Reviewed, UniProtKB/Swiss-Prot P10632 (CP2C8_HUMAN)

Names and origin

Protein names

Recommended name:
    Cytochrome P450 2C8
    EC=1.14.14.1
Alternative name(s):
    CYPIIC8
    P450 form 1
    P450 MP-12/MP-20
    P450 IIC2
    S-mephenytoin 4-hydroxylase

Gene names

Name:

CYP2C8

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

General annotation (Comments)

Function	Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. In the epoxidation of arachidonic acid it generates only 14,15- and 11,12-cis-epoxyeicosatrienoic acids. It is the principal enzyme responsible for the metabolism the anti-cancer drug paclitaxel (taxol). Ref.10
Catalytic activity	RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O. Ref.10
Cofactor	Heme group.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Induction	By phenobarbital.
Sequence similarities	Belongs to the cytochrome P450 family.
Caution	Alternative splicing has been shown to occur but the shorter forms are believed to be non-functional.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Non-traceable author statement. Source: UniProtKB
Cellular component	endoplasmic reticulum membrane Inferred from Experiment. Source: Reactome extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Non-traceable author statement. Source: UniProtKB
Molecular function	aromatase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro oxygen binding Inferred from Experiment. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 490

490

Cytochrome P450 2C8

PRO_0000051699

Sites

Metal binding

435

1

Iron (heme axial ligand)

Natural variations

Natural variant

139

1

R → K in allele CYP2C8*3. dbSNP rs11572080. Ref.5 Ref.12 Ref.15 Ref.16 Ref.17

VAR_012238

Natural variant

154

1

E → D in clone MP-12. Ref.11

VAR_001250

Natural variant

193

1

N → K in MP-20. Ref.11

VAR_001251

Natural variant

244

1

I → V: dbSNP rs11572102. Ref.5

VAR_018958

Natural variant

249

1

K → R in clone MP-12. Ref.11

VAR_001252

Natural variant

264

1

I → M in allele CYP2C8*4. dbSNP rs1058930. Ref.5 Ref.16 Ref.17 Ref.3

VAR_011754

Natural variant

269

1

I → F in allele CYP2C8*2; only found in African-Americans. dbSNP rs11572103. Ref.5 Ref.15 Ref.16 Ref.17

VAR_012239

Natural variant

390

1

L → S

VAR_016947

Natural variant

399

1

K → R in allele CYP2C8*3. dbSNP rs10509681. Ref.5 Ref.15 Ref.16 Ref.17 Ref.4 Ref.13

VAR_012240

Natural variant

411

1

H → L in clone MP-20. Ref.10 Ref.11

VAR_001253

Experimental info

Sequence conflict

54

1

F → L Ref.12

Sequence conflict

67

1

V → L Ref.12

Sequence conflict

76

1

V → C Ref.12

Sequence conflict

82

1

A → S in AAH20596. Ref.8

Sequence conflict

130

1

T → N in AAA35739. Ref.1

Sequence conflict

130

1

T → N in AAA35740. Ref.1

Sequence conflict

130

1

T → N Ref.3

Sequence conflict

209

1

N → S Ref.12

Sequence conflict

386

1

T → A in BAF85442. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

490

Helix Strand Turn

Details...

