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   24-JAN-2024, entry version 155.
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; 24.
DR   DIP; DIP-47295N; -.
DR   IntAct; Q9NXG0; 12.
DR   MINT; Q9NXG0; -.
DR   STRING; 9606.ENSP00000370021; -.
DR   CarbonylDB; Q9NXG0; -.
DR   GlyGen; Q9NXG0; 2 sites, 1 O-linked glycan (2 sites).
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; 9606-ENSP00000370021; -.
DR   PeptideAtlas; Q9NXG0; -.
DR   ProteomicsDB; 83091; -. [Q9NXG0-1]
DR   ProteomicsDB; 83092; -. [Q9NXG0-2]
DR   ProteomicsDB; 83093; -. [Q9NXG0-3]
DR   Pumba; Q9NXG0; -.
DR   Antibodypedia; 24606; 95 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   AGR; HGNC:23432; -.
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; EYFTIMK; -.
DR   OrthoDB; 2913664at2759; -.
DR   PhylomeDB; Q9NXG0; -.
DR   TreeFam; TF329190; -.
DR   PathwayCommons; Q9NXG0; -.
DR   SignaLink; Q9NXG0; -.
DR   BioGRID-ORCS; 54875; 15 hits in 1157 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 125 other cell types or tissues.
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; CENTLEIN; 1.
DR   PANTHER; PTHR18957:SF0; CENTLEIN; 1.
DR   Genevisible; Q9NXG0; HS.
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
//