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Q9UPV0

- CE164_HUMAN

UniProt

Q9UPV0 - CE164_HUMAN

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Protein
Centrosomal protein of 164 kDa
Gene
CEP164, KIAA1052, NPHP15
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays a role in microtubule organization and/or maintenance for the formation of primary cilia (PC), a microtubule-based structure that protrudes from the surface of epithelial cells. Plays a critical role in G2/M checkpoint and nuclear divisions. A key player in the DNA damage-activated ATR/ATM signaling cascade since it is required for the proper phosphorylation of H2AX, RPA, CHEK2 and CHEK1. Plays a critical role in chromosome segregation, acting as a mediator required for the maintenance of genomic stability through modulation of MDC1, RPA and CHEK1.3 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. G2/M transition of mitotic cell cycle Source: Reactome
  3. cilium assembly Source: UniProtKB
  4. mitotic cell cycle Source: Reactome
  5. mitotic nuclear division Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Cilium biogenesis/degradation, DNA damage, DNA repair, Mitosis

Enzyme and pathway databases

ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Names & Taxonomyi

Protein namesi
Recommended name:
Centrosomal protein of 164 kDa
Short name:
Cep164
Gene namesi
Name:CEP164
Synonyms:KIAA1052, NPHP15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:29182. CEP164.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Nucleus
Note: Localizes specifically to very distally located appendage structures on the mature centriole from which initiate PC formation. Persisted at centrioles throughout mitosis. Expressed in chromatin-enriched nuclear fraction of HeLa cells. In response to DNA damage, it translocates to nuclear foci that contain the DNA damage response proteins KAT5/TIP60 and CHEK1.8 Publications

GO - Cellular componenti

  1. centriole Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. ciliary transition fiber Source: MGI
  4. cytoplasm Source: HPA
  5. cytosol Source: Reactome
  6. extracellular space Source: UniProt
  7. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

Nephronophthisis 15 (NPHP15) [MIM:614845]: An autosomal recessive disorder characterized by the association of nephronophthisis with Leber congenital amaurosis and retinal degeneration, often resulting in blindness during childhood. Additional features include seizures, cerebellar vermis hypoplasia, facial dysmorphism, bronchiectasis and liver failure. Nephronophthisis is a chronic tubulo-interstitial nephritis that progresses to end-stage renal failure.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111Q → P in NPHP15. 1 Publication
VAR_068503
Natural varianti93 – 931R → W in NPHP15. 1 Publication
VAR_068504

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi186 – 1861S → A: Prevents phosphorylation. 1 Publication

Keywords - Diseasei

Ciliopathy, Disease mutation, Nephronophthisis

Organism-specific databases

MIMi614845. phenotype.
Orphaneti3156. Senior-Loken syndrome.
PharmGKBiPA142672127.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14601460Centrosomal protein of 164 kDa
PRO_0000312494Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei186 – 1861Phosphoserine; by ATR and ATM1 Publication

Post-translational modificationi

Phosphorylation at Ser-186 is induced upon DNA-damage caused by treatment with IR irradiation, UV irradiation, hydroxyurea or amphidicolin. Also MDC1-mediated chromatin remodeling is critical for DNA damage-induced phosphorylation.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UPV0.
PaxDbiQ9UPV0.
PRIDEiQ9UPV0.

PTM databases

PhosphoSiteiQ9UPV0.

Expressioni

Tissue specificityi

Expressed in several cell lines.1 Publication

Gene expression databases

ArrayExpressiQ9UPV0.
BgeeiQ9UPV0.
CleanExiHS_CEP164.
GenevestigatoriQ9UPV0.

Organism-specific databases

HPAiHPA037605.
HPA037606.

Interactioni

Subunit structurei

Interacts (via N-terminus) with ATRIP. Interacts with ATM, ATR and MDC1. Interacts with XPA (via N-terminus) upon UV irradiation. Interacts with CEP83, CCDC92, TTBK2, DVL3, NPHP3 and weakly with NPHP4.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC92Q53HC05EBI-3937015,EBI-719994
DVL3Q929975EBI-3937015,EBI-739789
NPHP3Q7Z4942EBI-3937015,EBI-2804263
TTBK2Q6IQ554EBI-3937015,EBI-1050303

Protein-protein interaction databases

BioGridi116561. 12 interactions.
IntActiQ9UPV0. 10 interactions.
STRINGi9606.ENSP00000278935.

