CETN2_HUMAN
ID CETN2_HUMAN Reviewed; 172 AA.
AC P41208; B2R4T4; Q53XW1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Centrin-2;
DE AltName: Full=Caltractin isoform 1;
GN Name=CETN2; Synonyms=CALT, CEN2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Umbilical vein;
RX PubMed=8248209; DOI=10.1073/pnas.90.23.11039;
RA Lee V.D., Huang B.;
RT "Molecular cloning and centrosomal localization of human caltractin.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11039-11043(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10854409; DOI=10.1101/gr.10.6.758;
RA Mallon A.-M., Platzer M., Bate R., Gloeckner G., Botcherby M.R.M.,
RA Nordsiek G., Strivens M.A., Kioschis P., Dangel A., Cunningham D.,
RA Straw R.N.A., Weston P., Gilbert M., Fernando S., Goodall K., Hunter G.,
RA Greystrong J.S., Clarke D., Kimberley C., Goerdes M., Blechschmidt K.,
RA Rump A., Hinzmann B., Mundy C.R., Miller W., Poustka A., Herman G.E.,
RA Rhodes M., Denny P., Rosenthal A., Brown S.D.M.;
RT "Comparative genome sequence analysis of the Bpa/Str region in mouse and
RT man.";
RL Genome Res. 10:758-775(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION IN DNA REPAIR, AND IDENTIFICATION IN THE XPC COMPLEX.
RX PubMed=11279143; DOI=10.1074/jbc.m100855200;
RA Araki M., Masutani C., Takemura M., Uchida A., Sugasawa K., Kondoh J.,
RA Ohkuma Y., Hanaoka F.;
RT "Centrosome protein centrin 2/caltractin 1 is part of the xeroderma
RT pigmentosum group C complex that initiates global genome nucleotide
RT excision repair.";
RL J. Biol. Chem. 276:18665-18672(2001).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12176356; DOI=10.1016/s0960-9822(02)01019-9;
RA Salisbury J.L., Suino K.M., Busby R., Springett M.;
RT "Centrin-2 is required for centriole duplication in mammalian cells.";
RL Curr. Biol. 12:1287-1292(2002).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [12]
RP HOMOOLIGOMERIZATION.
RX PubMed=15356003; DOI=10.1074/jbc.m404996200;
RA Tourbez M., Firanescu C., Yang A., Unipan L., Duchambon P., Blouquit Y.,
RA Craescu C.T.;
RT "Calcium-dependent self-assembly of human centrin 2.";
RL J. Biol. Chem. 279:47672-47680(2004).
RN [13]
RP FUNCTION IN DNA REPAIR, AND INTERACTION WITH XPC.
RX PubMed=15964821; DOI=10.1128/mcb.25.13.5664-5674.2005;
RA Nishi R., Okuda Y., Watanabe E., Mori T., Iwai S., Masutani C.,
RA Sugasawa K., Hanaoka F.;
RT "Centrin 2 stimulates nucleotide excision repair by interacting with
RT xeroderma pigmentosum group C protein.";
RL Mol. Cell. Biol. 25:5664-5674(2005).
RN [14]
RP FUNCTION IN DNA REPAIR.
RX PubMed=17154534; DOI=10.1021/bi061370o;
RA Bunick C.G., Miller M.R., Fuller B.E., Fanning E., Chazin W.J.;
RT "Biochemical and structural domain analysis of xeroderma pigmentosum
RT complementation group C protein.";
RL Biochemistry 45:14965-14979(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [16]
RP INTERACTION WITH SFI1.
RX PubMed=16956364; DOI=10.1111/j.1742-4658.2006.05456.x;
RA Martinez-Sanz J., Yang A., Blouquit Y., Duchambon P., Assairi L.,
RA Craescu C.T.;
RT "Binding of human centrin 2 to the centrosomal protein hSfi1.";
RL FEBS J. 273:4504-4515(2006).
RN [17]
RP FUNCTION, AND INTERACTION WITH CCP110.
