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Protein

Centrosomal protein of 72 kDa

Gene

CEP72

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the recruitment of key centrosomal proteins to the centrosome. Provides centrosomal microtubule-nucleation activity on the gamma-tubulin ring complexes (gamma-TuRCs) and has critical roles in forming a focused bipolar spindle, which is needed for proper tension generation between sister chromatids. Required for localization of KIZ, AKAP9 and gamma-tubulin ring complexes (gamma-TuRCs) (PubMed:19536135). Involved in centriole duplication. Required for CDK5RAP22, CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:26297806).2 Publications

GO - Biological processi

  • centriole replication Source: UniProtKB
  • G2/M transition of mitotic cell cycle Source: Reactome
  • gamma-tubulin complex localization Source: UniProtKB
  • regulation of protein localization to centrosome Source: UniProtKB
  • spindle organization Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
Centrosomal protein of 72 kDa
Short name:
Cep72
Gene namesi
Name:CEP72
Synonyms:KIAA1519
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:25547. CEP72.

Subcellular locationi

GO - Cellular componenti

  • centriolar satellite Source: UniProtKB
  • centrosome Source: UniProtKB
  • cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672125.

Polymorphism and mutation databases

BioMutaiCEP72.
DMDMi62901504.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 647647Centrosomal protein of 72 kDaPRO_0000089499Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei237 – 2371PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9P209.
MaxQBiQ9P209.
PaxDbiQ9P209.
PRIDEiQ9P209.

PTM databases

iPTMnetiQ9P209.
PhosphoSiteiQ9P209.

Expressioni

Gene expression databases

BgeeiQ9P209.
CleanExiHS_CEP72.
GenevisibleiQ9P209. HS.

Organism-specific databases

HPAiHPA058235.

Interactioni

Subunit structurei

Interacts with KIZ, PCM1 and CDK5RAP2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATXN7O152652EBI-739498,EBI-708350
CATIPQ7Z7H35EBI-739498,EBI-10258233
FAM90A1Q86YD73EBI-739498,EBI-6658203
KIZQ2M2Z53EBI-739498,EBI-2554344
NME7Q9Y5B85EBI-739498,EBI-744782
PCM1Q151544EBI-739498,EBI-741421
PIN4Q9Y2373EBI-739498,EBI-714599
PSMA1P257865EBI-739498,EBI-359352
SFRS2Q6NXQ03EBI-739498,EBI-10251550
SPATA24Q86W543EBI-739498,EBI-3916986
STAMBPL1Q96FJ05EBI-739498,EBI-745021

Protein-protein interaction databases

BioGridi120844. 95 interactions.
DIPiDIP-54272N.
IntActiQ9P209. 77 interactions.
MINTiMINT-1442378.
STRINGi9606.ENSP00000264935.

Structurei

3D structure databases

ProteinModelPortaliQ9P209.
SMRiQ9P209. Positions 6-149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati29 – 5022LRR 1Add
BLAST
Repeati55 – 7622LRR 2Add
BLAST
Repeati77 – 9822LRR 3Add
BLAST
Domaini111 – 15040LRRCTAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili476 – 620145Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the CEP72 family.Curated
Contains 3 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated

Keywords - Domaini

Coiled coil, Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiENOG410IH75. Eukaryota.
ENOG4111P3A. LUCA.
GeneTreeiENSGT00530000063884.
HOGENOMiHOG000111549.
HOVERGENiHBG050900.
InParanoidiQ9P209.
KOiK16532.
OMAiQHLDKSL.
OrthoDBiEOG7CVPXN.
PhylomeDBiQ9P209.
TreeFamiTF338646.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]
SMARTiSM00369. LRR_TYP. 2 hits.
SM00446. LRRcap. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9P209-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARAGPRLVL SEEAVRAKSG LGPHRDLAEL QSLSIPGTYQ EKITHLGHSL
60 70 80 90 100
MSLTGLKSLD LSRNSLVSLE GIQYLTALES LNLYYNCISS LAEVFRLHAL
110 120 130 140 150
TELVDVDFRL NPVVKVEPDY RLFVVHLLPK LQQLDDRPVR ASERKASRLH
160 170 180 190 200
FASEDSLDSK ESVPASLKEG RPHHPRAKCT EALAKQSLVM DADDEAVLNL
210 220 230 240 250
IAECEWDLGR PPGSTSFSQK GREADSRGSQ ESRHLLSPQL VQYQCGDSGK
260 270 280 290 300
QGRETRRSSC RGCCLEKMPW SQLCGELPPL YGAEPEASRA PRPHTYFTPH
310 320 330 340 350
PDSMDTEDSA SSQKLDLSGE MVPGPLPAPG KCRKRRMPVG RFQTFSDQEG
360 370 380 390 400
LGCPERTHGS SVPKESLSRQ DSSESRNGRT LSQPEASETE EQRSRGVTDT
410 420 430 440 450
REPSPGSHSA LPGKKTALQA ALLETLLDLV DRSWGGCRSL HSNEAFLAQA
460 470 480 490 500
RHILSSVEEF TAAQDSSAMV GEDVGSLALE SKSLQSRLAE QQQQHAREMS
510 520 530 540 550
EVTAELHHTH KELDDLRQHL DKSLEENSRL KSLLLSMKKE VKSADTAATL
560 570 580 590 600
NLQIAGLQTS VKRLCGEIVE LKQHLEHYDK IQELTQMLQE SHSSLVSTNE
610 620 630 640
HLLQELSQVR AQHRAEVEQM HWSYQELKKT MALFPHSSAS HGGCQAC
Length:647
Mass (Da):71,718
Last modified:February 1, 2005 - v2
Checksum:i9F45C88511311460
GO
Isoform 2 (identifier: Q9P209-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     172-193: PHHPRAKCTEALAKQSLVMDAD → IQTSVEPAVGTVPVWGLWEAGP
     194-647: Missing.

