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Centrosomal protein of 135 kDa (Cep135) (Centrosomal protein 4)

 CP135_HUMAN             Reviewed;        1140 AA.
Q66GS9; B2RMY0; O75130; Q58F25; Q9H8H7;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
30-AUG-2017, entry version 128.
RecName: Full=Centrosomal protein of 135 kDa;
Short=Cep135;
AltName: Full=Centrosomal protein 4;
Name=CEP135; Synonyms=CEP4, KIAA0635;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 277-1140 (ISOFORM 1).
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[5]
IDENTIFICATION (ISOFORM 1), AND SUBCELLULAR LOCATION [LARGE SCALE
ANALYSIS].
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17681131; DOI=10.1016/j.devcel.2007.07.002;
Kleylein-Sohn J., Westendorf J., Le Clech M., Habedanck R.,
Stierhof Y.-D., Nigg E.A.;
"Plk4-induced centriole biogenesis in human cells.";
Dev. Cell 13:190-202(2007).
[7]
FUNCTION, AND INTERACTION WITH CEP250.
PubMed=18851962; DOI=10.1016/j.yexcr.2008.09.016;
Kim K., Lee S., Chang J., Rhee K.;
"A novel function of CEP135 as a platform protein of C-NAP1 for its
centriolar localization.";
Exp. Cell Res. 314:3692-3700(2008).
[8]
INVOLVEMENT IN MCPH8.
PubMed=22521416; DOI=10.1016/j.ajhg.2012.03.016;
Hussain M.S., Baig S.M., Neumann S., Nurnberg G., Farooq M., Ahmad I.,
Alef T., Hennies H.C., Technau M., Altmuller J., Frommolt P.,
Thiele H., Noegel A.A., Nurnberg P.;
"A truncating mutation of CEP135 causes primary microcephaly and
disturbed centrosomal function.";
Am. J. Hum. Genet. 90:871-878(2012).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-439; SER-688
AND THR-1121, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
FUNCTION.
PubMed=26675238; DOI=10.1242/jcs.179713;
Kurtulmus B., Wang W., Ruppert T., Neuner A., Cerikan B., Viol L.,
Duenas-Sanchez R., Gruss O.J., Pereira G.;
"WDR8 is a centriolar satellite and centriole-associated protein that
promotes ciliary vesicle docking during ciliogenesis.";
J. Cell Sci. 129:621-636(2016).
-!- FUNCTION: Centrosomal protein involved in centriole biogenesis.
Acts as a scaffolding protein during early centriole biogenesis.
Required for the targeting of centriole satellite proteins to
centrosomes such as of PCM1, SSX2IP and CEP290 and recruitment of
WRAP73 to centrioles. Also required for centriole-centriole
cohesion during interphase by acting as a platform protein for
CEP250 at the centriole. {ECO:0000269|PubMed:17681131,
ECO:0000269|PubMed:18851962, ECO:0000269|PubMed:26675238}.
-!- SUBUNIT: Interacts with DCTN2 (By similarity). Interacts with
CEP250 (PubMed:18851962). {ECO:0000250|UniProtKB:Q6P5D4,
ECO:0000269|PubMed:18851962}.
-!- INTERACTION:
Q9HC77:CENPJ; NbExp=8; IntAct=EBI-1046993, EBI-946194;
Q5TB80:CEP162; NbExp=3; IntAct=EBI-1046993, EBI-1059012;
A0A087WUI6:PIBF1; NbExp=3; IntAct=EBI-1046993, EBI-11749468;
Q6UVJ0:SASS6; NbExp=8; IntAct=EBI-1046993, EBI-1570153;
Q8N0Z3:SPICE1; NbExp=4; IntAct=EBI-1046993, EBI-2361917;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome, centriole
{ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:17681131}.
