P30307 (MPIP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
M-phase inducer phosphatase 3
EC=3.1.3.48

Alternative name(s):
Dual specificity phosphatase Cdc25C

Gene names

Name:

CDC25C

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as a dosage-dependent inducer in mitotic control. It is a tyrosine protein phosphatase required for progression of the cell cycle. It directly dephosphorylates CDK1 and activate its kinase activity.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Interacts with HIV-1 Vpr, thereby inactivating CDC25C phosphatase activity. Interacts with MAPK14 and 14-3-3 proteins. Ref.10 Ref.13
Subcellular location	Nucleus Ref.12.
Developmental stage	Expressed predominantly in G2 phase.
Post-translational modification	Phosphorylated by CHEK1 and MAPK14 at Ser-216. This phosphorylation creates a binding site for 14-3-3 protein and inhibits the phosphatase. Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity. Phosphorylation by PLK3 at Ser-191 promotes nuclear translocation. Ser-198 is a minor phosphorylation site. Was initially reported to be phosphorylated by PLK3 at Ser-216 (Ref.8). However, such phosphorylation by PLK3 was not confirmed by other groups. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18
Sequence similarities	Belongs to the MPI phosphatase family. Contains 1 rhodanese domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Host-virus interaction Mitosis
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Traceable author statement. Source: Reactome G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome cell cycle checkpoint Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Traceable author statement Ref.6. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW regulation of cyclin-dependent protein kinase activity Traceable author statement Ref.6. Source: UniProtKB regulation of mitosis Traceable author statement. Source: ProtInc traversing start control point of mitotic cell cycle Traceable author statement. Source: ProtInc
Cellular component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular function	WW domain binding Inferred from physical interaction. Source: BHF-UCL protein kinase binding Inferred from physical interaction Ref.12. Source: UniProtKB protein tyrosine phosphatase activity Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDK1	P06493	2	EBI-974439,EBI-444308
CHEK1	O14757	2	EBI-974439,EBI-974488
LZTS1	Q9Y250	2	EBI-974439,EBI-1216080

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P30307-1)

Also known as: CDC25C1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P30307-2)

Also known as: CDC25C2;

The sequence of this isoform differs from the canonical sequence as follows:
     124-153: Missing.

Isoform 3 (identifier: P30307-5)

Also known as: CDC25C3;

The sequence of this isoform is not available.

Isoform 4 (identifier: P30307-3)

Also known as: CDC25C4;

The sequence of this isoform differs from the canonical sequence as follows:
     66-123: GTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSP → SPGFFRTSGSAFSWD

Isoform 5 (identifier: P30307-4)

Also known as: CDC25C5; Cdc25Cdm;

The sequence of this isoform differs from the canonical sequence as follows:
     66-123: GTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSP → SPGFFRTSGSAFSWD
     124-153: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 473

473

M-phase inducer phosphatase 3

PRO_0000198647

Regions

Domain

321 – 428

108

Rhodanese

Region

334 – 379

46

HIV-1 Vpr binding site

Sites

Active site

377

1

By similarity

Amino acid modifications

Modified residue

15

1

Phosphoserine Ref.17

Modified residue

38

1

Phosphoserine Ref.18

Modified residue

48

1

Phosphothreonine Ref.18

Modified residue

57

1

Phosphoserine Ref.18

Modified residue

61

1

Phosphoserine Ref.18

Modified residue

64

1

Phosphoserine Ref.17 Ref.18

Modified residue

67

1

Phosphothreonine Ref.18

Modified residue

168

1

Phosphoserine Ref.15 Ref.17

Modified residue

191

1

Phosphoserine; by PLK3 Ref.12

Modified residue

198

1

Phosphoserine; by PLK3 Ref.12

Modified residue

216

1

Phosphoserine; by CHEK1, CHEK2, BRSK1 and MAPK14 Ref.10 Ref.11 Ref.14

Modified residue

472

1

Phosphoserine Ref.17

Natural variations

Alternative sequence

66 – 123

58

GTPKR…MKCSP → SPGFFRTSGSAFSWD in isoform 4 and isoform 5.

VSP_000863

Alternative sequence

124 – 153

30

Missing in isoform 2 and isoform 5.

VSP_000864

Natural variant

14

1

S → N.
Corresponds to variant rs11567959 [ dbSNP | Ensembl ].

VAR_027922

Natural variant

70

1

R → C. Ref.1 Ref.5 Ref.6
Corresponds to variant rs3734166 [ dbSNP | Ensembl ].

VAR_027923

Natural variant

78

1

S → N.
Corresponds to variant rs11567962 [ dbSNP | Ensembl ].

