P41208 (CETN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	172 AA.
Sequence status	Complete.
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.9 Ref.10 Ref.12 Ref.13 Ref.16 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. Ref.1 Ref.9 Ref.10 Ref.12 Ref.13 Ref.16 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. Ref.1 Ref.9 Ref.10 Ref.12 Ref.13 Ref.16
Subunit structure	Monomer. Homooligomer. Interacts with CEP110, SFI1. Component of the XPC complex composed of XPC, RAD23B and CETN2. Ref.9 Ref.11 Ref.12 Ref.15 Ref.16
Subcellular location	Cytoplasm › cytoskeleton › centrosome › centriole. Nucleus Probable. Note: Centrosome of S-phase, interphase and mitotic cells. Ref.1 Ref.10
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 DNA damage DNA repair Mitosis
Cellular component	Cytoplasm Cytoskeleton Nucleus
Domain	Repeat
Ligand	Calcium Metal-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW centriole replication Inferred from mutant phenotype Ref.10. Source: UniProtKB mitosis Non-traceable author statement Ref.1. Source: UniProtKB nucleotide-excision repair Inferred from direct assay Ref.12. Source: UniProtKB regulation of cytokinesis Inferred from mutant phenotype Ref.16. Source: UniProtKB spermatogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	XPC complex Inferred from direct assay Ref.9. Source: UniProtKB centriole Inferred from direct assay Ref.10. Source: UniProtKB cytosol Traceable author statement. Source: Reactome microtubule basal body Inferred from electronic annotation. Source: Compara photoreceptor connecting cilium Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro calcium ion binding Non-traceable author statement Ref.1. Source: UniProtKB nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCP110	O43303	3	EBI-1789926,EBI-1566217
SFI1	A8K8P3	4	EBI-1789926,EBI-743371
XPC	Q01831	3	EBI-1789926,EBI-372610

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 Ref.21 Ref.22 Ref.23

Calcium binding

150 – 161

12

2 Ref.21 Ref.22 Ref.23

Region

1 – 25

25

Required for self-assembly

Amino acid modifications

Modified residue

20

1

Phosphoserine Ref.17 Ref.18 Ref.20

Modified residue

26

1

Phosphothreonine Ref.14 Ref.18 Ref.20

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

172

Helix Strand Turn

Details...

Beta strand

22 – 24

3

Helix

27 – 38

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

115 – 117

3

Beta strand

118 – 121

4

Helix

123 – 132

10

Helix

139 – 149

11

Beta strand

150 – 152

3

Beta strand

153 – 157

5

Helix

159 – 166

8

Sequences

	Sequence		Length	Mass (Da)
	P41208 [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] [Europe PMC] [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] [Europe PMC] [Abstract] 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]	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].
[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]	"Calcium-dependent self-assembly of human centrin 2." Tourbez M., Firanescu C., Yang A., Unipan L., Duchambon P., Blouquit Y., Craescu C.T. J. Biol. Chem. 279:47672-47680(2004) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. 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 CEP110.
[17]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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. NM_004344.1.

UniGene

Hs.82794.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P41208.

ModBase

Search...

Protein-protein interaction databases

IntAct

P41208. 9 interactions.

MINT

MINT-3015206.

STRING

9606.ENSP00000359300.

PTM databases

PhosphoSite

P41208.

Polymorphism databases

DMDM

729052.

Proteomic databases

PaxDb

P41208.

PRIDE

P41208.

Protocols and materials databases

DNASU

1069.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000370277; ENSP00000359300; ENSG00000147400.
ENST00000601896; ENSP00000469720; ENSG00000268512.

GeneID

1069.

KEGG

hsa:1069.

UCSC

uc004fgq.3. human.

Organism-specific databases

CTD

1069.

GeneCards

GC0XM151996.

HGNC

HGNC:1867. CETN2.

HPA

HPA028956.

MIM

300006. gene.

neXtProt

NX_P41208.

PharmGKB

PA26420.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5126.

HOGENOM

HOG000233018.

HOVERGEN

HBG012180.

InParanoid

P41208.

KO

K10840.

OMA

RDSREEM.

OrthoDB

EOG4NZTVG.

PhylomeDB

P41208.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.

Gene expression databases

Bgee

P41208.

CleanEx

HS_CETN2.

Genevestigator

P41208.

GermOnline

ENSG00000147400. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 2 hits.

InterPro

IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000629. RNA-helicase_DEAD-box_CS.
[Graphical view]

Pfam

PF13499. EF_hand_5. 1 hit.
[Graphical view]

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

EvolutionaryTrace

P41208.

GenomeRNAi

1069.

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:	May 29, 2013
This is version 141 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.