033301"
FT VARIANT 272
FT /note="E -> Q (in dbSNP:rs16874323)"
FT /id="VAR_033302"
FT VARIANT 342
FT /note="S -> C (in dbSNP:rs17790493)"
FT /id="VAR_051293"
FT VARIANT 348
FT /note="E -> Q (in dbSNP:rs16874323)"
FT /id="VAR_051294"
FT CONFLICT 168
FT /note="S -> I (in Ref. 1; BAA76853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1403 AA; 161943 MW; 93638BE4BC3A4B29 CRC64;
MANCSQEELD EEFEQFMKEL SDDSFENSDK TARQSKKEMK KKDTVPWWIT EDDFKDDGLL
GTNVSYLKTK KTSQPVMEIE EESAEKIQFL KSSGTSLLST DSLETNELVV SELNHSSLGV
GLDTLEEQEE KEQFFARLEK GLTSSIDYSR LNKELDSNDS THFKALHSNQ ANAELTDDEH
ENESKHEELA ENYSDDFEDE YVGAPLTTKD EEMPSKENSK SEKISVPKQE EEKTGMLANV
VLLDSLDSVA EVNLDEQDKI TPKPRCLPEM TENEMTGTGV SYGQSSSDVE ALHQAYCHIA
HSLGDEDKQK IESNTVEDIK SSVKGHPQEN EENSKNISTM ESDLPTVEEL MKPIRIDSFG
ISGFDLQPVS SEKVAERKET EFFSSLPLKM NPNILSQDSQ HVNLFFDKND ENVILQKTTN
ESMENSCPQV TEVTATEEHV DKMYLNILRK KITVNSSSLS QDDKINKTYR SQLSSEEEGA
VMGKQVPYKK ARSAPPLLKR KPQSGLYASV RSSGYGKPSS PLKMFSTLEK KTSEDIIKSK
NLRSISTSNQ PRKKEILSGT KLIKPAALDK PAHKTESCLS TRKKSENPTE TDSCIQFQTD
SLGYCGENKE KKLLMFKRVQ EAEDKWRGAQ ALIEQIKATF SEKEKELENK LEELKKQQEK
ELFKLNQDNY ILQAKLSSFE ETNKKQRWLH FGEAADPVTG EKLKQIQKEI QEQETLLQGY
QQENERLYNQ VKDLQEQNKK NEERMFKENQ SLFSEVASLK EQMHKSRFLS QVVEDSEPTR
NQNFTDLLAE LRMAQKEKDS LLEDIKRLKQ DKQALEVDFE KMKKERDQAK DQIAYVTGEK
LYEIKILEET HKQEISRLQK RLQWYAENQE LLDKDALRLR EANEEIEKLK LEIEKLKAES
GNPSIRQKIR LKDKAADAKK IQDLERQVKE MEGILKRRYP NSLPALILAA SAAGDTVDKN
TVEFMEKRIK KLEADLEGKD EDAKKSLRTM EQQFQKMKIQ YEQRLEQQEQ LLACKLNQHD
SPRIKALEKE LDDIKEAHQI TVRNLEAEID VLKHQNAELD VKKNDKDDED FQSIEFQVEQ
AHAKAKLVRL NEELAAKKRE IQDLSKTVER LQKDRRMMLS NQNSKGREEM SAKRAKKDVL
HSSKGNANSF PGTLDSKLYQ PHTFTDSHVS EVLQENYRLK NELEGLISEK NELKMKSEAV
MNQFENSMRR VKEDTAAHIA SLKASHQREI EKLLCQNAVE NSSSKVAELN RKIATQEVLI
RHFQSQVNEL QSKQESLVVS EVREEILQKE ITKLLEELRE AKENHTPEMK HFVGLEKKIK
QMEMRHAQRE QELQQIIQQT HQVVETEQNK EVEKWKRLAQ LKNRELEKFR TELDSILDVL
RELHRQGVVV PVAFADEMNA PEY