RX PubMed=16760425; DOI=10.1091/mbc.e06-04-0371;
RA Tsang W.Y., Spektor A., Luciano D.J., Indjeian V.B., Chen Z.,
RA Salisbury J.L., Sanchez I., Dynlacht B.D.;
RT "CP110 cooperates with two calcium-binding proteins to regulate cytokinesis
RT and genome stability.";
RL Mol. Biol. Cell 17:3423-3434(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-26, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-26, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP INTERACTION WITH TREX-2 COMPLEX, AND FUNCTION.
RX PubMed=22307388; DOI=10.1093/nar/gks059;
RA Jani D., Lutz S., Hurt E., Laskey R.A., Stewart M., Wickramasinghe V.O.;
RT "Functional and structural characterization of the mammalian TREX-2 complex
RT that links transcription with nuclear messenger RNA export.";
RL Nucleic Acids Res. 40:4562-4573(2012).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP FUNCTION, IDENTIFICATION IN THE TREX-2 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=23591820; DOI=10.1242/jcs.118000;
RA Umlauf D., Bonnet J., Waharte F., Fournier M., Stierle M., Fischer B.,
RA Brino L., Devys D., Tora L.;
RT "The human TREX-2 complex is stably associated with the nuclear pore
RT basket.";
RL J. Cell Sci. 126:2656-2667(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [28]
RP STRUCTURE BY NMR OF 84-172, AND CALCIUM-BINDING.
RX PubMed=12578356; DOI=10.1021/bi0269714;
RA Matei E., Miron S., Blouquit Y., Duchambon P., Durussel I., Cox J.A.,
RA Craescu C.T.;
RT "C-terminal half of human centrin 2 behaves like a regulatory EF-hand
RT domain.";
RL Biochemistry 42:1439-1450(2003).
RN [29]
RP STRUCTURE BY NMR OF 1-98, AND CALCIUM-BINDING.
RX PubMed=16411764; DOI=10.1021/bi051397s;
RA Yang A., Miron S., Duchambon P., Assairi L., Blouquit Y., Craescu C.T.;
RT "The N-terminal domain of human centrin 2 has a closed structure, binds
RT calcium with a very low affinity, and plays a role in the protein self-
RT assembly.";
RL Biochemistry 45:880-889(2006).
RN [30]
RP STRUCTURE BY NMR OF 94-172 IN COMPLEX WITH XPC, AND CALCIUM-BINDING.
RX PubMed=16533048; DOI=10.1021/bi0524868;
RA Yang A., Miron S., Mouawad L., Duchambon P., Blouquit Y., Craescu C.T.;
RT "Flexibility and plasticity of human centrin 2 binding to the xeroderma
RT pigmentosum group C protein (XPC) from nuclear excision repair.";
RL Biochemistry 45:3653-3663(2006).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-172 IN COMPLEX WITH CALCIUM
RP IONS AND XPC.
RX PubMed=16627479; DOI=10.1074/jbc.m513667200;
RA Thompson J.R., Ryan Z.C., Salisbury J.L., Kumar R.;
RT "The structure of the human centrin 2-xeroderma pigmentosum group C protein
RT complex.";
RL J. Biol. Chem. 281:18746-18752(2006).
CC -!- FUNCTION: Plays a fundamental role in microtubule organizing center
CC structure and function. Required for centriole duplication and correct
CC spindle formation. Has a role in regulating cytokinesis and genome
CC stability via cooperation with CALM1 and CCP110.
CC -!- FUNCTION: Involved in global genome nucleotide excision repair (GG-NER)
CC by acting as component of the XPC complex. Cooperatively with RAD23B
CC appears to stabilize XPC. In vitro, stimulates DNA binding of the
CC XPC:RAD23B dimer.
CC -!- FUNCTION: The XPC complex is proposed to represent the first factor
CC bound at the sites of DNA damage and together with other core
CC recognition factors, XPA, RPA and the TFIIH complex, is part of the
CC pre-incision (or initial recognition) complex. The XPC complex
CC recognizes a wide spectrum of damaged DNA characterized by distortions
CC of the DNA helix such as single-stranded loops, mismatched bubbles or
CC single-stranded overhangs. The orientation of XPC complex binding
CC appears to be crucial for inducing a productive NER. XPC complex is
CC proposed to recognize and to interact with unpaired bases on the
CC undamaged DNA strand which is followed by recruitment of the TFIIH
CC complex and subsequent scanning for lesions in the opposite strand in a
CC 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers
CC (CPDs) which are formed upon UV-induced DNA damage esacpe detection by
CC the XPC complex due to a low degree of structural perurbation. Instead
CC they are detected by the UV-DDB complex which in turn recruits and
CC cooperates with the XPC complex in the respective DNA repair.
