Reviewed, UniProtKB/Swiss-Prot P09960 (LKHA4_HUMAN)

Names and origin

Protein names

Recommended name:
    Leukotriene A-4 hydrolase
    EC=3.3.2.6
Alternative name(s):
    Leukotriene A(4) hydrolase
      Short name=LTA-4 hydrolase

Gene names

Name:	LTA4H
Synonyms:	LTA4

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	611 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	Hydrolyzes an epoxide moiety of leukotriene A4 (LTA-4) to form leukotriene B4 (LTB-4). The enzyme also has some peptidase activity. Ref.7 Ref.10 Ref.11
Catalytic activity	(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate. Ref.7
Cofactor	Binds 1 zinc ion per subunit.
Pathway	Lipid metabolism; leukotriene B4 biosynthesis.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the peptidase M1 family.

Ontologies

Keywords
Biological process	Leukotriene biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	inflammatory response Ref.17 Non-traceable author statement. Source: ProtInc leukotriene biosynthetic process Ref.12 Traceable author statement. Source: ProtInc proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay. Source: HPA
Molecular function	epoxide hydrolase activity Traceable author statement. Source: UniProtKB leukotriene-A4 hydrolase activity Ref.12 Traceable author statement. Source: ProtInc metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Ref.12 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GH1	P01241	1	EBI-721089,EBI-1026046
MCC	P23508	1	EBI-721089,EBI-307531

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P09960-1)

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: P09960-2)

The sequence of this isoform differs from the canonical sequence as follows:
     538-611: Missing.

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 – 611

610

Leukotriene A-4 hydrolase

PRO_0000095124

Sites

Active site

297

1

Active site

384

1

Proton donor Potential

Metal binding

296

1

Zinc; catalytic

Metal binding

300

1

Zinc; catalytic

Metal binding

319

1

Zinc; catalytic

Binding site

200

1

Substrate Potential

Amino acid modifications

Modified residue

73

1

N6-acetyllysine Ref.16

Modified residue

337

1

N6-acetyllysine Ref.16

Modified residue

414

1

N6-acetyllysine Ref.16

Modified residue

573

1

N6-acetyllysine Ref.16

Natural variations

Alternative sequence

538 – 611

74

Missing in isoform 2.

VSP_012553

Natural variant

131

1

Y → H: dbSNP rs45630737.

VAR_051570

Experimental info

Mutagenesis

137

1

Q → A: No loss of activity. Ref.12 Ref.18

Mutagenesis

137

1

Q → L: Aminopeptidase activity strongly impaired, but keeps LTA4 activity. Ref.12 Ref.18

Mutagenesis

137

1

Q → N: Aminopeptidase activity almost absent, but keeps LTA4 activity. Ref.12 Ref.18

Mutagenesis

269

1

G → A: No loss of activity. Ref.12

Mutagenesis

270

1

G → A: No loss of activity. Ref.12 Ref.18

Mutagenesis

271

1

M → L: No loss of activity. Ref.12 Ref.18

Mutagenesis

272

1

E → A or D: Complete loss of activity. Ref.12 Ref.18

Mutagenesis

272

1

E → Q: Loss of LTA4 activity, and aminopeptidase activity strongly impaired. Ref.12 Ref.18

Mutagenesis

273

1

N → A: No loss of activity. Ref.12 Ref.18

Mutagenesis

296

1

H → Y: Complete loss of activity. Ref.12

Mutagenesis

297

1

E → A: Loss of both activities. Ref.12 Ref.13 Ref.14

Mutagenesis

297

1

E → K: Loss of both activities. Ref.12 Ref.13 Ref.14

Mutagenesis

297

1

E → Q: Loss of aminopeptidase activity, but keeps LTA4 activity. Ref.12 Ref.13 Ref.14

Mutagenesis

300

1

H → L: Complete loss of activity. Ref.12

Mutagenesis

319

1

E → A: Complete loss of activity. Ref.12

Secondary structure

1

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611

Helix Strand Turn

Details...