VAR_027924

Natural variant

297

1

G → R.
Corresponds to variant rs11567997 [ dbSNP | Ensembl ].

VAR_020146

Experimental info

Mutagenesis

191

1

S → A: Facilitates nuclear exclusion. Ref.12

Mutagenesis

191

1

S → D: Mimicks phosphorylation state, leading to enhanced accumulation in the nucleus. Ref.12

Mutagenesis

352

1

E → K: Partial loss of HIV-1 Vpr binding. Ref.13

Mutagenesis

359

1

K → E: No effect on HIV-1 Vpr binding. Ref.13

Secondary structure

1

.

.

.

473

Helix Strand Turn

Details...

Beta strand

127 – 129

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CDC25C1) [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 0658A1F1B9B8996A	FASTA	473	53,365
	10 20 30 40 50 60 MSTELFSSTR EEGSSGSGPS FRSNQRKMLN LLLERDTSFT VCPDVPRTPV GKFLGDSANL 70 80 90 100 110 120 SILSGGTPKR CLDLSNLSSG EITATQLTTS ADLDETGHLD SSGLQEVHLA GMNHDQHLMK 130 140 150 160 170 180 CSPAQLLCST PNGLDRGHRK RDAMCSSSAN KENDNGNLVD SEMKYLGSPI TTVPKLDKNP 190 200 210 220 230 240 NLGEDQAEEI SDELMEFSLK DQEAKVSRSG LYRSPSMPEN LNRPRLKQVE KFKDNTIPDK 250 260 270 280 290 300 VKKKYFSGQG KLRKGLCLKK TVSLCDITIT QMLEEDSNQG HLIGDFSKVC ALPTVSGKHQ 310 320 330 340 350 360 DLKYVNPETV AALLSGKFQG LIEKFYVIDC RYPYEYLGGH IQGALNLYSQ EELFNFFLKK 370 380 390 400 410 420 PIVPLDTQKR IIIVFHCEFS SERGPRMCRC LREEDRSLNQ YPALYYPELY ILKGGYRDFF 430 440 450 460 470 PEYMELCEPQ SYCPMHHQDH KTELLRCRSQ SKVQEGERQL REQIALLVKD MSP
	Isoform 2 (CDC25C2) [UniParc]. Checksum: 11480DF49B3F04DD	FASTA	443	50,122
	10 20 30 40 50 60 MSTELFSSTR EEGSSGSGPS FRSNQRKMLN LLLERDTSFT VCPDVPRTPV GKFLGDSANL 70 80 90 100 110 120 SILSGGTPKR CLDLSNLSSG EITATQLTTS ADLDETGHLD SSGLQEVHLA GMNHDQHLMK 130 140 150 160 170 180 CSPDNGNLVD SEMKYLGSPI TTVPKLDKNP NLGEDQAEEI SDELMEFSLK DQEAKVSRSG 190 200 210 220 230 240 LYRSPSMPEN LNRPRLKQVE KFKDNTIPDK VKKKYFSGQG KLRKGLCLKK TVSLCDITIT 250 260 270 280 290 300 QMLEEDSNQG HLIGDFSKVC ALPTVSGKHQ DLKYVNPETV AALLSGKFQG LIEKFYVIDC 310 320 330 340 350 360 RYPYEYLGGH IQGALNLYSQ EELFNFFLKK PIVPLDTQKR IIIVFHCEFS SERGPRMCRC 370 380 390 400 410 420 LREEDRSLNQ YPALYYPELY ILKGGYRDFF PEYMELCEPQ SYCPMHHQDH KTELLRCRSQ 430 440 SKVQEGERQL REQIALLVKD MSP
	Isoform 3 (CDC25C3) (Sequence not available).		–	–
	Isoform 4 (CDC25C4) [UniParc]. Checksum: F2DDF9DB1653BCEE	FASTA	430	48,851
	10 20 30 40 50 60 MSTELFSSTR EEGSSGSGPS FRSNQRKMLN LLLERDTSFT VCPDVPRTPV GKFLGDSANL 70 80 90 100 110 120 SILSGSPGFF RTSGSAFSWD AQLLCSTPNG LDRGHRKRDA MCSSSANKEN DNGNLVDSEM 130 140 150 160 170 180 KYLGSPITTV PKLDKNPNLG EDQAEEISDE LMEFSLKDQE AKVSRSGLYR SPSMPENLNR 190 200 210 220 230 240 PRLKQVEKFK DNTIPDKVKK KYFSGQGKLR KGLCLKKTVS LCDITITQML EEDSNQGHLI 250 260 270 280 290 300 GDFSKVCALP TVSGKHQDLK YVNPETVAAL LSGKFQGLIE KFYVIDCRYP YEYLGGHIQG 310 320 330 340 350 360 ALNLYSQEEL FNFFLKKPIV PLDTQKRIII VFHCEFSSER GPRMCRCLRE EDRSLNQYPA 370 380 390 400 410 420 LYYPELYILK GGYRDFFPEY MELCEPQSYC PMHHQDHKTE LLRCRSQSKV QEGERQLREQ 430 IALLVKDMSP
	Isoform 5 (CDC25C5) (Cdc25Cdm) [UniParc]. Checksum: 212EA5FD75672289	FASTA	400	45,608
	10 20 30 40 50 60 MSTELFSSTR EEGSSGSGPS FRSNQRKMLN LLLERDTSFT VCPDVPRTPV GKFLGDSANL 70 80 90 100 110 120 SILSGSPGFF RTSGSAFSWD DNGNLVDSEM KYLGSPITTV PKLDKNPNLG EDQAEEISDE 130 140 150 160 170 180 LMEFSLKDQE AKVSRSGLYR SPSMPENLNR PRLKQVEKFK DNTIPDKVKK KYFSGQGKLR 190 200 210 220 230 240 KGLCLKKTVS LCDITITQML EEDSNQGHLI GDFSKVCALP TVSGKHQDLK YVNPETVAAL 250 260 270 280 290 300 LSGKFQGLIE KFYVIDCRYP YEYLGGHIQG ALNLYSQEEL FNFFLKKPIV PLDTQKRIII 310 320 330 340 350 360 VFHCEFSSER GPRMCRCLRE EDRSLNQYPA LYYPELYILK GGYRDFFPEY MELCEPQSYC 370 380 390 400 PMHHQDHKTE LLRCRSQSKV QEGERQLREQ IALLVKDMSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human homolog of fission yeast cdc25 mitotic inducer is predominantly expressed in G2." Sadhu K., Reed B.I., Richardson H., Russell P. Proc. Natl. Acad. Sci. U.S.A. 87:5139-5143(1990) [PubMed: 2195549] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CYS-70.
