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Protein

Centrin-2

Gene

Cetn2

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity
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 (By similarity).By similarity
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 (By similarity).By similarity
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. 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.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi114 – 125121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi150 – 161122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • calcium ion binding Source: MGI
  • G-protein beta/gamma-subunit complex binding Source: MGI
  • heterotrimeric G-protein binding Source: MGI
  • microtubule binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-5696394. DNA Damage Recognition in GG-NER.
R-MMU-5696395. Formation of Incision Complex in GG-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
Centrin-2
Alternative name(s):
Caltractin isoform 1
Gene namesi
Name:Cetn2
Synonyms:Calt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1347085. Cetn2.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: MGI
  • centrosome Source: MGI
  • ciliary basal body Source: UniProtKB
  • cilium Source: UniProtKB
  • intracellular Source: MGI
  • photoreceptor connecting cilium Source: MGI
  • XPC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 172171Centrin-2PRO_0000073562Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei20 – 201PhosphoserineCombined sources
Modified residuei26 – 261PhosphothreonineBy similarity
Modified residuei138 – 1381PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9R1K9.
MaxQBiQ9R1K9.
PaxDbiQ9R1K9.
PRIDEiQ9R1K9.

PTM databases

iPTMnetiQ9R1K9.
PhosphoSiteiQ9R1K9.

Expressioni

Tissue specificityi

Ubiquitously expressed in all adult tissues tested, with strongest expression in brain, spleen, kidney, small intestine and ovary. Also expressed in the NIH 3T3 fibroblast cell line and peripheral blood lymphocytes.1 Publication

Gene expression databases

BgeeiQ9R1K9.
CleanExiMM_CETN2.
ExpressionAtlasiQ9R1K9. baseline and differential.
GenevisibleiQ9R1K9. MM.

Interactioni

Subunit structurei

Monomer. Homooligomer. Interacts with CCP110, SFI1. Component of the XPC complex composed of XPC, RAD23B and CETN2 (By similarity). 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 (By similarity).By similarity

GO - Molecular functioni

  • G-protein beta/gamma-subunit complex binding Source: MGI
  • heterotrimeric G-protein binding Source: MGI
  • microtubule binding Source: MGI

Protein-protein interaction databases

BioGridi204930. 29 interactions.
IntActiQ9R1K9. 31 interactions.
STRINGi10090.ENSMUSP00000110198.

Structurei

3D structure databases

ProteinModelPortaliQ9R1K9.
SMRiQ9R1K9. Positions 24-172.
ModBaseiSearch...
MobiDBiSearch...

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-assemblyBy similarityAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0028. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00670000097718.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiQ9R1K9.
KOiK10840.
OMAiMIDTKEL.
OrthoDBiEOG7H1JN9.
PhylomeDBiQ9R1K9.
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:SF180. PTHR23050:SF180. 1 hit.
PfamiPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
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.

Q9R1K9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASNFKKTTM ASSAQRKRMS PKPELTEDQK QEIREAFDLF DADGTGTIDI
60 70 80 90 100
KELKVAMRAL GFEPKKEEIK KMISEIDKEG TGKMNFSDFL TVMTQKMSEK
110 120 130 140 150
DTKEEILKAF KLFDDDETGK ISFKNLKRVA KELGENLTDE ELQEMIDEAD
160 170
RDGDGEVNEQ EFLRIMKKTS LY
Length:172
Mass (Da):19,797
Last modified:May 1, 2000 - v1
Checksum:i75311C8386861567
GO

Sequence cautioni

The sequence CAM20357.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341R → P in BAB27017 (PubMed:16141072).Curated
Sequence conflicti76 – 761I → N in BAB27017 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF080592 Genomic DNA. Translation: AAD46391.1.
AL021127 Genomic DNA. Translation: CAB88169.1.
AK004081 mRNA. Translation: BAB23161.1.
AK010541 mRNA. Translation: BAB27017.1.
AK140156 mRNA. Translation: BAE24259.1.
AK151033 mRNA. Translation: BAE30050.1.
AL671908 Genomic DNA. Translation: CAM20357.1. Sequence problems.
AL671908 Genomic DNA. Translation: CAM20359.1.
CH466624 Genomic DNA. Translation: EDL26558.1.
BC013545 mRNA. Translation: AAH13545.1.
CCDSiCCDS41003.1.
RefSeqiNP_062278.2. NM_019405.6.
UniGeneiMm.24643.

Genome annotation databases

EnsembliENSMUST00000114551; ENSMUSP00000110198; ENSMUSG00000031347.
GeneIDi26370.
KEGGimmu:26370.
UCSCiuc009tkt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF080592 Genomic DNA. Translation: AAD46391.1.
AL021127 Genomic DNA. Translation: CAB88169.1.
AK004081 mRNA. Translation: BAB23161.1.
AK010541 mRNA. Translation: BAB27017.1.
AK140156 mRNA. Translation: BAE24259.1.
AK151033 mRNA. Translation: BAE30050.1.
AL671908 Genomic DNA. Translation: CAM20357.1. Sequence problems.
AL671908 Genomic DNA. Translation: CAM20359.1.
CH466624 Genomic DNA. Translation: EDL26558.1.
BC013545 mRNA. Translation: AAH13545.1.
CCDSiCCDS41003.1.
RefSeqiNP_062278.2. NM_019405.6.
UniGeneiMm.24643.

3D structure databases

ProteinModelPortaliQ9R1K9.
SMRiQ9R1K9. Positions 24-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204930. 29 interactions.
IntActiQ9R1K9. 31 interactions.
STRINGi10090.ENSMUSP00000110198.

PTM databases

iPTMnetiQ9R1K9.
PhosphoSiteiQ9R1K9.

Proteomic databases

EPDiQ9R1K9.
MaxQBiQ9R1K9.
PaxDbiQ9R1K9.
PRIDEiQ9R1K9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000114551; ENSMUSP00000110198; ENSMUSG00000031347.
GeneIDi26370.
KEGGimmu:26370.
UCSCiuc009tkt.1. mouse.

Organism-specific databases

CTDi1069.
MGIiMGI:1347085. Cetn2.

Phylogenomic databases

eggNOGiKOG0028. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00670000097718.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiQ9R1K9.
KOiK10840.
OMAiMIDTKEL.
OrthoDBiEOG7H1JN9.
PhylomeDBiQ9R1K9.
TreeFamiTF101141.

Enzyme and pathway databases

ReactomeiR-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-5696394. DNA Damage Recognition in GG-NER.
R-MMU-5696395. Formation of Incision Complex in GG-NER.

Miscellaneous databases

NextBioi304261.
PROiQ9R1K9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R1K9.
CleanExiMM_CETN2.
ExpressionAtlasiQ9R1K9. baseline and differential.
GenevisibleiQ9R1K9. MM.

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:SF180. PTHR23050:SF180. 1 hit.
PfamiPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: 129/Ola.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Corpora quadrigemina and Embryo.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Kidney.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Liver, Lung and Spleen.

Entry informationi

Entry nameiCETN2_MOUSE
AccessioniPrimary (citable) accession number: Q9R1K9
Secondary accession number(s): B1AUQ6
, B1AUQ8, Q3UBB4, Q9CWM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds two moles of calcium per mole of protein.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.