CC -!- FUNCTION: As a component of the TREX-2 complex, involved in the export
CC of mRNAs to the cytoplasm through the nuclear pores.
CC {ECO:0000269|PubMed:22307388, ECO:0000305|PubMed:23591820}.
CC -!- SUBUNIT: Monomer. Homooligomer (PubMed:15356003). Interacts with SFI1
CC (PubMed:16956364). Interacts with CCP110 (PubMed:16760425). Component
CC of the XPC complex composed of XPC, RAD23B and CETN2 (PubMed:11279143,
CC PubMed:15964821, PubMed:16533048, PubMed:16627479). Component of the
CC nuclear pore complex (NPC)-associated TREX-2 complex (transcription and
CC export complex 2), composed of at least GANP, 2 copies of ENY2, PCID2,
CC SEM1/DSS1, and either centrin CETN2 or centrin CETN3. The TREX-2
CC complex also associates with ALYREF/ALY and with the nucleoporin NUP153
CC (PubMed:22307388, PubMed:23591820). {ECO:0000269|PubMed:11279143,
CC ECO:0000269|PubMed:15356003, ECO:0000269|PubMed:15964821,
CC ECO:0000269|PubMed:16533048, ECO:0000269|PubMed:16627479,
CC ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:16956364,
CC ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820}.
CC -!- INTERACTION:
CC P41208; O43303: CCP110; NbExp=3; IntAct=EBI-1789926, EBI-1566217;
CC P41208; P42858: HTT; NbExp=13; IntAct=EBI-1789926, EBI-466029;
CC P41208; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-1789926, EBI-10171633;
CC P41208; Q8NA72: POC5; NbExp=9; IntAct=EBI-1789926, EBI-2561090;
CC P41208; Q8NA72-3: POC5; NbExp=4; IntAct=EBI-1789926, EBI-11751537;
CC P41208; A8K8P3: SFI1; NbExp=4; IntAct=EBI-1789926, EBI-743371;
CC P41208; Q2NKQ1-4: SGSM1; NbExp=6; IntAct=EBI-1789926, EBI-10182463;
CC P41208; Q9H0E7: USP44; NbExp=2; IntAct=EBI-1789926, EBI-2512823;
CC P41208; Q01831: XPC; NbExp=5; IntAct=EBI-1789926, EBI-372610;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:23591820}. Nucleus envelope
CC {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:23591820}. Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Binds two moles of calcium per mole of protein.
CC -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cetn2/";
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DR EMBL; X72964; CAA51467.1; -; mRNA.
DR EMBL; U82671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK311940; BAG34881.1; -; mRNA.
DR EMBL; BT007256; AAP35920.1; -; mRNA.
DR EMBL; AY919675; AAW82436.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72900.1; -; Genomic_DNA.
DR EMBL; BC005334; AAH05334.1; -; mRNA.
DR EMBL; BC013873; AAH13873.1; -; mRNA.
DR CCDS; CCDS14716.1; -.
DR PIR; A49652; A49652.
DR RefSeq; NP_004335.1; NM_004344.1.
DR PDB; 1M39; NMR; -; A=84-172.
DR PDB; 1ZMZ; NMR; -; A=1-98.
DR PDB; 2A4J; NMR; -; A=94-172.
DR PDB; 2GGM; X-ray; 2.35 A; A/B=1-172.
DR PDB; 2K2I; NMR; -; A=94-172.
DR PDB; 2OBH; X-ray; 1.80 A; A/B=26-168.
DR PDBsum; 1M39; -.
DR PDBsum; 1ZMZ; -.
DR PDBsum; 2A4J; -.
DR PDBsum; 2GGM; -.
DR PDBsum; 2K2I; -.
DR PDBsum; 2OBH; -.
DR AlphaFoldDB; P41208; -.
DR SMR; P41208; -.
DR BioGRID; 107496; 100.
DR IntAct; P41208; 59.
DR STRING; 9606.ENSP00000359300; -.
