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Protein

Centrosomal protein of 164 kDa

Gene

CEP164

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 - Biological processi

  1. cell division Source: UniProtKB-KW
  2. cilium assembly Source: UniProtKB
  3. DNA repair Source: UniProtKB-KW
  4. G2/M transition of mitotic cell cycle Source: Reactome
  5. mitotic cell cycle Source: Reactome
  6. mitotic nuclear division Source: UniProtKB-KW
  7. organelle organization Source: Reactome
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.
REACT_267965. Anchoring of the basal body to the plasma membrane.

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 Componenti: 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.

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

Nephronophthisis 15 (NPHP15)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:614845
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 kDaPRO_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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UPV0.
PaxDbiQ9UPV0.
PRIDEiQ9UPV0.

PTM databases

PhosphoSiteiQ9UPV0.

Expressioni

Tissue specificityi

Expressed in several cell lines.1 Publication

Gene expression databases

BgeeiQ9UPV0.
CleanExiHS_CEP164.
ExpressionAtlasiQ9UPV0. baseline and differential.
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. 15 interactions.
IntActiQ9UPV0. 10 interactions.
STRINGi9606.ENSP00000278935.

Structurei

3D structure databases

ProteinModelPortaliQ9UPV0.
SMRiQ9UPV0. Positions 56-90.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 8934WWPROSITE-ProRule annotationAdd
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1154 – 120653Sequence AnalysisAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 WW domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG73730.
GeneTreeiENSGT00730000111178.
HOGENOMiHOG000111523.
HOVERGENiHBG065113.
InParanoidiQ9UPV0.
KOiK16462.
OMAiKEEHQQV.
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. AlignAdd to basket

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

        10         20         30         40         50
MAGRPLRIGD QLVLEEDYDE TYIPSEQEIL EFAREIGIDP IKEPELMWLA
60 70 80 90 100
REGIVAPLPG EWKPCQDITG DIYYFNFANG QSMWDHPCDE HYRSLVIQER
110 120 130 140 150
AKLSTSGAIK KKKKKKEKKD KKDRDPPKSS LALGSSLAPV HVPLGGLAPL
160 170 180 190 200
RGLVDTPPSA LRGSQSVSLG SSVESGRQLG ELMLPSQGLK TSAYTKGLLG
210 220 230 240 250
SIYEDKTALS LLGLGEETNE EDEEESDNQS VHSSSEPLRN LHLDIGALGG
260 270 280 290 300
DFEYEESLRT SQPEEKKDVS LDSDAAGPPT PCKPSSPGAD SSLSSAVGKG
310 320 330 340 350
RQGSGARPGL PEKEENEKSE PKICRNLVTP KADPTGSEPA KASEKEAPED
360 370 380 390 400
TVDAGEEGSR REEAAKEPKK KASALEEGSS DASQELEISE HMKEPQLSDS
410 420 430 440 450
IASDPKSFHG LDFGFRSRIS EHLLDVDVLS PVLGGACRQA QQPLGIEDKD
460 470 480 490 500
DSQSSQDELQ SKQSKGLEER LSPPLPHEER AQSPPRSLAT EEEPPQGPEG
510 520 530 540 550
QPEWKEAEEL GEDSAASLSL QLSLQREQAP SPPAACEKGK EQHSQAEELG
560 570 580 590 600
PGQEEAEDPE EKVAVSPTPP VSPEVRSTEP VAPPEQLSEA ALKAMEEAVA
610 620 630 640 650
QVLEQDQRHL LESKQEKMQQ LREKLCQEEE EEILRLHQQK EQSLSSLRER
660 670 680 690 700
LQKAIEEEEA RMREEESQRL SWLRAQVQSS TQADEDQIRA EQEASLQKLR
710 720 730 740 750
EELESQQKAE RASLEQKNRQ MLEQLKEEIE ASEKSEQAAL NAAKEKALQQ
760 770 780 790 800
LREQLEGERK EAVATLEKEH SAELERLCSS LEAKHREVVS SLQKKIQEAQ
810 820 830 840 850
QKEEAQLQKC LGQVEHRVHQ KSYHVAGYEH ELSSLLREKR QEVEGEHERR
860 870 880 890 900
LDKMKEEHQQ VMAKAREQYE AEERKQRAEL LGHLTGELER LQRAHERELE
910 920 930 940 950
TVRQEQHKRL EDLRRRHREQ ERKLQDLELD LETRAKDVKA RLALLEVQEE
960 970 980 990 1000
TARREKQQLL DVQRQVALKS EEATATHQQL EEAQKEHTHL LQSNQQLREI
1010 1020 1030 1040 1050
LDELQARKLK LESQVDLLQA QSQQLQKHFS SLEAEAQKKQ HLLREVTVEE
1060 1070 1080 1090 1100
NNASPHFEPD LHIEDLRKSL GTNQTKEVSS SLSQSKEDLY LDSLSSHNVW
1110 1120 1130 1140 1150
HLLSAEGVAL RSAKEFLVQQ TRSMRRRQTA LKAAQQHWRH ELASAQEVAK
1160 1170 1180 1190 1200
DPPGIKALED MRKNLEKETR HLDEMKSAMR KGHNLLKKKE EKLNQLESSL
1210 1220 1230 1240 1250
WEEASDEGTL GGSPTKKAVT FDLSDMDSLS SESSESFSPP HREWWRQQRI
1260 1270 1280 1290 1300
DSTPSLTSRK IHGLSHSLRQ ISSQLSSVLS ILDSLNPQSP PPLLASMPAQ
1310 1320 1330 1340 1350
LPPRDPKSTP TPTYYGSLAR FSALSSATPT STQWAWDSGQ GPRLPSSVAQ
1360 1370 1380 1390 1400
TVDDFLLEKW RKYFPSGIPL LSNSPTPLES RLGYMSASEQ LRLLQHSHSQ
1410 1420 1430 1440 1450
VPEAGSTTFQ GIIEANRRWL ERVKNDPRLP LFSSTPKPKA TLSLLQLGLD
1460
EHNRVKVYRF
Length:1,460
Mass (Da):164,314
Last modified:December 3, 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.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH54015.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAA83004.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA91677.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAB56023.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101K → N in AAH54015 (PubMed:15489334).Curated