[2]	"An additional transcript of the cdc25C gene from A431 cells encodes a functional protein." Bureik M., Rief N., Drescher R., Jungbluth A., Montenarh M., Wagner P. Int. J. Oncol. 17:1251-1258(2000) [PubMed: 11078813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[3]	NIEHS SNPs program Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	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].
[5]	"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] (ISOFORM 1), VARIANT CYS-70. Tissue: Skin.
[6]	"Alternative splicing in the regulatory region of the human phosphatases CDC25A and CDC25C." Wegener S., Hampe W., Herrmann D., Schaller H.C. Eur. J. Cell Biol. 79:810-815(2000) [PubMed: 11139144] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-210 (ISOFORMS 2; 4 AND 5), VARIANT CYS-70.
[7]	"Differential expression of cdc25 cell-cycle-activating phosphatases in human colorectal carcinoma." Hernandez S., Bessa X., Bea S., Hernandez L., Nadal A., Mallofre C., Muntane J., Castells A., Fernandez P.L., Cardesa A., Campo E. Lab. Invest. 81:465-473(2001) [PubMed: 11304565] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). Tissue: Colon carcinoma.
[8]	"The physical association and phosphorylation of Cdc25C protein phosphatase by Prk." Ouyang B., Li W., Pan H., Meadows J., Hoffmann I., Dai W. Oncogene 18:6029-6036(1999) [PubMed: 10557092] [Abstract] Cited for: PHOSPHORYLATION BY PLK3.
[9]	"The human polo-like kinase, PLK, regulates cdc2/cyclin B through phosphorylation and activation of the cdc25C phosphatase." Roshak A.K., Capper E.A., Imburgia C., Fornwald J., Scott G., Marshall L.A. Cell. Signal. 12:405-411(2000) [PubMed: 11202906] [Abstract] Cited for: PHOSPHORYLATION BY PLK1.
[10]	"Initiation of a G2/M checkpoint after ultraviolet radiation requires p38 kinase." Bulavin D.V., Higashimoto Y., Popoff I.J., Gaarde W.A., Basrur V., Potapova O., Appella E., Fornace A.J. Jr. Nature 411:102-107(2001) [PubMed: 11333986] [Abstract] Cited for: PHOSPHORYLATION AT SER-216, INTERACTION WITH MAPK14 AND 14-3-3 PROTEINS.
[11]	"Human SAD1 kinase is involved in UV-induced DNA damage checkpoint function." Lu R., Niida H., Nakanishi M. J. Biol. Chem. 279:31164-31170(2004) [PubMed: 15150265] [Abstract] Cited for: PHOSPHORYLATION AT SER-216. Tissue: Testis.
[12]	"Cdc25C phosphorylation on serine 191 by Plk3 promotes its nuclear translocation." Bahassi el M., Hennigan R.F., Myer D.L., Stambrook P.J. Oncogene 23:2658-2663(2004) [PubMed: 14968113] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-191 AND SER-198, MUTAGENESIS OF SER-191.
[13]	"The human immunodeficiency virus Vpr protein binds Cdc25C: implications for G2 arrest." Goh W.C., Manel N., Emerman M. Virology 318:337-349(2004) [PubMed: 14972559] [Abstract] Cited for: INTERACTION WITH HIV-1 VPR, MUTAGENESIS OF GLU-352 AND LYS-359.
[14]	"MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates the G2/M transition and S phase progression in response to UV irradiation." Manke I.A., Nguyen A., Lim D., Stewart M.Q., Elia A.E., Yaffe M.B. Mol. Cell 17:37-48(2005) [PubMed: 15629715] [Abstract] Cited for: PHOSPHORYLATION AT SER-216 BY MAPKAPK2.
[15]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Human Plk4 phosphorylates Cdc25C." Bonni S., Ganuelas M.L., Petrinac S., Hudson J.W. Cell Cycle 7:545-547(2008) [PubMed: 18239451] [Abstract] Cited for: PHOSPHORYLATION BY PLK4.
[17]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-64; SER-168 AND SER-472, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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-38; THR-48; SER-57; SER-61; SER-64 AND THR-67, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M34065 mRNA. Translation: AAA35666.1.
AJ304504 mRNA. Translation: CAC19192.1.
AY497474 Genomic DNA. Translation: AAR32098.1.
CH471062 Genomic DNA. Translation: EAW62145.1.
CH471062 Genomic DNA. Translation: EAW62149.1.
BC019089 mRNA. Translation: AAH19089.1.
AF277723 mRNA. Translation: AAG41885.1.
AF277725 mRNA. Translation: AAG41887.1.
AF277726 mRNA. Translation: AAG41888.1.
AF312681 mRNA. Translation: AAL26835.1.

