P23526 (SAHH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenosylhomocysteinase
Short name=AdoHcyase
EC=3.3.1.1

Alternative name(s):
S-adenosyl-L-homocysteine hydrolase

Gene names

Name:	AHCY
Synonyms:	SAHH

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	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine. Ref.15
Catalytic activity	S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.
Cofactor	Binds 1 NAD per subunit. Ref.14 Ref.15
Pathway	Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subunit structure	Homotetramer. Ref.14
Subcellular location	Cytoplasm. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.11
Involvement in disease	Defects in AHCY are the cause of hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD) [MIM:613752]. A metabolic disorder characterized by hypermethioninemia associated with failure to thrive, mental and motor retardation, facial dysmorphism with abnormal hair and teeth, and myocardiopathy. Ref.17 Ref.18 Ref.19 Ref.20
Sequence similarities	Belongs to the adenosylhomocysteinase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	NAD
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	methylation Traceable author statement. Source: Reactome xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	adenosylhomocysteinase activity Traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7 Ref.8

Chain

2 – 432

431

Adenosylhomocysteinase

PRO_0000116902

Regions

Nucleotide binding

157 – 159

3

NAD

Nucleotide binding

222 – 227

6

NAD

Nucleotide binding

299 – 301

3

NAD

Sites

Binding site

57

1

Substrate By similarity

Binding site

131

1

Substrate By similarity

Binding site

156

1

Substrate By similarity

Binding site

186

1

Substrate By similarity

Binding site

190

1

Substrate By similarity

Binding site

243

1

NAD

Binding site

248

1

NAD

Binding site

346

1

NAD

Binding site

353

1

NAD

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.8

Modified residue

408

1

N6-acetyllysine Ref.12

Natural variations

Natural variant

38

1

R → W. Ref.16
Corresponds to variant rs13043752 [ dbSNP | Ensembl ].

VAR_052286

Natural variant

49

1

R → C in HMAHCHD. Ref.19 Ref.20

VAR_058588

Natural variant

86

1

D → G in HMAHCHD. Ref.19 Ref.20

VAR_058589

Natural variant

86

1

D → N. Ref.1

VAR_006934

Natural variant

89

1

A → V in HMAHCHD. Ref.18

VAR_058590

Natural variant

143

1

Y → C in HMAHCHD. Ref.17 Ref.18

VAR_058591

Secondary structure

1

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432

Helix Strand Turn

Details...

