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Q9Y592 (CEP83_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centrosomal protein of 83 kDa

Short name=Cep83
Alternative name(s):
Coiled-coil domain-containing protein 41
Renal carcinoma antigen NY-REN-58
Gene names
Name:CCDC41
Synonyms:CEP83
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length693 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the distal appendage region of the centriole involved in the initiation of primary cilium assembly. May collaborate with IFT20 in the trafficking of ciliary membrane proteins from the Golgi complex to the cilium during the initiation of primary cilium assembly. Ref.5 Ref.6

Subunit structure

Interacts with CEP164 and IFT20. Ref.6

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Note: Localizes specifically to the distal appendage region of the centriole, which anchors the mother centriole to the plasma membrane. Localizes to centrioles at all stages of the cell cycle, including mitosis. Ref.5 Ref.6

Sequence similarities

Belongs to the CEP83 family.

Sequence caution

The sequence AAD42881.1 differs from that shown. Reason: Frameshift at positions 105, 590 and 601.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y592-1)

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.
Isoform 2 (identifier: Q9Y592-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: Missing.
     562-593: RKSLHENKLKRLQEKVEVLEAKKEELETENQV → LEQDLELGCPSVTDTYRESVFPPPPLKRDLLK
     594-693: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 693693Centrosomal protein of 83 kDa
PRO_0000234495

Regions

Coiled coil32 – 626595 Potential
Coiled coil657 – 69034 Potential

Natural variations

Alternative sequence1 – 2525Missing in isoform 2.
VSP_037760
Alternative sequence562 – 59332RKSLH…TENQV → LEQDLELGCPSVTDTYRESV FPPPPLKRDLLK in isoform 2.
VSP_037761
Alternative sequence594 – 693100Missing in isoform 2.
VSP_037762
Natural variant701Q → R.
Corresponds to variant rs2271979 [ dbSNP | Ensembl ].
VAR_058397

Experimental info

Sequence conflict2591E → G in AAD42881. Ref.1
Sequence conflict3361I → L in AAD42881. Ref.1
Sequence conflict5361E → D in AAD42881. Ref.1
Sequence conflict5371R → C in AAI25087. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: 0310952944AE6970

FASTA69382,059
        10         20         30         40         50         60 
MDTFPNNFPP GGDSGLTGSQ SEFQKMLIDE RLRCEHHKAN YQTLKAEHTR LQNEHVKLQN 

        70         80         90        100        110        120 
ELKHLFNEKQ TQQEKLQLLL EELRGELVEK TKDLEEMKLQ ILTPQKLELL RAQIQQELET 

       130        140        150        160        170        180 
PMRERFRNLD EEVEKYRAVY NKLRYEHTFL KSEFEHQKEE YARILDEGKI KYESEIARLE 

       190        200        210        220        230        240 
EDKEELRNQL LNVDLTKDSK RVEQLAREKV YLCQKLKGLE AEVAELKAEK ENSEAQVENA 

       250        260        270        280        290        300 
QRIQVRQLAE MQATVRSLEA EKQSANLRAE RLEKELQSSS EQNTFLINKL HKAEREINTL 

       310        320        330        340        350        360 
SSKVKELKHS NKLEITDIKL ETARAKSELE RERNKIQSEL DGLQSDNEIL KAAVEHHKVL 

       370        380        390        400        410        420 
LVEKDRELIR KVQAAKEEGY QKLVVLQDEK LELENRLADL EKMKVEHDVW RQSEKDQYEE 

       430        440        450        460        470        480 
KLRASQMAEE ITRKELQSVR LKLQQQIVTI ENAEKEKNEN SDLKQQISSL QIQVTSLAQS 

       490        500        510        520        530        540 
ENDLLNSNQM LKEMVERLKQ ECRNFRSQAE KAQLEAEKTL EEKQIQWLEE KHKLHERITD 

       550        560        570        580        590        600 
REEKYNQAKE KLQRAAIAQK KRKSLHENKL KRLQEKVEVL EAKKEELETE NQVLNRQNVP 

       610        620        630        640        650        660 
FEDYTRLQKR LKDIQRRHNE FRSLILVPNM PPTASINPVS FQSSAMVPSM ELPFPPHMQE 

       670        680        690 
EQHQRELSLL RKRLEELETT QRKQLEELGS SGE 

« Hide

Isoform 2 [UniParc].

Checksum: 870DDD0933F30FD7
Show »

FASTA56867,408

References

« Hide 'large scale' references
[1]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION AS A RENAL CANCER ANTIGEN.
[2]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-634 (ISOFORM 1).
Tissue: Retinoblastoma.
[4]"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. expand/collapse author list , 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] OF 1-559 (ISOFORM 1).
[5]"Centriole distal appendages promote membrane docking, leading to cilia initiation."
Tanos B.E., Yang H.J., Soni R., Wang W.J., Macaluso F.P., Asara J.M., Tsou M.F.
Genes Dev. 27:163-168(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"CCDC41 is required for ciliary vesicle docking to the mother centriole."
Joo K., Kim C.G., Lee M.S., Moon H.Y., Lee S.H., Kim M.J., Kweon H.S., Park W.Y., Kim C.H., Gleeson J.G., Kim J.
Proc. Natl. Acad. Sci. U.S.A. 110:5987-5992(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CEP164 AND IFT20.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF155115 mRNA. Translation: AAD42881.1. Frameshift.
AC073655 Genomic DNA. No translation available.
BC053614 mRNA. No translation available.
BC125086 mRNA. Translation: AAI25087.1.
BC125087 mRNA. Translation: AAI25088.1.
AK056316 mRNA. No translation available.
RefSeqNP_057206.2. NM_016122.2.
UniGeneHs.279209.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119321. 2 interactions.
IntActQ9Y592. 1 interaction.
MINTMINT-1790539.
STRING9606.ENSP00000344655.

PTM databases

PhosphoSiteQ9Y592.

Polymorphism databases

DMDM97045295.

Proteomic databases

PaxDbQ9Y592.
PRIDEQ9Y592.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000397807; ENSP00000380909; ENSG00000173588. [Q9Y592-2]
ENST00000547232; ENSP00000447783; ENSG00000173588. [Q9Y592-2]
GeneID51134.
KEGGhsa:51134.

Organism-specific databases

CTD51134.
GeneCardsGC12M094702.
HGNCHGNC:17966. CCDC41.
HPAHPA038161.
neXtProtNX_Q9Y592.
PharmGKBPA142672158.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG125204.
HOGENOMHOG000111412.
HOVERGENHBG053993.
InParanoidQ9Y592.
KOK16754.
OrthoDBEOG75TMBC.
PhylomeDBQ9Y592.

Gene expression databases

ArrayExpressQ9Y592.
BgeeQ9Y592.
CleanExHS_CCDC41.
GenevestigatorQ9Y592.

Family and domain databases

ProtoNetSearch...

Other

ChiTaRSCCDC41. human.
GenomeRNAi51134.
NextBio53977.
PROQ9Y592.

Entry information

Entry nameCEP83_HUMAN
AccessionPrimary (citable) accession number: Q9Y592
Secondary accession number(s): A4FVB1, Q08AP1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: April 16, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM