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P41208 (CETN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. 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·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centrin-2
Alternative name(s):
Caltractin isoform 1
Gene names
Name:CETN2
Synonyms:CALT, CEN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110. Ref.1 Ref.9 Ref.10 Ref.12 Ref.13 Ref.16

Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer. Ref.1 Ref.9 Ref.10 Ref.12 Ref.13 Ref.16

The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. Ref.1 Ref.9 Ref.10 Ref.12 Ref.13 Ref.16

Subunit structure

Monomer. Homooligomer. Interacts with CCP110, SFI1. Component of the XPC complex composed of XPC, RAD23B and CETN2. Ref.9 Ref.11 Ref.12 Ref.15 Ref.16

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Nucleus Probable. Note: Centrosome of S-phase, interphase and mitotic cells. Ref.1 Ref.10

Miscellaneous

Binds two moles of calcium per mole of protein.

Sequence similarities

Belongs to the centrin family.

Contains 4 EF-hand domains.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA repair
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   DomainRepeat
   LigandCalcium
Metal-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

centriole replication

Inferred from mutant phenotype Ref.10. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Non-traceable author statement Ref.1. Source: UniProtKB

nucleotide-excision repair

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of cytokinesis

Inferred from mutant phenotype Ref.16. Source: UniProtKB

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentXPC complex

Inferred from direct assay Ref.9. Source: UniProtKB

centriole

Inferred from direct assay Ref.10. Source: UniProtKB

centrosome

Inferred from direct assay Ref.16PubMed 21399614. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

intracellular

Inferred from direct assay. Source: LIFEdb

photoreceptor connecting cilium

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

calcium ion binding

Non-traceable author statement Ref.1. Source: UniProtKB

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.16. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.21
Chain2 – 172171Centrin-2
PRO_0000073561

Regions

Domain28 – 6336EF-hand 1
Domain64 – 9936EF-hand 2
Domain101 – 13636EF-hand 3
Domain137 – 17236EF-hand 4
Calcium binding114 – 125121 Ref.22 Ref.23 Ref.24
Calcium binding150 – 161122 Ref.22 Ref.23 Ref.24
Region2 – 2524Required for self-assembly

Amino acid modifications

Modified residue21N-acetylalanine Ref.21
Modified residue201Phosphoserine Ref.17 Ref.18 Ref.20
Modified residue261Phosphothreonine Ref.14 Ref.18 Ref.20

Secondary structure

.......................... 172
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P41208 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 59CFD706AD7011B5

FASTA17219,738
        10         20         30         40         50         60 
MASNFKKANM ASSSQRKRMS PKPELTEEQK QEIREAFDLF DADGTGTIDV KELKVAMRAL 

        70         80         90        100        110        120 
GFEPKKEEIK KMISEIDKEG TGKMNFGDFL TVMTQKMSEK DTKEEILKAF KLFDDDETGK 