Note=During centriole biogenesis, it is concentrated within the
proximal lumen of both parental centrioles and procentrioles.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q66GS9-1; Sequence=Displayed;
Name=2;
IsoId=Q66GS9-2; Sequence=VSP_012743, VSP_012744;
-!- DISEASE: Microcephaly 8, primary, autosomal recessive (MCPH8)
[MIM:614673]: A disease defined as a head circumference more than
3 standard deviations below the age-related mean. Brain weight is
markedly reduced and the cerebral cortex is disproportionately
small. Despite this marked reduction in size, the gyral pattern is
relatively well preserved, with no major abnormality in cortical
architecture. Affected individuals are mentally retarded. Primary
microcephaly is further defined by the absence of other syndromic
features or significant neurological deficits due to degenerative
brain disorder. {ECO:0000269|PubMed:22521416}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the CEP135/TSGA10 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH12003.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA31610.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; AK023683; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC118280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC110611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC012003; AAH12003.1; ALT_SEQ; mRNA.
EMBL; BC136535; AAI36536.1; -; mRNA.
EMBL; BC136536; AAI36537.1; -; mRNA.
EMBL; AB014535; BAA31610.2; ALT_SEQ; mRNA.
EMBL; BK005586; DAA05590.1; -; mRNA.
CCDS; CCDS33986.1; -. [Q66GS9-1]
RefSeq; NP_079285.2; NM_025009.4. [Q66GS9-1]
UniGene; Hs.518767; -.
PDB; 5FCN; X-ray; 1.80 A; A/B=82-144.
PDBsum; 5FCN; -.
ProteinModelPortal; Q66GS9; -.
SMR; Q66GS9; -.
BioGrid; 115018; 171.
DIP; DIP-50271N; -.
IntAct; Q66GS9; 175.
MINT; MINT-1200560; -.
STRING; 9606.ENSP00000257287; -.
iPTMnet; Q66GS9; -.
PhosphoSitePlus; Q66GS9; -.
BioMuta; CEP135; -.
DMDM; 296434460; -.
EPD; Q66GS9; -.
MaxQB; Q66GS9; -.
PaxDb; Q66GS9; -.
PeptideAtlas; Q66GS9; -.
PRIDE; Q66GS9; -.
Ensembl; ENST00000257287; ENSP00000257287; ENSG00000174799. [Q66GS9-1]
Ensembl; ENST00000422247; ENSP00000412799; ENSG00000174799. [Q66GS9-2]
GeneID; 9662; -.
KEGG; hsa:9662; -.
UCSC; uc003hbh.3; human. [Q66GS9-1]
CTD; 9662; -.
DisGeNET; 9662; -.
GeneCards; CEP135; -.
GeneReviews; CEP135; -.
H-InvDB; HIX0019826; -.
HGNC; HGNC:29086; CEP135.
MalaCards; CEP135; -.
MIM; 611423; gene.
MIM; 614673; phenotype.
neXtProt; NX_Q66GS9; -.
OpenTargets; ENSG00000174799; -.
Orphanet; 2512; Autosomal recessive primary microcephaly.
PharmGKB; PA128394551; -.
eggNOG; ENOG410IGCA; Eukaryota.
eggNOG; ENOG410XRIP; LUCA.
GeneTree; ENSGT00530000063949; -.
HOGENOM; HOG000060077; -.
HOVERGEN; HBG081318; -.
InParanoid; Q66GS9; -.
KO; K16461; -.
OMA; EFHSHLT; -.
OrthoDB; EOG091G032W; -.
PhylomeDB; Q66GS9; -.
TreeFam; TF326518; -.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
ChiTaRS; CEP135; human.
GeneWiki; CEP135; -.
GenomeRNAi; 9662; -.
PRO; PR:Q66GS9; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000174799; -.
CleanEx; HS_CEP135; -.
Genevisible; Q66GS9; HS.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
GO; GO:0010457; P:centriole-centriole cohesion; IMP:UniProtKB.
GO; GO:0097711; P:ciliary basal body docking; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IMP:UniProtKB.
InterPro; IPR026732; Cep135.
PANTHER; PTHR23159:SF23; PTHR23159:SF23; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Mental retardation; Phosphoprotein;
Polymorphism; Primary microcephaly; Reference proteome.
CHAIN 1 1140 Centrosomal protein of 135 kDa.
/FTId=PRO_0000089491.
COILED 71 152 {ECO:0000255}.
COILED 195 420 {ECO:0000255}.
COILED 447 1039 {ECO:0000255}.
COILED 1069 1116 {ECO:0000255}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1121 1121 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1130 1130 Phosphoserine.
{ECO:0000250|UniProtKB:Q6P5D4}.
VAR_SEQ 234 249 IELREREIERLSVALD -> VGFLFTCIVGIEIGML (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_012743.
VAR_SEQ 250 1140 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_012744.
VARIANT 769 769 I -> L (in dbSNP:rs3214045).
/FTId=VAR_057785.
CONFLICT 336 336 V -> L (in Ref. 4; BAA31610).
{ECO:0000305}.
CONFLICT 509 509 Q -> R (in Ref. 3; AAH12003).
{ECO:0000305}.
HELIX 82 131 {ECO:0000244|PDB:5FCN}.
SEQUENCE 1140 AA; 133490 MW; AD56754BEBB3AA5B CRC64;
MTTAVERKYI NIRKRLDQLG YRQTLTVECL PLVEKLFSDL VHTTESLRQS KLSAVKAEKE
SANFDFVLEP YKLENARLSR ENNELYLELM KLREHSDQHV KELKTSLKKC ARETADLKFL
NNQYAHKLKL LEKESKAKNE RIQQLQEKNL HAVVQTPGGK KRSIAFRRQR MQIDEPVPPS
EVSSYPVPQP DDPYIADLLQ VADNRIQELQ QEVHQLQEKL AMMESGVRDY SKQIELRERE
IERLSVALDG GRSPDVLSLE SRNKTNEKLI AHLNIQVDFL QQANKDLEKR IRELMETKET
VTSEVVNLSN KNEKLCQELT EIDQLAQQLE RHKEEVLETA DKELGEAKKE IKRKLSEMQD
LEETMAKLQL ELNLCQKEKE RLSDELLVKS DLETVVHQLE QEKQRLSKKV ESFAVTERQL
TLEVERMRLE HGIKRRDRSP SRLDTFLKGI EEERDYYKKE LERLQHIIQR RSCSTSYSAR
EKSSIFRTPE KGDYNSEIHQ ITRERDELQR MLERFEKYME DIQSNVKLLT AERDKLSVLY
NEAQEELSAL RKESTQTTAP HNIVSLMEKE KELALSDLRR IMAEKEALRE KLEHIEEVSL
FGKSELEKTI EHLTCVNHQL ESEKYELKSK VLIMKETIES LENKLKVQAQ KFSHVAGDSS
HQKTEVNSLR IVNEQLQRSV DDYQHRLSIK RGELESAQAQ IKILEEKIDE LNLKMTSQDE
EAHVMKKTIG VIDKEKDFLQ ETVDEKTEKI ANLQENLANK EKAVAQMKIM ISECESSVNQ
LKETLVNRDR EINSLRRQLD AAHKELDEVG RSREIAFKEN RRLQDDLATM ARENQEISLE
LEAAVQEKEE MKSRVHKYIT EVSRWESLMA AKEKENQDLL DRFQMLHNRA EDWEVKAHQA
EGESSSVRLE LLSIDTERRH LRERVELLEK EIQEHINAHH AYESQISSMA KAMSRLEEEL
RHQEDEKATV LNDLSSLREL CIKLDSGKDI MTQQLNSKNL EFERVVVELE NVKSESDLLK
KQLSNERHTV KNLESLLATN RDKEFHSHLT SHEKDTEIQL LKEKLTLSES KLTSQSRENT
MLRAKVAQLQ TDYDALKRQI STERYERERA IQEMRRHGLA TPPLSSTLRS PSHSPEHRNV


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