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. 2 PublicationsVSP_029843
Alternative sequencei1242 – 12509REWWRQQRI → L in isoform 2. 2 PublicationsVSP_029844

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9UPV0.
SMRiQ9UPV0. Positions 56-90.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116561. 15 interactions.
IntActiQ9UPV0. 10 interactions.
STRINGi9606.ENSP00000278935.

PTM databases

PhosphoSiteiQ9UPV0.

Polymorphism databases

DMDMi162416241.

Proteomic databases

MaxQBiQ9UPV0.
PaxDbiQ9UPV0.
PRIDEiQ9UPV0.

Protocols and materials databases

DNASUi22897.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi22897.
GeneCardsiGC11P117198.
H-InvDBHIX0010166.
HGNCiHGNC:29182. CEP164.
HPAiHPA037605.
HPA037606.
MIMi614845. phenotype.
614848. gene.
neXtProtiNX_Q9UPV0.
Orphaneti3156. Senior-Loken syndrome.
PharmGKBiPA142672127.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG73730.
GeneTreeiENSGT00730000111178.
HOGENOMiHOG000111523.
HOVERGENiHBG065113.
InParanoidiQ9UPV0.
KOiK16462.
OMAiKEEHQQV.
OrthoDBiEOG76HQ0R.
PhylomeDBiQ9UPV0.
TreeFamiTF333034.

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.
REACT_267965. Anchoring of the basal body to the plasma membrane.

Miscellaneous databases

ChiTaRSiCEP164. human.
GeneWikiiCEP164.
GenomeRNAii22897.
NextBioi43519.
PROiQ9UPV0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UPV0.
CleanExiHS_CEP164.
ExpressionAtlasiQ9UPV0. baseline and differential.
GenevestigatoriQ9UPV0.

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]
ProtoNetiSearch...

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(2006) [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(2007) [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(1998) [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(2003) [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(2003) [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(2002) [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(2008) [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(2010) [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(2011) [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(2012) [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 3, 2007
Last sequence update: December 3, 2007
Last modified: March 31, 2015
This is version 109 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

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 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.