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Protein

Centrin-2

Gene

CETN2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.
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.
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.
Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, DSS1, and either centrin CETN2 or CETN3 (PubMed:22307388). The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery (PubMed:22307388).1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi114 – 125121Add
BLAST
Calcium bindingi150 – 161122Add
BLAST

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cellular protein metabolic process Source: Reactome
  • centriole replication Source: UniProtKB
  • G2/M transition of mitotic cell cycle Source: Reactome
  • mitotic cell cycle Source: Reactome
  • mitotic nuclear division Source: UniProtKB
  • nucleotide-excision repair Source: UniProtKB
  • organelle organization Source: Reactome
  • post-translational protein modification Source: Reactome
  • protein sumoylation Source: Reactome
  • regulation of cytokinesis Source: UniProtKB
  • 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.
REACT_267965. Anchoring of the basal body to the plasma membrane.
REACT_355174. SUMOylation of DNA damage response and repair proteins.

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 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:1867. CETN2.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: UniProtKB
  • centrosome Source: UniProtKB
  • ciliary basal body Source: Ensembl
  • cytosol Source: Reactome
  • intracellular Source: LIFEdb
  • nucleoplasm Source: Reactome
  • photoreceptor connecting cilium Source: Ensembl
  • XPC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26420.

Polymorphism and mutation databases

BioMutaiCETN2.
DMDMi729052.

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
Modified residuei138 – 1381PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP41208.
PaxDbiP41208.
PRIDEiP41208.

PTM databases

PhosphoSiteiP41208.

Expressioni

Gene expression databases

BgeeiP41208.
CleanExiHS_CETN2.
GenevisibleiP41208. HS.

Organism-specific databases

HPAiHPA028956.

Interactioni

Subunit structurei

Monomer. Homooligomer. Interacts with CCP110, SFI1. Component of the XPC complex composed of XPC, RAD23B and CETN2. Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, DSS1, and either centrin CETN2 or CETN3 (PubMed:22307388).8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCP110O433033EBI-1789926,EBI-1566217
PNMA5Q96PV43EBI-1789926,EBI-10171633
POC5Q8NA725EBI-1789926,EBI-2561090
SFI1A8K8P34EBI-1789926,EBI-743371
SGSM1Q2NKQ1-43EBI-1789926,EBI-10182463
XPCQ018313EBI-1789926,EBI-372610

Protein-protein interaction databases

BioGridi107496. 27 interactions.
IntActiP41208. 12 interactions.
MINTiMINT-3015206.
STRINGi9606.ENSP00000359300.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41208.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the centrin family.Curated
Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00670000097718.
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

        10         20         30         40         50
MASNFKKANM ASSSQRKRMS PKPELTEEQK QEIREAFDLF DADGTGTIDV
60 70 80 90 100
KELKVAMRAL GFEPKKEEIK KMISEIDKEG TGKMNFGDFL TVMTQKMSEK
110 120 130 140 150
DTKEEILKAF KLFDDDETGK ISFKNLKRVA KELGENLTDE ELQEMIDEAD
160 170
RDGDGEVSEQ EFLRIMKKTS LY
Length:172
Mass (Da):19,738
Last modified:February 1, 1995 - v1
Checksum:i59CFD706AD7011B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
GeneIDi1069.
KEGGihsa:1069.
UCSCiuc004fgq.3. human.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107496. 27 interactions.
IntActiP41208. 12 interactions.
MINTiMINT-3015206.
STRINGi9606.ENSP00000359300.

PTM databases

PhosphoSiteiP41208.

Polymorphism and mutation databases

BioMutaiCETN2.
DMDMi729052.

Proteomic databases

MaxQBiP41208.
PaxDbiP41208.
PRIDEiP41208.

Protocols and materials databases

DNASUi1069.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1069.
GeneCardsiGC0XM151996.
HGNCiHGNC:1867. CETN2.
HPAiHPA028956.
MIMi300006. gene.
neXtProtiNX_P41208.
PharmGKBiPA26420.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00670000097718.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP41208.
KOiK10840.
OMAiLMTVKMA.
OrthoDBiEOG7H1JN9.
PhylomeDBiP41208.
TreeFamiTF101141.

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.
REACT_355174. SUMOylation of DNA damage response and repair proteins.

Miscellaneous databases

EvolutionaryTraceiP41208.
GeneWikiiCETN2.
GenomeRNAii1069.
NextBioi4464.
PROiP41208.
SOURCEiSearch...

Gene expression databases

BgeeiP41208.
CleanExiHS_CETN2.
GenevisibleiP41208. HS.

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]
ProtoNetiSearch...

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. "Functional and structural characterization of the mammalian TREX-2 complex that links transcription with nuclear messenger RNA export."
    Jani D., Lutz S., Hurt E., Laskey R.A., Stewart M., Wickramasinghe V.O.
    Nucleic Acids Res. 40:4562-4573(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TREX-2 COMPLEX, FUNCTION.
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  23. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. "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.
  25. "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.
  26. "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.
  27. "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: July 22, 2015
This is version 164 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

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.