DR iPTMnet; P41208; -.
DR MetOSite; P41208; -.
DR PhosphoSitePlus; P41208; -.
DR BioMuta; CETN2; -.
DR DMDM; 729052; -.
DR EPD; P41208; -.
DR jPOST; P41208; -.
DR MassIVE; P41208; -.
DR MaxQB; P41208; -.
DR PaxDb; P41208; -.
DR PeptideAtlas; P41208; -.
DR PRIDE; P41208; -.
DR ProteomicsDB; 55415; -.
DR TopDownProteomics; P41208; -.
DR Antibodypedia; 30770; 199 antibodies from 28 providers.
DR DNASU; 1069; -.
DR Ensembl; ENST00000370277.5; ENSP00000359300.3; ENSG00000147400.10.
DR GeneID; 1069; -.
DR KEGG; hsa:1069; -.
DR MANE-Select; ENST00000370277.5; ENSP00000359300.3; NM_004344.3; NP_004335.1.
DR UCSC; uc004fgq.4; human.
DR CTD; 1069; -.
DR DisGeNET; 1069; -.
DR GeneCards; CETN2; -.
DR HGNC; HGNC:1867; CETN2.
DR HPA; ENSG00000147400; Tissue enhanced (fallopian).
DR MIM; 300006; gene.
DR neXtProt; NX_P41208; -.
DR OpenTargets; ENSG00000147400; -.
DR PharmGKB; PA26420; -.
DR VEuPathDB; HostDB:ENSG00000147400; -.
DR eggNOG; KOG0028; Eukaryota.
DR GeneTree; ENSGT00940000155935; -.
DR HOGENOM; CLU_061288_18_2_1; -.
DR InParanoid; P41208; -.
DR OMA; YDEFEYM; -.
DR OrthoDB; 1382571at2759; -.
DR PhylomeDB; P41208; -.
DR TreeFam; TF101141; -.
DR PathwayCommons; P41208; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; P41208; -.
DR SIGNOR; P41208; -.
DR BioGRID-ORCS; 1069; 13 hits in 703 CRISPR screens.
DR ChiTaRS; CETN2; human.
DR EvolutionaryTrace; P41208; -.
DR GeneWiki; CETN2; -.
DR GenomeRNAi; 1069; -.
DR Pharos; P41208; Tbio.
DR PRO; PR:P41208; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P41208; protein.
DR Bgee; ENSG00000147400; Expressed in bronchial epithelial cell and 207 other tissues.
DR Genevisible; P41208; HS.
DR GO; GO:0097729; C:9+2 motile cilium; IEA:Ensembl.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0070390; C:transcription export complex 2; IDA:UniProtKB.
DR GO; GO:0071942; C:XPC complex; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:Ensembl.
DR GO; GO:0032795; F:heterotrimeric G-protein binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR CDD; cd00051; EFh; 2.
DR DisProt; DP01259; -.
DR IDEAL; IID00551; -.
DR InterPro; IPR037629; Centrin_2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR PANTHER; PTHR23050:SF305; PTHR23050:SF305; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; DNA damage; DNA repair; Isopeptide bond; Metal-binding;
KW Mitosis; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..172
FT /note="Centrin-2"
FT /id="PRO_0000073561"
FT DOMAIN 28..63
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 64..99
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 101..136
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 137..172
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..25
FT /note="Required for self-assembly"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1ZMZ"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:2OBH"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2OBH"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2OBH"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:2OBH"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:2OBH"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2OBH"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2OBH"
FT HELIX 86..113
FT /evidence="ECO:0007829|PDB:2OBH"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:2A4J"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2OBH"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:2OBH"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:2OBH"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:2A4J"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:2OBH"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:2OBH"
SQ SEQUENCE 172 AA; 19738 MW; 59CFD706AD7011B5 CRC64;
MASNFKKANM ASSSQRKRMS PKPELTEEQK QEIREAFDLF DADGTGTIDV KELKVAMRAL
GFEPKKEEIK KMISEIDKEG TGKMNFGDFL TVMTQKMSEK DTKEEILKAF KLFDDDETGK
ISFKNLKRVA KELGENLTDE ELQEMIDEAD RDGDGEVSEQ EFLRIMKKTS LY
