Reviewed, UniProtKB/Swiss-Prot P41208 (CETN2_HUMAN)

Names and origin

Protein names

Recommended name:
    Centrin-2
Alternative name(s):
    Caltractin isoform 1

Gene names

Name:	CETN2
Synonyms:	CALT, CEN2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	172 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 CEP110. Ref.1 Ref.8 Ref.11
Subunit structure	Monomer. Interacts with CEP110, SFI1 and with XPC. Ref.11 Ref.10
Subcellular location	Centrosome › centriole. Note: Centrosome of S-phase, interphase and mitotic cells. Ref.1 Ref.8
Miscellaneous	Binds two moles of calcium per mole of protein.
Sequence similarities	Belongs to the centrin family. Contains 4 EF-hand domains.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Domain	Repeat
Ligand	Calcium
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW centriole replication Ref.8 Inferred from mutant phenotype. Source: UniProtKB mitosis Ref.1 Non-traceable author statement. Source: UniProtKB regulation of cytokinesis Ref.11 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	centriole Ref.8 Inferred from direct assay. Source: UniProtKB
Molecular function	calcium ion binding Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CEP110	O43303	2	EBI-1789926,EBI-1566217

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 172

172

Centrin-2

PRO_0000073561

Regions

Domain

28 – 63

36

EF-hand 1

Domain

64 – 99

36

EF-hand 2

Domain

101 – 136

36

EF-hand 3

Domain

137 – 172

36

EF-hand 4

Calcium binding

114 – 125

12

1

Calcium binding

150 – 161

12

2

Amino acid modifications

Modified residue

20

1

Phosphoserine Ref.9 Ref.12 Ref.13

Modified residue

26

1

Phosphothreonine Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

172

Helix Strand Turn

Details...

Helix

28 – 39

12

Beta strand

46 – 49

4

Helix

50 – 52

3

Helix

53 – 59

7

Helix

66 – 76

11

Turn

77 – 79

3

Beta strand

82 – 85

4

Helix

86 – 113

28

Beta strand

119 – 121

3

Helix

123 – 132

10

Helix

139 – 149

11

Beta strand

151 – 157

7

Helix

159 – 167

9

Sequences

	Sequence		Length	Mass (Da)
	P41208-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 59CFD706AD7011B5	FASTA	172	19,738
	10 20 30 40 50 60 MASNFKKANM ASSSQRKRMS PKPELTEEQK QEIREAFDLF DADGTGTIDV KELKVAMRAL 70 80 90 100 110 120 GFEPKKEEIK KMISEIDKEG TGKMNFGDFL TVMTQKMSEK DTKEEILKAF KLFDDDETGK 130 140 150 160 170 ISFKNLKRVA KELGENLTDE ELQEMIDEAD RDGDGEVSEQ EFLRIMKKTS LY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8248209] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION. Tissue: Umbilical vein.
[2]	"Comparative genome sequence analysis of the Bpa/Str region in mouse and man." Mallon A.-M., Platzer M., Bate R., Gloeckner G., Botcherby M.R.M., Nordsiek G., Strivens M.A., Kioschis P., Dangel A., Cunningham D., Straw R.N.A., Weston P., Gilbert M., Fernando S., Goodall K., Hunter G., Greystrong J.S., Clarke D. , Kimberley C., Goerdes M., Blechschmidt K., Rump A., Hinzmann B., Mundy C.R., Miller W., Poustka A., Herman G.E., Rhodes M., Denny P., Rosenthal A., Brown S.D.M. Genome Res. 10:758-775(2000) [PubMed: 10854409] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Fetal brain.
[4]	"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].
[5]	NIEHS SNPs program Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary and Urinary bladder.
[8]	"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: 12176356] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-26, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"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: 16956364] [Abstract] Cited for: INTERACTION WITH SFI1.
[11]	"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: 16760425] [Abstract] Cited for: FUNCTION, INTERACTION WITH CEP110.
[12]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, MASS SPECTROMETRY.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, MASS SPECTROMETRY.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]	"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: 12578356] [Abstract] Cited for: STRUCTURE BY NMR OF 84-172, CALCIUM BINDING.
[16]	"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: 16411764] [Abstract] Cited for: STRUCTURE BY NMR OF 1-98, CALCIUM BINDING.
[17]	"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: 16533048] [Abstract] Cited for: STRUCTURE BY NMR OF 94-172 IN COMPLEX WITH XPC, CALCIUM BINDING.
[18]	"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: 16627479] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-172 IN COMPLEX WITH CALCIUM IONS AND XPC.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00215928.

PIR

A49652.

RefSeq

NP_004335.1.

UniGene

Hs.82794

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P41208. 1 interaction.

PTM databases

PhosphoSite

P41208.

Proteomic databases

PRIDE

P41208.

Genome annotation databases

Ensembl

ENSG00000147400. Homo sapiens. [Contig view]

GeneID

1069.

KEGG

hsa:1069.

NMPDR

fig|9606.3.peg.33572.

UCSC

uc004fgq.1. human.

Organism-specific databases

GeneCards

GC0XM151746.

H-InvDB

HIX0017121.

HGNC

HGNC:1867. CETN2.

MIM

300006. gene.

PharmGKB

PA26420.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P41208.

HOVERGEN

P41208.

OMA

P41208. RIMKKTC.

Enzyme and pathway databases

Reactome

REACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpress

P41208.

Bgee

P41208.

CleanEx

HS_CETN2.

GermOnline

ENSG00000147400. Homo sapiens.

Family and domain databases

InterPro

IPR011992. EF-Hand_type.
IPR018248. EF_hand.
IPR018247. EF_HAND_1.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
[Graphical view]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 1 hit.

Pfam

PF00036. efhand. 4 hits.
[Graphical view]

ProDom

PD000012. EF-hand. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00054. EFh. 4 hits.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

4464.

SOURCE

Search...

Entry information

Entry name

CETN2_HUMAN

Accession

Primary (citable) accession number: P41208
Secondary accession number(s): B2R4T4, Q53XW1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	July 7, 2009
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)