Beta strand

8 – 10

3

Helix

12 – 14

3

Helix

15 – 26

12

Helix

30 – 39

10

Turn

40 – 42

3

Turn

44 – 47

4

Beta strand

49 – 54

6

Helix

58 – 69

12

Beta strand

73 – 77

5

Helix

86 – 94

9

Beta strand

99 – 101

3

Helix

107 – 115

9

Beta strand

118 – 120

3

Beta strand

126 – 133

8

Helix

134 – 142

9

Helix

144 – 149

6

Beta strand

152 – 155

4

Helix

158 – 169

12

Beta strand

175 – 179

5

Helix

184 – 187

4

Helix

190 – 207

18

Beta strand

215 – 219

5

Helix

223 – 234

12

Beta strand

238 – 242

5

Helix

246 – 254

9

Helix

262 – 265

4

Turn

266 – 268

3

Beta strand

270 – 274

5

Helix

284 – 287

4

Beta strand

294 – 298

5

Beta strand

300 – 302

3

Helix

308 – 314

7

Beta strand

316 – 322

7

Beta strand

325 – 329

5

Beta strand

335 – 339

5

Helix

340 – 342

3

Helix

345 – 348

4

Helix

355 – 374

20

Helix

376 – 378

3

Beta strand

381 – 384

4

Helix

388 – 399

12

Turn

400 – 403

4

Helix

411 – 417

7

Sequences

	Sequence		Length	Mass (Da)
	P23526 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 2833C025F969553E	FASTA	432	47,716
	10 20 30 40 50 60 MSDKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMRERYS ASKPLKGARI AGCLHMTVET 70 80 90 100 110 120 AVLIETLVTL GAEVQWSSCN IFSTQDHAAA AIAKAGIPVY AWKGETDEEY LWCIEQTLYF 130 140 150 160 170 180 KDGPLNMILD DGGDLTNLIH TKYPQLLPGI RGISEETTTG VHNLYKMMAN GILKVPAINV 190 200 210 220 230 240 NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI 250 260 270 280 290 300 ITEIDPINAL QAAMEGYEVT TMDEACQEGN IFVTTTGCID IILGRHFEQM KDDAIVCNIG 310 320 330 340 350 360 HFDVEIDVKW LNENAVEKVN IKPQVDRYRL KNGRRIILLA EGRLVNLGCA MGHPSFVMSN 370 380 390 400 410 420 SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG KLNVKLTKLT EKQAQYLGMS 430 CDGPFKPDHY RY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of full length cDNA for human S-adenosylhomocysteine hydrolase." Coulter-Karis D.E., Hershfield M.S. Ann. Hum. Genet. 53:169-175(1989) [PubMed: 2596825] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-86. Tissue: Placenta.
[2]	"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: Umbilical cord blood.
[4]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[6]	"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: Placenta and Skin.
[7]	"Limited proteolysis of S-adenosylhomocysteine hydrolase: implications for the three-dimensional structure." Gupta R.A., Yuan C.-S., Ault-Riche D.B., Borchardt R.T. Arch. Biochem. Biophys. 319:365-371(1995) [PubMed: 7786017] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-6; 104-108 AND 198-202.
[8]	Bienvenut W.V., Heiserich L., Gottlieb E. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-34; 95-103; 143-186; 215-226; 336-343 AND 389-405, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[9]	"Isozyme and DNA analysis of human S-adenosyl-L-homocysteine hydrolase (AHCY)." Arredondo-Vega F.X., Charlton J.A., Edwards Y.H., Hopkinson D.A., Whitehouse D.B. Ann. Hum. Genet. 53:157-167(1989) [PubMed: 2574561] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-432. Tissue: Placenta.
[10]	"Photoaffinity labeling of human placental S-adenosylhomocysteine hydrolase with [2-3H]8-azido-adenosine." Yuan C.S., Borchardt R.T. J. Biol. Chem. 270:16140-16146(1995) [PubMed: 7608178] [Abstract] Cited for: PROTEIN SEQUENCE OF 175-186 AND 319-327.
[11]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-408, MASS SPECTROMETRY.
[13]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength." Turner M.A., Yuan C.S., Borchardt R.T., Hershfield M.S., Smith G.D., Howell P.L. Nat. Struct. Biol. 5:369-376(1998) [PubMed: 9586999] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD AND ADENOSINE ANALOG, SUBUNIT, COFACTOR. Tissue: Placenta.
[15]	"Catalytic strategy of S-adenosyl-L-homocysteine hydrolase: transition-state stabilization and the avoidance of abortive reactions." Yang X., Hu Y., Yin D.H., Turner M.A., Wang M., Borchardt R.T., Howell P.L., Kuczera K., Schowen R.L. Biochemistry 42:1900-1909(2003) [PubMed: 12590576] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH NAD AND NEPLANOCIN A, FUNCTION, COFACTOR.
[16]	"Effect of genetic variation in the human S-adenosylhomocysteine hydrolase gene on total homocysteine concentrations and risk of recurrent venous thrombosis." Gellekink H., den Heijer M., Kluijtmans L.A., Blom H.J. Eur. J. Hum. Genet. 12:942-948(2004) [PubMed: 15241484] [Abstract] Cited for: VARIANT TRP-38.
[17]	"S-adenosylhomocysteine hydrolase deficiency in a human: a genetic disorder of methionine metabolism." Baric I., Fumic K., Glenn B., Cuk M., Schulze A., Finkelstein J.D., James S.J., Mejaski-Bosnjak V., Pazanin L., Pogribny I.P., Rados M., Sarnavka V., Scukanec-Spoljar M., Allen R.H., Stabler S., Uzelac L., Vugrek O., Wagner C., Zeisel S., Mudd S.H. Proc. Natl. Acad. Sci. U.S.A. 101:4234-4239(2004) [PubMed: 15024124] [Abstract] Cited for: VARIANT HMAHCHD CYS-143.
[18]	"S-adenosylhomocysteine hydrolase deficiency in a 26-year-old man." Buist N.R., Glenn B., Vugrek O., Wagner C., Stabler S., Allen R.H., Pogribny I., Schulze A., Zeisel S.H., Baric I., Mudd S.H. J. Inherit. Metab. Dis. 29:538-545(2006) [PubMed: 16736098] [Abstract] Cited for: VARIANTS HMAHCHD VAL-89 AND CYS-143.
[19]	"S-adenosylhomocysteine hydrolase (AHCY) deficiency: two novel mutations with lethal outcome." Vugrek O., Beluzic R., Nakic N., Mudd S.H. Hum. Mutat. 30:E555-E565(2009) [PubMed: 19177456] [Abstract] Cited for: VARIANTS HMAHCHD CYS-49 AND GLY-86.
[20]	"S-adenosylhomocysteine hydrolase deficiency: two siblings with fetal hydrops and fatal outcomes." Grubbs R., Vugrek O., Deisch J., Wagner C., Stabler S., Allen R., Baric I., Rados M., Mudd S.H. J. Inherit. Metab. Dis. 33:705-713(2010) [PubMed: 20852937] [Abstract] Cited for: VARIANTS HMAHCHD CYS-49 AND GLY-86.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M61831 mRNA. Translation: AAA51681.1.
M61832 mRNA. Translation: AAA51682.1.
BT006697 mRNA. Translation: AAP35343.1.
AK290422 mRNA. Translation: BAF83111.1.
AL356299 Genomic DNA. Translation: CAC09528.1.
CH471077 Genomic DNA. Translation: EAW76279.1.
CH471077 Genomic DNA. Translation: EAW76280.1.
BC010018 mRNA. Translation: AAH10018.1.
BC011606 mRNA. Translation: AAH11606.1.

