CNTLN_HUMAN
ID CNTLN_HUMAN Reviewed; 1405 AA.
AC Q9NXG0; A5Z2X6; Q5VYJ0; Q8N1G9; Q9HAJ5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 6.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Centlein;
DE AltName: Full=Centrosomal protein;
GN Name=CNTLN; Synonyms=C9orf101, C9orf39;
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] (ISOFORMS 2 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 278-1405 (ISOFORM 1), AND VARIANT ILE-695.
RC TISSUE=Embryo, and Gastric mucosa;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP 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 [4]
RP FUNCTION, INTERACTION WITH CEP250; NEK2 AND CEP68, SUBCELLULAR LOCATION,
RP AND PHOSPHORYLATION.
RX PubMed=24554434; DOI=10.1242/jcs.139451;
RA Fang G., Zhang D., Yin H., Zheng L., Bi X., Yuan L.;
RT "Centlein mediates an interaction between C-Nap1 and Cep68 to maintain
RT centrosome cohesion.";
RL J. Cell Sci. 127:1631-1639(2014).
CC -!- FUNCTION: Required for centrosome cohesion and recruitment of CEP68 to
CC centrosomes. {ECO:0000269|PubMed:24554434}.
CC -!- SUBUNIT: Interacts with CEP250 and CEP68. Interacts with NEK2; the
CC interaction leads to phosphorylation of CNTLN.
CC {ECO:0000269|PubMed:24554434}.
CC -!- INTERACTION:
CC Q9NXG0-2; Q8IYD9: LAS2; NbExp=3; IntAct=EBI-9640137, EBI-749878;
CC Q9NXG0-2; A0A024R275: RFK; NbExp=3; IntAct=EBI-9640137, EBI-13040992;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:24554434}.
CC Note=Colocalizes with gamma-tubulin during interphase and mitosis.
CC Appears to associate with the mother centriole during G1 phase and with
CC daughter centrioles towards G1/S phase (By similarity). Localizes to
CC the proximal ends of the centrioles (PubMed:24554434). Levels are high
CC at interphase centrosomes but are reduced on mitotic spindle poles
CC (PubMed:24554434). {ECO:0000250|UniProtKB:A9ZSY0,
CC ECO:0000269|PubMed:24554434}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NXG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NXG0-2; Sequence=VSP_017558;
CC Name=3;
CC IsoId=Q9NXG0-3; Sequence=VSP_032864, VSP_032865;
CC -!- PTM: Phosphorylated directly or indirectly by NEK2.
CC {ECO:0000269|PubMed:24554434}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91052.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB13850.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK000283; BAA91052.1; ALT_INIT; mRNA.
DR EMBL; AK021596; BAB13850.1; ALT_INIT; mRNA.
DR EMBL; AK098502; BAC05319.1; -; mRNA.
DR EMBL; AL133214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS43789.1; -. [Q9NXG0-2]
DR CCDS; CCDS47953.1; -. [Q9NXG0-3]
DR RefSeq; NP_001107867.1; NM_001114395.2. [Q9NXG0-3]
DR RefSeq; NP_060208.2; NM_017738.3. [Q9NXG0-2]
DR AlphaFoldDB; Q9NXG0; -.
DR SMR; Q9NXG0; -.
DR BioGRID; 120223; 20.
DR DIP; DIP-47295N; -.
DR IntAct; Q9NXG0; 12.
DR MINT; Q9NXG0; -.
DR STRING; 9606.ENSP00000370021; -.
DR CarbonylDB; Q9NXG0; -.
DR iPTMnet; Q9NXG0; -.
DR PhosphoSitePlus; Q9NXG0; -.
DR BioMuta; CNTLN; -.
DR DMDM; 317373585; -.
DR EPD; Q9NXG0; -.
DR jPOST; Q9NXG0; -.
DR MassIVE; Q9NXG0; -.
DR MaxQB; Q9NXG0; -.
DR PaxDb; Q9NXG0; -.
DR PeptideAtlas; Q9NXG0; -.
DR PRIDE; Q9NXG0; -.