       130        140        150        160        170 
ISFKNLKRVA KELGENLTDE ELQEMIDEAD RDGDGEVSEQ EFLRIMKKTS LY 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and centrosomal localization of human caltractin."
Lee V.D., Huang B.
Proc. Natl. Acad. Sci. U.S.A. 90:11039-11043(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
Tissue: Umbilical vein.
[2]"Comparative genome sequence analysis of the Bpa/Str region in mouse and man."
Mallon A.-M., Platzer M., Bate R., Gloeckner G., Botcherby M.R.M., Nordsiek G., Strivens M.A., Kioschis P., Dangel A., Cunningham D., Straw R.N.A., Weston P., Gilbert M., Fernando S., Goodall K., Hunter G., Greystrong J.S., Clarke D. expand/collapse author list , Kimberley C., Goerdes M., Blechschmidt K., Rump A., Hinzmann B., Mundy C.R., Miller W., Poustka A., Herman G.E., Rhodes M., Denny P., Rosenthal A., Brown S.D.M.
Genome Res. 10:758-775(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Fetal brain.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]NIEHS SNPs program
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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].
Tissue: Ovary and Urinary bladder.
[9]"Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair."
Araki M., Masutani C., Takemura M., Uchida A., Sugasawa K., Kondoh J., Ohkuma Y., Hanaoka F.
J. Biol. Chem. 276:18665-18672(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA REPAIR, IDENTIFICATION IN THE XPC COMPLEX.
[10]"Centrin-2 is required for centriole duplication in mammalian cells."
Salisbury J.L., Suino K.M., Busby R., Springett M.
Curr. Biol. 12:1287-1292(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"Calcium-dependent self-assembly of human centrin 2."
Tourbez M., Firanescu C., Yang A., Unipan L., Duchambon P., Blouquit Y., Craescu C.T.
J. Biol. Chem. 279:47672-47680(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[12]"Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein."
Nishi R., Okuda Y., Watanabe E., Mori T., Iwai S., Masutani C., Sugasawa K., Hanaoka F.
Mol. Cell. Biol. 25:5664-5674(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA REPAIR, INTERACTION WITH XPC.
[13]"Biochemical and structural domain analysis of xeroderma pigmentosum complementation group C protein."
Bunick C.G., Miller M.R., Fuller B.E., Fanning E., Chazin W.J.
Biochemistry 45:14965-14979(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA REPAIR.
[14]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Binding of human centrin 2 to the centrosomal protein hSfi1."
Martinez-Sanz J., Yang A., Blouquit Y., Duchambon P., Assairi L., Craescu C.T.
FEBS J. 273:4504-4515(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SFI1.
[16]"CP110 cooperates with two calcium-binding proteins to regulate cytokinesis and genome stability."
Tsang W.Y., Spektor A., Luciano D.J., Indjeian V.B., Chen Z., Salisbury J.L., Sanchez I., Dynlacht B.D.
Mol. Biol. Cell 17:3423-3434(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CCP110.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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-20 AND THR-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[22]"C-terminal half of human centrin 2 behaves like a regulatory EF-hand domain."
Matei E., Miron S., Blouquit Y., Duchambon P., Durussel I., Cox J.A., Craescu C.T.
Biochemistry 42:1439-1450(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 84-172, CALCIUM-BINDING.
[23]"The N-terminal domain of human centrin 2 has a closed structure, binds calcium with a very low affinity, and plays a role in the protein self-assembly."
Yang A., Miron S., Duchambon P., Assairi L., Blouquit Y., Craescu C.T.
Biochemistry 45:880-889(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-98, CALCIUM-BINDING.
[24]"Flexibility and plasticity of human centrin 2 binding to the xeroderma pigmentosum group C protein (XPC) from nuclear excision repair."
Yang A., Miron S., Mouawad L., Duchambon P., Blouquit Y., Craescu C.T.
Biochemistry 45:3653-3663(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 94-172 IN COMPLEX WITH XPC, CALCIUM-BINDING.
[25]"The structure of the human centrin 2-xeroderma pigmentosum group C protein complex."
Thompson J.R., Ryan Z.C., Salisbury J.L., Kumar R.
J. Biol. Chem. 281:18746-18752(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-172 IN COMPLEX WITH CALCIUM IONS AND XPC.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X72964 mRNA. Translation: CAA51467.1.
U82671 Genomic DNA. No translation available.
AK311940 mRNA. Translation: BAG34881.1.
BT007256 mRNA. Translation: AAP35920.1.
AY919675 Genomic DNA. Translation: AAW82436.1.
CH471172 Genomic DNA. Translation: EAW72900.1.
BC005334 mRNA. Translation: AAH05334.1.
BC013873 mRNA. Translation: AAH13873.1.
CCDSCCDS14716.1.
PIRA49652.
RefSeqNP_004335.1. NM_004344.1.
UniGeneHs.82794.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M39NMR-A84-172[»]
1ZMZNMR-A1-98[»]
2A4JNMR-A94-172[»]
2GGMX-ray2.35A/B1-172[»]
2K2INMR-A94-172[»]
2OBHX-ray1.80A/B26-168[»]
ProteinModelPortalP41208.
SMRP41208. Positions 26-168.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107496. 15 interactions.
IntActP41208. 9 interactions.
MINTMINT-3015206.
STRING9606.ENSP00000359300.

PTM databases

PhosphoSiteP41208.

Polymorphism databases

DMDM729052.

Proteomic databases

MaxQBP41208.
PaxDbP41208.
PRIDEP41208.

Protocols and materials databases

DNASU1069.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370277; ENSP00000359300; ENSG00000147400.
ENST00000601896; ENSP00000469720; ENSG00000268512.
GeneID1069.
KEGGhsa:1069.
UCSCuc004fgq.3. human.

Organism-specific databases

CTD1069.
GeneCardsGC0XM151996.
HGNCHGNC:1867. CETN2.
HPAHPA028956.
MIM300006. gene.
neXtProtNX_P41208.
PharmGKBPA26420.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5126.
HOGENOMHOG000233018.
HOVERGENHBG012180.
InParanoidP41208.
KOK10840.
OMALMTVKMA.
OrthoDBEOG7H1JN9.
PhylomeDBP41208.
TreeFamTF101141.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

BgeeP41208.
CleanExHS_CETN2.
GenevestigatorP41208.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000629. RNA-helicase_DEAD-box_CS.
[Graphical view]
PfamPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 4 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP41208.
GeneWikiCETN2.
GenomeRNAi1069.
NextBio4464.
PROP41208.
SOURCESearch...

Entry information

Entry nameCETN2_HUMAN
AccessionPrimary (citable) accession number: P41208
Secondary accession number(s): B2R4T4, Q53XW1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 152 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

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