Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P41208

- CETN2_HUMAN

UniProt

P41208 - CETN2_HUMAN

Protein

Centrin-2

Gene

CETN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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.

    Regions

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

    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 Curated
    Note: Centrosome of S-phase, interphase and mitotic cells.

    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

    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 CETN2.7 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.
    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.
    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.
    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 .
    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

    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: October 1, 2014
    This is version 154 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