Structurei

3D structure databases

ProteinModelPortaliQ9UPV0.
SMRiQ9UPV0. Positions 55-88.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 8934WW
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 194194Interaction with ATRIP
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1154 – 120653 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi110 – 12213Lys-rich
Add
BLAST
Compositional biasi468 – 955488Glu-rich
Add
BLAST

Sequence similaritiesi

Contains 1 WW domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG73730.
HOGENOMiHOG000111523.
HOVERGENiHBG065113.
InParanoidiQ9UPV0.
KOiK16462.
OMAiKKEHTHL.
OrthoDBiEOG76HQ0R.
PhylomeDBiQ9UPV0.
TreeFamiTF333034.

Family and domain databases

InterProiIPR001202. WW_dom.
[Graphical view]
SMARTiSM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UPV0-1) [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

MAGRPLRIGD QLVLEEDYDE TYIPSEQEIL EFAREIGIDP IKEPELMWLA     50
REGIVAPLPG EWKPCQDITG DIYYFNFANG QSMWDHPCDE HYRSLVIQER 100
AKLSTSGAIK KKKKKKEKKD KKDRDPPKSS LALGSSLAPV HVPLGGLAPL 150
RGLVDTPPSA LRGSQSVSLG SSVESGRQLG ELMLPSQGLK TSAYTKGLLG 200
SIYEDKTALS LLGLGEETNE EDEEESDNQS VHSSSEPLRN LHLDIGALGG 250
DFEYEESLRT SQPEEKKDVS LDSDAAGPPT PCKPSSPGAD SSLSSAVGKG 300
RQGSGARPGL PEKEENEKSE PKICRNLVTP KADPTGSEPA KASEKEAPED 350
TVDAGEEGSR REEAAKEPKK KASALEEGSS DASQELEISE HMKEPQLSDS 400
IASDPKSFHG LDFGFRSRIS EHLLDVDVLS PVLGGACRQA QQPLGIEDKD 450
DSQSSQDELQ SKQSKGLEER LSPPLPHEER AQSPPRSLAT EEEPPQGPEG 500
QPEWKEAEEL GEDSAASLSL QLSLQREQAP SPPAACEKGK EQHSQAEELG 550
PGQEEAEDPE EKVAVSPTPP VSPEVRSTEP VAPPEQLSEA ALKAMEEAVA 600
QVLEQDQRHL LESKQEKMQQ LREKLCQEEE EEILRLHQQK EQSLSSLRER 650
LQKAIEEEEA RMREEESQRL SWLRAQVQSS TQADEDQIRA EQEASLQKLR 700
EELESQQKAE RASLEQKNRQ MLEQLKEEIE ASEKSEQAAL NAAKEKALQQ 750
LREQLEGERK EAVATLEKEH SAELERLCSS LEAKHREVVS SLQKKIQEAQ 800
QKEEAQLQKC LGQVEHRVHQ KSYHVAGYEH ELSSLLREKR QEVEGEHERR 850
LDKMKEEHQQ VMAKAREQYE AEERKQRAEL LGHLTGELER LQRAHERELE 900
TVRQEQHKRL EDLRRRHREQ ERKLQDLELD LETRAKDVKA RLALLEVQEE 950
TARREKQQLL DVQRQVALKS EEATATHQQL EEAQKEHTHL LQSNQQLREI 1000
LDELQARKLK LESQVDLLQA QSQQLQKHFS SLEAEAQKKQ HLLREVTVEE 1050
NNASPHFEPD LHIEDLRKSL GTNQTKEVSS SLSQSKEDLY LDSLSSHNVW 1100
HLLSAEGVAL RSAKEFLVQQ TRSMRRRQTA LKAAQQHWRH ELASAQEVAK 1150
DPPGIKALED MRKNLEKETR HLDEMKSAMR KGHNLLKKKE EKLNQLESSL 1200
WEEASDEGTL GGSPTKKAVT FDLSDMDSLS SESSESFSPP HREWWRQQRI 1250
DSTPSLTSRK IHGLSHSLRQ ISSQLSSVLS ILDSLNPQSP PPLLASMPAQ 1300
LPPRDPKSTP TPTYYGSLAR FSALSSATPT STQWAWDSGQ GPRLPSSVAQ 1350
TVDDFLLEKW RKYFPSGIPL LSNSPTPLES RLGYMSASEQ LRLLQHSHSQ 1400
VPEAGSTTFQ GIIEANRRWL ERVKNDPRLP LFSSTPKPKA TLSLLQLGLD 1450
EHNRVKVYRF 1460
Length:1,460
Mass (Da):164,314
Last modified:December 4, 2007 - v3
Checksum:i7A4F91E1CB7D1E43
GO
Isoform 2 (identifier: Q9UPV0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     469-469: E → ERYH
     1242-1250: REWWRQQRI → L