Note: No experimental confirmation available.
Show »
Length:193
Mass (Da):21,336
Checksum:iEA8DBAF2E36B983F
GO

Sequence cautioni

The sequence BAA91685.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA96043.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti566 – 5661G → V in BAA91685 (PubMed:12168954).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti238 – 2381P → L.
Corresponds to variant rs869955 [ dbSNP | Ensembl ].
VAR_050798
Natural varianti412 – 4121P → T.
Corresponds to variant rs12522955 [ dbSNP | Ensembl ].
VAR_050799
Natural varianti509 – 5091T → A.1 Publication
Corresponds to variant rs868649 [ dbSNP | Ensembl ].
VAR_050800

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei172 – 19322PHHPR…VMDAD → IQTSVEPAVGTVPVWGLWEA GP in isoform 2. 1 PublicationVSP_037835Add
BLAST
Alternative sequencei194 – 647454Missing in isoform 2. 1 PublicationVSP_037836Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB040952 mRNA. Translation: BAA96043.1. Different initiation.
AK001427 mRNA. Translation: BAA91685.1. Different initiation.
AK299072 mRNA. Translation: BAG61138.1.
BC000132 mRNA. Translation: AAH00132.1.
BC001750 mRNA. Translation: AAH01750.2.
CCDSiCCDS34126.1. [Q9P209-1]
RefSeqiNP_060610.2. NM_018140.3. [Q9P209-1]
XP_011512365.1. XM_011514063.1. [Q9P209-1]
UniGeneiHs.591741.

Genome annotation databases

EnsembliENST00000264935; ENSP00000264935; ENSG00000112877. [Q9P209-1]
GeneIDi55722.
KEGGihsa:55722.
UCSCiuc003jbf.4. human. [Q9P209-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB040952 mRNA. Translation: BAA96043.1. Different initiation.
AK001427 mRNA. Translation: BAA91685.1. Different initiation.
AK299072 mRNA. Translation: BAG61138.1.
BC000132 mRNA. Translation: AAH00132.1.
BC001750 mRNA. Translation: AAH01750.2.
CCDSiCCDS34126.1. [Q9P209-1]
RefSeqiNP_060610.2. NM_018140.3. [Q9P209-1]
XP_011512365.1. XM_011514063.1. [Q9P209-1]
UniGeneiHs.591741.

3D structure databases

ProteinModelPortaliQ9P209.
SMRiQ9P209. Positions 6-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120844. 95 interactions.
DIPiDIP-54272N.
IntActiQ9P209. 77 interactions.
MINTiMINT-1442378.
STRINGi9606.ENSP00000264935.

PTM databases

iPTMnetiQ9P209.
PhosphoSiteiQ9P209.

Polymorphism and mutation databases

BioMutaiCEP72.
DMDMi62901504.

Proteomic databases

EPDiQ9P209.
MaxQBiQ9P209.
PaxDbiQ9P209.
PRIDEiQ9P209.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264935; ENSP00000264935; ENSG00000112877. [Q9P209-1]
GeneIDi55722.
KEGGihsa:55722.
UCSCiuc003jbf.4. human. [Q9P209-1]

Organism-specific databases

CTDi55722.
GeneCardsiCEP72.
HGNCiHGNC:25547. CEP72.
HPAiHPA058235.
MIMi616475. gene.
neXtProtiNX_Q9P209.
PharmGKBiPA142672125.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IH75. Eukaryota.
ENOG4111P3A. LUCA.
GeneTreeiENSGT00530000063884.
HOGENOMiHOG000111549.
HOVERGENiHBG050900.
InParanoidiQ9P209.
KOiK16532.
OMAiQHLDKSL.
OrthoDBiEOG7CVPXN.
PhylomeDBiQ9P209.
TreeFamiTF338646.

Enzyme and pathway databases

ReactomeiR-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-8854518. AURKA Activation by TPX2.

Miscellaneous databases

GeneWikiiCEP72.
GenomeRNAii55722.
PROiQ9P209.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P209.
CleanExiHS_CEP72.
GenevisibleiQ9P209. HS.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]
SMARTiSM00369. LRR_TYP. 2 hits.
SM00446. LRRcap. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-509.
    Tissue: Brain.
  2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 93-647 (ISOFORM 1).
    Tissue: Teratocarcinoma.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung and Placenta.
  5. "Proteomic characterization of the human centrosome by protein correlation profiling."
    Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.
    Nature 426:570-574(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Lymphoblast.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Cep72 regulates the localization of key centrosomal proteins and proper bipolar spindle formation."
    Oshimori N., Li X., Ohsugi M., Yamamoto T.
    EMBO J. 28:2066-2076(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIZ.
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Centriolar satellites assemble centrosomal microcephaly proteins to recruit CDK2 and promote centriole duplication."
    Kodani A., Yu T.W., Johnson J.R., Jayaraman D., Johnson T.L., Al-Gazali L., Sztriha L., Partlow J.N., Kim H., Krup A.L., Dammermann A., Krogan N., Walsh C.A., Reiter J.F.
    Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDK5RAP2 AND PCM1.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCEP72_HUMAN
AccessioniPrimary (citable) accession number: Q9P209
Secondary accession number(s): B4DR26
, Q9BV03, Q9BWM3, Q9NVR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 2005
Last modified: June 8, 2016
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.