IPI

IPI00012007.

PIR

A43629.

RefSeq

NP_000678.1. NM_000687.2.
NP_001155238.1. NM_001161766.1.

UniGene

Hs.388004.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A7A	X-ray	2.80	A/B	1-432	[»]
1LI4	X-ray	2.01	A	1-432	[»]
3NJ4	X-ray	2.50	A/B/C/D	1-432	[»]

ProteinModelPortal

P23526.

SMR

P23526. Positions 3-432.

ModBase

Search...

Protein-protein interaction databases

IntAct

P23526. 8 interactions.

MINT

MINT-5000523.

STRING

P23526.

PTM databases

PhosphoSite

P23526.

Polymorphism databases

DMDM

20141702.

2D gel databases

REPRODUCTION-2DPAGE

IPI00012007.

Proteomic databases

PeptideAtlas

P23526.

PRIDE

P23526.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000217426; ENSP00000217426; ENSG00000101444.

GeneID

191.

KEGG

hsa:191.

UCSC

uc002xai.1. human.

Organism-specific databases

CTD

191.

GeneCards

GC20M032868.

H-InvDB

HIX0015744.

HGNC

HGNC:343. AHCY.

MIM

180960. gene.
613752. phenotype.

neXtProt

NX_P23526.

Orphanet

88618. Psychomotor retardation due to S-adenosylhomocysteine hydrolase deficiency.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13777.

HOGENOM

HBG352029.

HOVERGEN

HBG005041.

InParanoid

P23526.

OMA

ELFTKTE.

OrthoDB

EOG4MW862.

PhylomeDB

P23526.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P23526.

Bgee

P23526.

CleanEx

HS_AHCY.

Genevestigator

P23526.

GermOnline

ENSG00000101444. Homo sapiens.

Family and domain databases

InterPro

IPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]

KO

K01251.

PANTHER

PTHR23420. Ad_hcy_hydrolase. 1 hit.

Pfam

PF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]

PIRSF

PIRSF001109. Ad_hcy_hydrolase. 1 hit.

SMART

SM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00936. AhcY. 1 hit.

PROSITE

PS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

780.

SOURCE

Search...

Entry information

Entry name

SAHH_HUMAN

Accession

Primary (citable) accession number: P23526
Secondary accession number(s): A8K307, E1P5P2, Q96A36

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 132 of the entry and version 4 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.