Show »
Length:1,455
Mass (Da):163,544
Checksum:i7F48093100C34819
GO

Sequence cautioni

The sequence AAH00602.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH54015.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence BAA83004.2 differs from that shown. Reason: Erroneous initiation.
The sequence BAA91677.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAB56023.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111Q → P in NPHP15. 1 Publication
VAR_068503
Natural varianti93 – 931R → W in NPHP15. 1 Publication
VAR_068504
Natural varianti94 – 941S → N.
Corresponds to variant rs490262 [ dbSNP | Ensembl ].
VAR_037511
Natural varianti988 – 9881T → S.1 Publication
Corresponds to variant rs2305830 [ dbSNP | Ensembl ].
VAR_037512
Natural varianti1119 – 11191Q → R.2 Publications
Corresponds to variant rs573455 [ dbSNP | Ensembl ].
VAR_037513

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei469 – 4691E → ERYH in isoform 2.
VSP_029843
Alternative sequencei1242 – 12509REWWRQQRI → L in isoform 2.
VSP_029844

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101K → N in AAH54015. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB028975 mRNA. Translation: BAA83004.2. Different initiation.
AP000892 Genomic DNA. No translation available.
AP001822 Genomic DNA. No translation available.
BC000602 mRNA. Translation: AAH00602.1. Sequence problems.
BC054015 mRNA. Translation: AAH54015.1. Sequence problems.
AL117632 mRNA. Translation: CAB56023.1. Different initiation.
AK001412 mRNA. Translation: BAA91677.1. Different initiation.
CCDSiCCDS31683.1. [Q9UPV0-1]
PIRiT17333.
RefSeqiNP_001258862.1. NM_001271933.1. [Q9UPV0-2]
NP_055771.4. NM_014956.4. [Q9UPV0-1]
XP_005271513.1. XM_005271456.1. [Q9UPV0-1]
XP_005271514.1. XM_005271457.1. [Q9UPV0-2]
UniGeneiHs.504009.

Genome annotation databases

EnsembliENST00000278935; ENSP00000278935; ENSG00000110274. [Q9UPV0-1]
GeneIDi22897.
KEGGihsa:22897.
UCSCiuc001prb.4. human. [Q9UPV0-2]
uc001prc.3. human. [Q9UPV0-1]

Polymorphism databases

DMDMi162416241.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB028975 mRNA. Translation: BAA83004.2 . Different initiation.
AP000892 Genomic DNA. No translation available.
AP001822 Genomic DNA. No translation available.
BC000602 mRNA. Translation: AAH00602.1 . Sequence problems.
BC054015 mRNA. Translation: AAH54015.1 . Sequence problems.
AL117632 mRNA. Translation: CAB56023.1 . Different initiation.
AK001412 mRNA. Translation: BAA91677.1 . Different initiation.
CCDSi CCDS31683.1. [Q9UPV0-1 ]
PIRi T17333.
RefSeqi NP_001258862.1. NM_001271933.1. [Q9UPV0-2 ]
NP_055771.4. NM_014956.4. [Q9UPV0-1 ]
XP_005271513.1. XM_005271456.1. [Q9UPV0-1 ]
XP_005271514.1. XM_005271457.1. [Q9UPV0-2 ]
UniGenei Hs.504009.

3D structure databases

ProteinModelPortali Q9UPV0.
SMRi Q9UPV0. Positions 55-88.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116561. 12 interactions.
IntActi Q9UPV0. 10 interactions.
STRINGi 9606.ENSP00000278935.

PTM databases

PhosphoSitei Q9UPV0.

Polymorphism databases

DMDMi 162416241.

Proteomic databases

MaxQBi Q9UPV0.
PaxDbi Q9UPV0.
PRIDEi Q9UPV0.