IPI

IPI00216684.
IPI00216685.
IPI00640320.
IPI01012097.

PIR

A38874. I59168.

RefSeq

NP_001781.2. NM_001790.3.
NP_073720.1. NM_022809.2.

UniGene

Hs.656.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BZI	X-ray	2.10	E	126-134	[»]
3OP3	X-ray	2.63	A	270-462	[»]

ProteinModelPortal

P30307.

SMR

P30307. Positions 280-448.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24183N.

IntAct

P30307. 5 interactions.

MINT

MINT-86355.

STRING

P30307.

PTM databases

PhosphoSite

P30307.

Polymorphism databases

DMDM

116242631.

Proteomic databases

PRIDE

P30307.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000323760; ENSP00000321656; ENSG00000158402.

GeneID

995.

KEGG

hsa:995.

UCSC

uc003lcp.1. human.
uc003lcq.1. human.

Organism-specific databases

CTD

995.

GeneCards

GC05M137648.

H-InvDB

HIX0005209.

HGNC

HGNC:1727. CDC25C.

HPA

CAB003800.

MIM

157680. gene.

neXtProt

NX_P30307.

PharmGKB

PA100.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15439.

GeneTree

ENSGT00390000018747.

HOVERGEN

HBG052501.

InParanoid

P30307.

OMA

ETGHLDS.

OrthoDB

EOG47D9G1.

PhylomeDB

P30307.

Enzyme and pathway databases

BRENDA

3.1.3.48. 2681.

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.

Gene expression databases

ArrayExpress

P30307.

Bgee

P30307.

CleanEx

HS_CDC25C.

Genevestigator

P30307.

GermOnline

ENSG00000158402. Homo sapiens.

Family and domain databases

InterPro

IPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like.
[Graphical view]

Gene3D

G3DSA:3.40.250.10. Rhodanese-like. 1 hit.

KO

K05867.

PANTHER

PTHR10828. MPI_Phosphatase. 1 hit.

Pfam

PF06617. M-inducer_phosp. 2 hits.
PF00581. Rhodanese. 1 hit.
[Graphical view]

PRINTS

PR00716. MPIPHPHTASE.

SMART

SM00450. RHOD. 1 hit.
[Graphical view]

SUPFAM

SSF52821. Rhodanese-like. 1 hit.

PROSITE

PS50206. RHODANESE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

4178.

SOURCE

Search...

Entry information

Entry name

MPIP3_HUMAN

Accession

Primary (citable) accession number: P30307
Secondary accession number(s): D3DQB8 , Q96PL3, Q9H168, Q9H2E8, Q9H2E9, Q9H2F1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 126 of the entry and version 2 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.