DR ProteomicsDB; 83091; -. [Q9NXG0-1]
DR ProteomicsDB; 83092; -. [Q9NXG0-2]
DR ProteomicsDB; 83093; -. [Q9NXG0-3]
DR Antibodypedia; 24606; 87 antibodies from 16 providers.
DR DNASU; 54875; -.
DR Ensembl; ENST00000380641.4; ENSP00000370015.3; ENSG00000044459.15. [Q9NXG0-3]
DR Ensembl; ENST00000380647.8; ENSP00000370021.3; ENSG00000044459.15. [Q9NXG0-2]
DR GeneID; 54875; -.
DR KEGG; hsa:54875; -.
DR MANE-Select; ENST00000380647.8; ENSP00000370021.3; NM_017738.4; NP_060208.2. [Q9NXG0-2]
DR UCSC; uc003zmx.6; human. [Q9NXG0-1]
DR CTD; 54875; -.
DR DisGeNET; 54875; -.
DR GeneCards; CNTLN; -.
DR HGNC; HGNC:23432; CNTLN.
DR HPA; ENSG00000044459; Low tissue specificity.
DR MIM; 611870; gene.
DR neXtProt; NX_Q9NXG0; -.
DR OpenTargets; ENSG00000044459; -.
DR PharmGKB; PA162382646; -.
DR VEuPathDB; HostDB:ENSG00000044459; -.
DR eggNOG; ENOG502QRVC; Eukaryota.
DR GeneTree; ENSGT00440000034932; -.
DR HOGENOM; CLU_006488_1_0_1; -.
DR InParanoid; Q9NXG0; -.
DR OMA; MSNMFEN; -.
DR OrthoDB; 846281at2759; -.
DR PhylomeDB; Q9NXG0; -.
DR TreeFam; TF329190; -.
DR PathwayCommons; Q9NXG0; -.
DR SignaLink; Q9NXG0; -.
DR BioGRID-ORCS; 54875; 14 hits in 1077 CRISPR screens.
DR ChiTaRS; CNTLN; human.
DR GeneWiki; CNTLN; -.
DR GenomeRNAi; 54875; -.
DR Pharos; Q9NXG0; Tbio.
DR PRO; PR:Q9NXG0; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9NXG0; protein.
DR Bgee; ENSG00000044459; Expressed in buccal mucosa cell and 124 other tissues.
DR Genevisible; Q9NXG0; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:UniProtKB.
DR GO; GO:0010457; P:centriole-centriole cohesion; IMP:UniProtKB.
DR GO; GO:0033365; P:protein localization to organelle; IMP:UniProtKB.
DR InterPro; IPR038810; CNTLN.
DR PANTHER; PTHR18957; PTHR18957; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:A2AM05"
FT CHAIN 2..1405
FT /note="Centlein"
FT /id="PRO_0000227567"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 95..126
FT /evidence="ECO:0000255"
FT COILED 613..655
FT /evidence="ECO:0000255"
FT COILED 681..793
FT /evidence="ECO:0000255"
FT COILED 980..1311
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:A2AM05"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AM05"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1343
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A2AM05"
FT VAR_SEQ 383..391
FT /note="LYNELHICF -> VCFYSVIKM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032864"
FT VAR_SEQ 392..1405
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032865"
FT VAR_SEQ 1374..1405
FT /note="SLTLSPRLKCNGAIVAHQNLRLPDSSSSASAS -> LPFASYLLEAVLEKIN
