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P41208

- CETN2_HUMAN

UniProt

P41208 - CETN2_HUMAN

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Protein

Centrin-2

Gene
CETN2, CALT, CEN2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 CCP110.6 Publications
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.6 Publications
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.6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi114 – 1251213 PublicationsAdd
BLAST
Calcium bindingi150 – 1611223 PublicationsAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. ATP-dependent helicase activity Source: InterPro
  3. calcium ion binding Source: UniProtKB
  4. nucleic acid binding Source: InterPro
  5. protein binding Source: UniProtKB

GO - Biological processi

  1. centriole replication Source: UniProtKB
  2. G2/M transition of mitotic cell cycle Source: Reactome
  3. mitotic cell cycle Source: Reactome
  4. mitotic nuclear division Source: UniProtKB
  5. nucleotide-excision repair Source: UniProtKB
  6. regulation of cytokinesis Source: UniProtKB
  7. spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA repair, Mitosis

Keywords - Ligandi

Calcium, Metal-binding

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:
Centrin-2
Alternative name(s):
Caltractin isoform 1
Gene namesi
Name:CETN2
Synonyms:CALT, CEN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:1867. CETN2.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Nucleus Inferred
Note: Centrosome of S-phase, interphase and mitotic cells.2 Publications

GO - Cellular componenti

  1. centriole Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. cytosol Source: Reactome
  4. intracellular Source: LIFEdb
  5. photoreceptor connecting cilium Source: Ensembl
  6. XPC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26420.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 172171Centrin-2PRO_0000073561Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei20 – 201Phosphoserine3 Publications
Modified residuei26 – 261Phosphothreonine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP41208.
PaxDbiP41208.
PRIDEiP41208.

PTM databases

PhosphoSiteiP41208.

Expressioni

Gene expression databases

BgeeiP41208.
CleanExiHS_CETN2.
GenevestigatoriP41208.

Organism-specific databases

HPAiHPA028956.

Interactioni

Subunit structurei

Monomer. Homooligomer. Interacts with CCP110, SFI1. Component of the XPC complex composed of XPC, RAD23B and CETN2.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCP110O433033EBI-1789926,EBI-1566217
SFI1A8K8P34EBI-1789926,EBI-743371
XPCQ018313EBI-1789926,EBI-372610

Protein-protein interaction databases

BioGridi107496. 15 interactions.
IntActiP41208. 9 interactions.
MINTiMINT-3015206.
STRINGi9606.ENSP00000359300.

Structurei

Secondary structure

1
172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 243
Helixi27 – 3812
Beta strandi46 – 494
Helixi50 – 523
Helixi53 – 597
Helixi66 – 7611
Turni77 – 793
Beta strandi82 – 854
Helixi86 – 11328
Beta strandi115 – 1173
Beta strandi118 – 1214
Helixi123 – 13210
Helixi139 – 14911
Beta strandi150 – 1523
Beta strandi153 – 1575
Helixi159 – 1668

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP41208.
SMRiP41208. Positions 26-168.

Miscellaneous databases

EvolutionaryTraceiP41208.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 6336EF-hand 1Add
BLAST
Domaini64 – 9936EF-hand 2Add
BLAST
Domaini101 – 13636EF-hand 3Add
BLAST
Domaini137 – 17236EF-hand 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2524Required for self-assemblyAdd
BLAST

Sequence similaritiesi

Belongs to the centrin family.
Contains 4 EF-hand domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5126.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP41208.
KOiK10840.
OMAiLMTVKMA.
OrthoDBiEOG7H1JN9.
PhylomeDBiP41208.
TreeFamiTF101141.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR029528. CETN2.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000629. RNA-helicase_DEAD-box_CS.
[Graphical view]
PANTHERiPTHR23050:SF135. PTHR23050:SF135. 1 hit.
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P41208-1 [UniParc]FASTAAdd to Basket

« Hide

MASNFKKANM ASSSQRKRMS PKPELTEEQK QEIREAFDLF DADGTGTIDV    50
KELKVAMRAL GFEPKKEEIK KMISEIDKEG TGKMNFGDFL TVMTQKMSEK 100
DTKEEILKAF KLFDDDETGK ISFKNLKRVA KELGENLTDE ELQEMIDEAD 150
RDGDGEVSEQ EFLRIMKKTS LY 172
Length:172
Mass (Da):19,738
Last modified:February 1, 1995 - v1
Checksum:i59CFD706AD7011B5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14716.1.
PIRiA49652.
RefSeqiNP_004335.1. NM_004344.1.
UniGeneiHs.82794.

Genome annotation databases

EnsembliENST00000370277; ENSP00000359300; ENSG00000147400.
ENST00000601896; ENSP00000469720; ENSG00000268512.
GeneIDi1069.
KEGGihsa:1069.
UCSCiuc004fgq.3. human.

Polymorphism databases

DMDMi729052.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14716.1.
PIRi A49652.
RefSeqi NP_004335.1. NM_004344.1.
UniGenei Hs.82794.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M39 NMR - A 84-172 [» ]
1ZMZ NMR - A 1-98 [» ]
2A4J NMR - A 94-172 [» ]
2GGM X-ray 2.35 A/B 1-172 [» ]
2K2I NMR - A 94-172 [» ]
2OBH X-ray 1.80 A/B 26-168 [» ]
ProteinModelPortali P41208.
SMRi P41208. Positions 26-168.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107496. 15 interactions.
IntActi P41208. 9 interactions.
MINTi MINT-3015206.
STRINGi 9606.ENSP00000359300.

PTM databases

PhosphoSitei P41208.

Polymorphism databases

DMDMi 729052.

Proteomic databases

MaxQBi P41208.
PaxDbi P41208.
PRIDEi P41208.

Protocols and materials databases

DNASUi 1069.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370277 ; ENSP00000359300 ; ENSG00000147400 .
ENST00000601896 ; ENSP00000469720 ; ENSG00000268512 .
GeneIDi 1069.
KEGGi hsa:1069.
UCSCi uc004fgq.3. human.

Organism-specific databases

CTDi 1069.
GeneCardsi GC0XM151996.
HGNCi HGNC:1867. CETN2.
HPAi HPA028956.
MIMi 300006. gene.
neXtProti NX_P41208.
PharmGKBi PA26420.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5126.
HOGENOMi HOG000233018.
HOVERGENi HBG012180.
InParanoidi P41208.
KOi K10840.
OMAi LMTVKMA.
OrthoDBi EOG7H1JN9.
PhylomeDBi P41208.
TreeFami TF101141.

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

EvolutionaryTracei P41208.
GeneWikii CETN2.
GenomeRNAii 1069.
NextBioi 4464.
PROi P41208.
SOURCEi Search...

Gene expression databases

Bgeei P41208.
CleanExi HS_CETN2.
Genevestigatori P41208.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
InterProi IPR029528. CETN2.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000629. RNA-helicase_DEAD-box_CS.
[Graphical view ]
PANTHERi PTHR23050:SF135. PTHR23050:SF135. 1 hit.
Pfami PF13499. EF-hand_7. 1 hit.
[Graphical view ]
SMARTi SM00054. EFh. 4 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiCETN2_HUMAN
AccessioniPrimary (citable) accession number: P41208
Secondary accession number(s): B2R4T4, Q53XW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 3, 2014
This is version 153 of the entry and version 1 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

Miscellaneous

Binds two moles of calcium per mole of protein.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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