Turn

37 – 39

3

Helix

42 – 44

3

Helix

50 – 61

12

Beta strand

63 – 69

7

Beta strand

72 – 77

6

Helix

80 – 87

8

Turn

88 – 94

7

Helix

101 – 107

7

Turn

111 – 113

3

Helix

117 – 130

14

Turn

133 – 136

4

Beta strand

137 – 139

3

Helix

141 – 157

17

Turn

158 – 161

4

Helix

167 – 182

16

Beta strand

183 – 185

3

Helix

192 – 208

17

Helix

212 – 218

7

Helix

220 – 225

6

Helix

227 – 252

26

Helix

263 – 273

11

Helix

284 – 298

15

Helix

300 – 315

16

Helix

317 – 330

14

Beta strand

333 – 335

3

Helix

339 – 344

6

Helix

346 – 359

14

Beta strand

374 – 376

3

Beta strand

379 – 381

3

Beta strand

386 – 389

4

Helix

391 – 395

5

Turn

398 – 400

3

Beta strand

401 – 403

3

Helix

409 – 412

4

Helix

431 – 433

3

Helix

438 – 455

18

Beta strand

456 – 459

4

Helix

464 – 466

3

Beta strand

472 – 479

8

Beta strand

485 – 489

5

Sequences

	Sequence		Length	Mass (Da)
	P10632-1 [UniParc]. Last modified November 1, 1990. Version 2. Checksum: E920EB2084F477E1	FASTA	490	55,825
	10 20 30 40 50 60 MEPFVVLVLC LSFMLLFSLW RQSCRRRKLP PGPTPLPIIG NMLQIDVKDI CKSFTNFSKV 70 80 90 100 110 120 YGPVFTVYFG MNPIVVFHGY EAVKEALIDN GEEFSGRGNS PISQRITKGL GIISSNGKRW 130 140 150 160 170 180 KEIRRFSLTT LRNFGMGKRS IEDRVQEEAH CLVEELRKTK ASPCDPTFIL GCAPCNVICS 190 200 210 220 230 240 VVFQKRFDYK DQNFLTLMKR FNENFRILNS PWIQVCNNFP LLIDCFPGTH NKVLKNVALT 250 260 270 280 290 300 RSYIREKVKE HQASLDVNNP RDFIDCFLIK MEQEKDNQKS EFNIENLVGT VADLFVAGTE 310 320 330 340 350 360 TTSTTLRYGL LLLLKHPEVT AKVQEEIDHV IGRHRSPCMQ DRSHMPYTDA VVHEIQRYSD 370 380 390 400 410 420 LVPTGVPHAV TTDTKFRNYL IPKGTTIMAL LTSVLHDDKE FPNPNIFDPG HFLDKNGNFK 430 440 450 460 470 480 KSDYFMPFSA GKRICAGEGL ARMELFLFLT TILQNFNLKS VDDLKNLNTT AVTKGIVSLP 490 PSYQICFIPV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of multiple human cytochrome P-450 1 cDNAs. The chromosomal localization of the gene and evidence for alternate RNA splicing." Okino S.T., Quattrochi L.C., Pendurthi U.R., McBride O.W., Tukey R.H. J. Biol. Chem. 262:16072-16079(1987) [PubMed: 3500169] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"cDNA and amino acid sequences of two members of the human P450IIC gene subfamily." Kimura S., Pastewka J., Gelboin H.V., Gonzalez F.J. Nucleic Acids Res. 15:10053-10054(1987) [PubMed: 3697070] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily." Romkes M., Faletto M.B., Blaisdell J.A., Raucy J.L., Goldstein J.A. Biochemistry 30:3247-3255(1991) [PubMed: 2009263] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-264.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-399. Tissue: Liver.
[5]	NIEHS SNPs program Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-139; VAL-244; MET-264; PHE-269 AND ARG-399.
[6]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[9]	"Isolation of the human cytochrome P-450 IIC8 gene: multiple glucocorticoid responsive elements in the 5' region." Ged C., Beaune P. Biochim. Biophys. Acta 1088:433-435(1991) [PubMed: 1707679] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56. Tissue: Blood.
[10]	"Molecular cloning, expression and characterization of an endogenous human cytochrome P450 arachidonic acid epoxygenase isoform." Zeldin D.C., DuBois R.N., Falck J.R., Capdevila J.H. Arch. Biochem. Biophys. 322:76-86(1995) [PubMed: 7574697] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-15, NUCLEOTIDE SEQUENCE [MRNA] OF 6-490, FUNCTION, CATALYTIC ACTIVITY, VARIANT LEU-411. Tissue: Kidney.
[11]	"Characterization of cDNAs, mRNAs, and proteins related to human liver microsomal cytochrome P-450 (S)-mephenytoin 4'-hydroxylase." Ged C., Umbenhauer D.R., Bellew T.M., Bork R.W., Srivastava P.K., Shinriki N., Lloyd R.S., Guengerich F.P. Biochemistry 27:6929-6940(1988) [PubMed: 3196692] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-490, VARIANTS ASP-154; LYS-193; ARG-249 AND LEU-411. Tissue: Liver.
[12]	"Cloning, expression and chromosomal localization of a member of the human cytochrome P450IIC gene sub-family." Shephard E.A., Phillips I.R., Santisteban I., Palmer C.N., Povey S. Ann. Hum. Genet. 53:23-31(1989) [PubMed: 2729895] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 34-382, VARIANT LYS-139.
[13]	"Sequence of a human liver cytochrome P-450 cDNA clone." Kolyada A.Y. Nucleic Acids Res. 18:5550-5550(1990) [PubMed: 2216732] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 281-490, VARIANT ARG-399.
[14]	"Structure of human microsomal cytochrome P450 2C8. Evidence for a peripheral fatty acid binding site." Schoch G.A., Yano J.K., Wester M.R., Griffin K.J., Stout C.D., Johnson E.F. J. Biol. Chem. 279:9497-9503(2004) [PubMed: 14676196] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 28-490.
[15]	"Polymorphisms in human CYP2C8 decrease metabolism of the anticancer drug paclitaxel and arachidonic acid." Dai D., Zeldin D.C., Blaisdell J.A., Chanas B., Coulter S.J., Ghanayem B.I., Goldstein J.A. Pharmacogenetics 11:597-607(2001) [PubMed: 11668219] [Abstract] Cited for: VARIANTS LYS-139; PHE-269 AND ARG-399.
[16]	"CYP2C8 polymorphisms in Caucasians and their relationship with paclitaxel 6alpha-hydroxylase activity in human liver microsomes." Bahadur N., Leathart J.B., Mutch E., Steimel-Crespi D., Dunn S.A., Gilissen R., Houdt J.V., Hendrickx J., Mannens G., Bohets H., Williams F.M., Armstrong M., Crespi C.L., Daly A.K. Biochem. Pharmacol. 64:1579-1589(2002) [PubMed: 12429347] [Abstract] Cited for: VARIANTS LYS-139; MET-264; PHE-269; SER-390 AND ARG-399.
[17]	"Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population." Solus J.F., Arietta B.J., Harris J.R., Sexton D.P., Steward J.Q., McMunn C., Ihrie P., Mehall J.M., Edwards T.L., Dawson E.P. Pharmacogenomics 5:895-931(2004) [PubMed: 15469410] [Abstract] Cited for: VARIANTS LYS-139; MET-264; PHE-269 AND ARG-399.
+	Additional computationally mapped references.