FT EKKKLVEGYFTIMKDIR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_017558"
FT VARIANT 284
FT /note="T -> A (in dbSNP:rs3808795)"
FT /id="VAR_056840"
FT VARIANT 291
FT /note="E -> D (in dbSNP:rs3808794)"
FT /id="VAR_056841"
FT VARIANT 562
FT /note="R -> C (in dbSNP:rs3808782)"
FT /id="VAR_025608"
FT VARIANT 695
FT /note="T -> I (in dbSNP:rs7035276)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_025609"
FT VARIANT 1376
FT /note="T -> A (in dbSNP:rs2499057)"
FT /id="VAR_025610"
FT CONFLICT 700
FT /note="R -> Q (in Ref. 1; BAB13850)"
FT /evidence="ECO:0000305"
FT CONFLICT 871
FT /note="Missing (in Ref. 1; BAB13850)"
FT /evidence="ECO:0000305"
FT CONFLICT 1004
FT /note="T -> A (in Ref. 1; BAB13850)"
FT /evidence="ECO:0000305"
FT CONFLICT 1240
FT /note="A -> V (in Ref. 1; BAB13850)"
FT /evidence="ECO:0000305"
FT CONFLICT 1388
FT /note="V -> M (in Ref. 1; BAA91052)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1405 AA; 161571 MW; 6170160F6995E843 CRC64;
MAARSPPSPH PSPPARQLGP RSPRVGRGAE VHAMRSEASG FAGAAREVVA DESDKIWVGE
EGSGGRRGPG GAAPAHAPLL SAPMGSRRLE GISVEEAMVT RTQLLEEELS SLKEELALCQ
ADKEFVWSLW KRLQVTNPDL TQVVSLVVER EKQKSEAKDR KVLEILQVKD AKIQEFEQRE
SVLKQEINDL VKRKIAVDEE NAFLRKEFSD LEKKFKDKSQ EIKDTKECVQ NKEEQNRLVI
KNLEEENKKL STRCTDLLND LEKLRKQEAH LRKEKYSTDA KIKTFEDNLI EARKEVEVSQ
SKYNALSLQL SNKQTELIQK DMDITLVRKE LQELQNLYKQ NSTHTAQQAE LIQQLQVLNM
DTQKVLRNQE DVHTAESISY QKLYNELHIC FETTKSNEAM LRQSVTNLQD QLLQKEQENA
KLKEKLQESQ GAPLPLPQES DPDYSAQVPH RPSLSSLETL MVSQKSEIEY LQEKLKIANE
KLSENISANK GFSRKSIMTS AEGKHKEPPV KRSRSLSPKS SFTDSEELQK LRKAERKIEN
LEKALQLKSQ ENDELRDAHE KRKERLQMLQ TNYRAVKEQL KQWEEGSGMT EIRKIKRADP
QQLRQEDSDA VWNELAYFKR ENQELMIQKM NLEEELDELK VHISIDKAAI QELNRCVAER
REEQLFRSGE DDEVKRSTPE KNGKEMLEQT LQKVTELENR LKSFEKRSRK LKEGNKKLMK
ENDFLKSLLK QQQEDTETRE KELEQIIKGS KDVEKENTEL QVKISELETE VTSLRRQVAE
ANALRNENEE LINPMEKSHQ SADRAKSEMA TMKVRSGRYD CKTTMTKVKF KAAKKNCSVG
RHHTVLNHSI KVMSNVFENL SKDGWEDVSE SSSDSEAQTS QTLGTIIVET SQKISPTEDG
KDQKESDPTE DSQTQGKEIV QTYLNIDGKT PKDYFHDKNA KKPTFQKKNC KMQKSSHTAV
PTRVNREKYK NITAQKSSSN IILLRERIIS LQQQNSVLQN AKKTAELSVK EYKEVNEKLL
HQQQVSDQRF QTSRQTIKKL NLDLAGLRKE KEDLLKKLES SSEITSLAEE NSQVTFPRIQ
VTSLSPSRSM DLEMKQLQYK LKNATNELTK QSSNVKTLKF ELLAKEEHIK EMHEKISRME
RDITMKRHLI EDLKFRQKVN LESNKSFSEM LQNLDKKVKT LTEECSNKKV SIDSLKQRLN
VAVKEKSQYE QMYQKSKEEL EKKDLKLTLL VSRISETESA MAEIETAASK QLQELALQSE
QVLEGAQKTL LLANEKVEEF TTFVKALAKE LQNDVHVVRR QIRELKKMKK NRDACKTSTH
KAQTLAASIL NISRSDLEEI LDTEDQVEIE KTKIDAENDK EWMLYIQKLL EGQSLTLSPR
LKCNGAIVAH QNLRLPDSSS SASAS