Protocols and materials databases

DNASUi 22897.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000278935 ; ENSP00000278935 ; ENSG00000110274 . [Q9UPV0-1 ]
GeneIDi 22897.
KEGGi hsa:22897.
UCSCi uc001prb.4. human. [Q9UPV0-2 ]
uc001prc.3. human. [Q9UPV0-1 ]

Organism-specific databases

CTDi 22897.
GeneCardsi GC11P117198.
H-InvDB HIX0010166.
HGNCi HGNC:29182. CEP164.
HPAi HPA037605.
HPA037606.
MIMi 614845. phenotype.
614848. gene.
neXtProti NX_Q9UPV0.
Orphaneti 3156. Senior-Loken syndrome.
PharmGKBi PA142672127.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG73730.
HOGENOMi HOG000111523.
HOVERGENi HBG065113.
InParanoidi Q9UPV0.
KOi K16462.
OMAi KKEHTHL.
OrthoDBi EOG76HQ0R.
PhylomeDBi Q9UPV0.
TreeFami TF333034.

Enzyme and pathway databases

Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

GeneWikii CEP164.
GenomeRNAii 22897.
NextBioi 43519.
PROi Q9UPV0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UPV0.
Bgeei Q9UPV0.
CleanExi HS_CEP164.
Genevestigatori Q9UPV0.

Family and domain databases

InterProi IPR001202. WW_dom.
[Graphical view ]
SMARTi SM00456. WW. 1 hit.
[Graphical view ]
SUPFAMi SSF51045. SSF51045. 1 hit.
PROSITEi PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cep164, a novel centriole appendage protein required for primary cilium formation."
    Graser S., Stierhof Y.-D., Lavoie S.B., Gassner O.S., Lamla S., Le Clech M., Nigg E.A.
    J. Cell Biol. 179:321-330(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Cep164 is a mediator protein required for the maintenance of genomic stability through modulation of MDC1, RPA, and CHK1."
    Sivasubramaniam S., Sun X., Pan Y.R., Wang S., Lee E.Y.
    Genes Dev. 22:587-600(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH ATM; ATR; ATRIP AND MDC1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-186, MUTAGENESIS OF SER-186.
  3. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] OF 1-116 (ISOFORMS 1/2).
    Tissue: Skin.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 868-1460 (ISOFORM 1), VARIANTS SER-988 AND ARG-1119.
    Tissue: Testis.
  7. "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] OF 1038-1460 (ISOFORM 1), VARIANT ARG-1119.
    Tissue: Testis.
  8. "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.
  9. "UV-dependent interaction between Cep164 and XPA mediates localization of Cep164 at sites of DNA damage and UV sensitivity."
    Pan Y.R., Lee E.Y.
    Cell Cycle 8:655-664(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH XPA, SUBCELLULAR LOCATION.
  10. "Assessing the localization of centrosomal proteins by PALM/STORM nanoscopy."
    Sillibourne J.E., Specht C.G., Izeddin I., Hurbain I., Tran P., Triller A., Darzacq X., Dahan M., Bornens M.
    Cytoskeleton 68:619-627(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Exome capture reveals ZNF423 and CEP164 mutations, linking renal ciliopathies to DNA damage response signaling."
    Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G., Wang H., Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G., Hong C.J., Hamilton B.A., Cervenka I., Ganji R.S., Bryja V., Arts H.H.
    , van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R., Husson H., Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L., Sayer J.A., Schermer B., Liebau M.C., Benzing T., Le Corre S., Drummond I., Janssen S., Allen S.J., Natarajan S., O'Toole J.F., Attanasio M., Saunier S., Antignac C., Koenekoop R.K., Ren H., Lopez I., Nayir A., Stoetzel C., Dollfus H., Massoudi R., Gleeson J.G., Andreoli S.P., Doherty D.G., Lindstrad A., Golzio C., Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A., Lewis R.A., Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R., Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J., Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A., Hildebrandt F.
    Cell 150:533-548(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CCDC92; TTBK2; NPHP3; NPHP4 AND DVL3, VARIANTS NPHP15 PRO-11 AND TRP-93.
  12. "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.
  13. Cited for: INTERACTION WITH CEP83, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCE164_HUMAN
AccessioniPrimary (citable) accession number: Q9UPV0
Secondary accession number(s): Q6PKH9
, Q7Z2X9, Q9NVS0, Q9UFJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 4, 2007
Last modified: September 3, 2014
This is version 102 of the entry and version 3 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 11
    Human chromosome 11: 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

External Data

Dasty 3

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