Web resources

Cytochrome P450 Allele Nomenclature Committee

CYP2C8 alleles

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

M17397 mRNA. Translation: AAA35739.1.
M17398 mRNA. Translation: AAA35740.1. Sequence problems.
Y00498 mRNA. Translation: CAA68550.1.
AK292753 mRNA. Translation: BAF85442.1.
AK315823 mRNA. Translation: BAF98714.1.
AY514490 Genomic DNA. Translation: AAR89907.1.
AL359672 Genomic DNA. Translation: CAH71307.1.
CH471066 Genomic DNA. Translation: EAW50018.1.
BC020596 mRNA. Translation: AAH20596.1.
X54807 Genomic DNA. Translation: CAA38578.1.
M21941 mRNA. Translation: AAA52160.1.
M21942 mRNA. Translation: AAA52161.1. Different initiation.
X51535 mRNA. Translation: CAA35915.1.

IPI

IPI00290301.

PIR

A29782.

RefSeq

NP_000761.3.

UniGene

Hs.282871
Hs.709188

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PQ2	X-ray	2.70	A/B	28-490	[»]
2NNH	X-ray	2.60	A/B	28-490	[»]
2NNI	X-ray	2.80	A	28-490	[»]
2NNJ	X-ray	2.28	A	28-490	[»]
2VN0	X-ray	2.70	A	28-490	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P10632.

PTM databases

PhosphoSite

P10632.

Proteomic databases

PRIDE

P10632.

Genome annotation databases

Ensembl

ENST00000371270; ENSP00000360317; ENSG00000138115; Homo sapiens. [Genome view]

GeneID

1558.

KEGG

hsa:1558.

UCSC

uc001kkb.1. human.

Organism-specific databases

CTD

1558.

GeneCards

GC10M096786.

H-InvDB

HIX0009058.

HGNC

HGNC:2622. CYP2C8.

HPA

HPA013547.
HPA013970.
HPA015066.

MIM

601129. gene.

PharmGKB

PA125.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P10632.

HOVERGEN

P10632.

OMA

PISQRIT

OrthoDB

EOG9TTK37

Enzyme and pathway databases

BRENDA

1.14.14.1. 247.

Reactome

REACT_13433. Biological oxidations.

Gene expression databases

ArrayExpress

P10632.

Bgee

P10632.

CleanEx

HS_CYP2C8.

Genevestigator

P10632.

GermOnline

ENSG00000138115. Homo sapiens.

Family and domain databases

InterPro

IPR001128. Cyt_P450.
IPR017973. Cyt_P450_C.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]

Gene3D

G3DSA:1.10.630.10. Cyt_P450. 1 hit.

PANTHER

PTHR19383. Cyt_P450. 1 hit.

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00463. EP450I.
PR00385. P450.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB01424. Aminophenazone.
DB01118. Amiodarone.
DB00613. Amodiaquine.
DB00865. Benzphetamine.
DB00564. Carbamazepine.
DB00439. Cerivastatin.
DB00586. Diclofenac.
DB01095. Fluvastatin.
DB01320. Fosphenytoin.
DB01241. Gemfibrozil.
DB01026. Ketoconazole.
DB01259. Lapatinib.
DB00227. Lovastatin.
DB00683. Midazolam.
DB00471. Montelukast.
DB00622. Nicardipine.
DB01229. Paclitaxel.
DB00252. Phenytoin.
DB01132. Pioglitazone.
DB00912. Repaglinide.
DB01045. Rifampin.
DB00412. Rosiglitazone.
DB00641. Simvastatin.
DB01261. Sitagliptin.
DB01124. Tolbutamide.
DB00214. Torasemide.
DB00755. Tretinoin.
DB00440. Trimethoprim.
DB00682. Warfarin.
DB00549. Zafirlukast.
DB01198. Zopiclone.

NextBio

6434.

SOURCE

Search...

Entry information

Entry name

CP2C8_HUMAN

Accession

Primary (citable) accession number: P10632
Secondary accession number(s): A8K9N8 , B0AZN2, Q5VX93, Q8WWB1, Q9UCZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1990
Last modified:	November 24, 2009
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.