Details for: CETN2

Gene ID: 1069

Symbol: CETN2

Ensembl ID: ENSG00000147400

Description: centrin 2

Associated with

Other Information

Genular Protein ID: 3782472839

Symbol: CETN2_HUMAN

Name: Centrin-2

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 8248209

Title: Molecular cloning and centrosomal localization of human caltractin.

PubMed ID: 8248209

DOI: 10.1073/pnas.90.23.11039

PubMed ID: 10854409

Title: Comparative genome sequence analysis of the Bpa/Str region in mouse and man.

PubMed ID: 10854409

DOI: 10.1101/gr.10.6.758

PubMed ID: 15772651

Title: The DNA sequence of the human X chromosome.

PubMed ID: 15772651

DOI: 10.1038/nature03440

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 11279143

Title: Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair.

PubMed ID: 11279143

DOI: 10.1074/jbc.m100855200

PubMed ID: 12176356

Title: Centrin-2 is required for centriole duplication in mammalian cells.

PubMed ID: 12176356

DOI: 10.1016/s0960-9822(02)01019-9

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 15356003

Title: Calcium-dependent self-assembly of human centrin 2.

PubMed ID: 15356003

DOI: 10.1074/jbc.m404996200

PubMed ID: 15964821

Title: Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein.

PubMed ID: 15964821

DOI: 10.1128/mcb.25.13.5664-5674.2005

PubMed ID: 17154534

Title: Biochemical and structural domain analysis of xeroderma pigmentosum complementation group C protein.

PubMed ID: 17154534

DOI: 10.1021/bi061370o

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16956364

Title: Binding of human centrin 2 to the centrosomal protein hSfi1.

PubMed ID: 16956364

DOI: 10.1111/j.1742-4658.2006.05456.x

PubMed ID: 16760425

Title: CP110 cooperates with two calcium-binding proteins to regulate cytokinesis and genome stability.

PubMed ID: 16760425

DOI: 10.1091/mbc.e06-04-0371

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22307388

Title: Functional and structural characterization of the mammalian TREX-2 complex that links transcription with nuclear messenger RNA export.

PubMed ID: 22307388

DOI: 10.1093/nar/gks059

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23591820

Title: The human TREX-2 complex is stably associated with the nuclear pore basket.

PubMed ID: 23591820

DOI: 10.1242/jcs.118000

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 12578356

Title: C-terminal half of human centrin 2 behaves like a regulatory EF-hand domain.

PubMed ID: 12578356

DOI: 10.1021/bi0269714

PubMed ID: 16411764

Title: 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.

PubMed ID: 16411764

DOI: 10.1021/bi051397s

PubMed ID: 16533048

Title: Flexibility and plasticity of human centrin 2 binding to the xeroderma pigmentosum group C protein (XPC) from nuclear excision repair.

PubMed ID: 16533048

DOI: 10.1021/bi0524868

PubMed ID: 16627479

Title: The structure of the human centrin 2-xeroderma pigmentosum group C protein complex.

PubMed ID: 16627479

DOI: 10.1074/jbc.m513667200

Sequence Information:

  • Length: 172
  • Mass: 19738
  • Checksum: 59CFD706AD7011B5
  • Sequence:
  • MASNFKKANM ASSSQRKRMS PKPELTEEQK QEIREAFDLF DADGTGTIDV KELKVAMRAL 
    GFEPKKEEIK KMISEIDKEG TGKMNFGDFL TVMTQKMSEK DTKEEILKAF KLFDDDETGK 
    ISFKNLKRVA KELGENLTDE ELQEMIDEAD RDGDGEVSEQ EFLRIMKKTS LY

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.