Turn

14 – 16

3

Beta strand

17 – 29

13

Turn

30 – 33

4

Beta strand

34 – 45

12

Beta strand

50 – 67

18

Beta strand

74 – 76

3

Helix

81 – 83

3

Beta strand

85 – 95

11

Beta strand

100 – 109

10

Beta strand

116 – 119

4

Helix

121 – 123

3

Beta strand

124 – 129

6

Beta strand

131 – 134

4

Turn

137 – 140

4

Helix

141 – 143

3

Beta strand

154 – 164

11

Beta strand

167 – 180

14

Beta strand

187 – 199

13

Helix

200 – 202

3

Beta strand

205 – 209

5

Beta strand

211 – 216

6

Beta strand

219 – 223

5

Helix

225 – 227

3

Helix

228 – 234

7

Turn

235 – 237

3

Helix

238 – 249

12

Beta strand

258 – 261

4

Beta strand

267 – 271

5

Beta strand

276 – 279

4

Helix

281 – 283

3

Beta strand

286 – 288

3

Turn

289 – 291

3

Helix

292 – 299

8

Turn

300 – 302

3

Turn

304 – 306

3

Beta strand

307 – 311

5

Helix

312 – 314

3

Helix

315 – 334

20

Helix

336 – 357

22

Helix

362 – 364

3

Beta strand

365 – 367

3

Helix

375 – 378

4

Helix

382 – 398

17

Helix

401 – 415

15

Beta strand

418 – 420

3

Helix

422 – 432

11

Helix

434 – 436

3

Helix

437 – 440

4

Helix

445 – 450

6

Turn

464 – 466

3

Helix

467 – 478

12

Helix

481 – 486

6

Helix

489 – 492

4

Helix

497 – 508

12

Helix

515 – 525

11

Helix

527 – 529

3

Helix

533 – 545

13

Helix

551 – 561

11

Helix

565 – 577

13

Helix

579 – 592

14

Helix

593 – 595

3

Helix

598 – 607

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 329BF6D04D4A06E1	FASTA	611	69,285
	10 20 30 40 50 60 MPEIVDTCSL ASPASVCRTK HLHLRCSVDF TRRTLTGTAA LTVQSQEDNL RSLVLDTKDL 70 80 90 100 110 120 TIEKVVINGQ EVKYALGERQ SYKGSPMEIS LPIALSKNQE IVIEISFETS PKSSALQWLT 130 140 150 160 170 180 PEQTSGKEHP YLFSQCQAIH CRAILPCQDT PSVKLTYTAE VSVPKELVAL MSAIRDGETP 190 200 210 220 230 240 DPEDPSRKIY KFIQKVPIPC YLIALVVGAL ESRQIGPRTL VWSEKEQVEK SAYEFSETES 250 260 270 280 290 300 MLKIAEDLGG PYVWGQYDLL VLPPSFPYGG MENPCLTFVT PTLLAGDKSL SNVIAHEISH 310 320 330 340 350 360 SWTGNLVTNK TWDHFWLNEG HTVYLERHIC GRLFGEKFRH FNALGGWGEL QNSVKTFGET 370 380 390 400 410 420 HPFTKLVVDL TDIDPDVAYS SVPYEKGFAL LFYLEQLLGG PEIFLGFLKA YVEKFSYKSI 430 440 450 460 470 480 TTDDWKDFLY SYFKDKVDVL NQVDWNAWLY SPGLPPIKPN YDMTLTNACI ALSQRWITAK 490 500 510 520 530 540 EDDLNSFNAT DLKDLSSHQL NEFLAQTLQR APLPLGHIKR MQEVYNFNAI NNSEIRFRWL 550 560 570 580 590 600 RLCIQSKWED AIPLALKMAT EQGRMKFTRP LFKDLAAFDK SHDQAVRTYQ EHKASMHPVT 610 AMLVGKDLKV D
	Isoform 2. Checksum: 8C267CB30BA1E5FF	FASTA	537	60,704
	10 20 30 40 50 60 MPEIVDTCSL ASPASVCRTK HLHLRCSVDF TRRTLTGTAA LTVQSQEDNL RSLVLDTKDL 70 80 90 100 110 120 TIEKVVINGQ EVKYALGERQ SYKGSPMEIS LPIALSKNQE IVIEISFETS PKSSALQWLT 130 140 150 160 170 180 PEQTSGKEHP YLFSQCQAIH CRAILPCQDT PSVKLTYTAE VSVPKELVAL MSAIRDGETP 190 200 210 220 230 240 DPEDPSRKIY KFIQKVPIPC YLIALVVGAL ESRQIGPRTL VWSEKEQVEK SAYEFSETES 250 260 270 280 290 300 MLKIAEDLGG PYVWGQYDLL VLPPSFPYGG MENPCLTFVT PTLLAGDKSL SNVIAHEISH 310 320 330 340 350 360 SWTGNLVTNK TWDHFWLNEG HTVYLERHIC GRLFGEKFRH FNALGGWGEL QNSVKTFGET 370 380 390 400 410 420 HPFTKLVVDL TDIDPDVAYS SVPYEKGFAL LFYLEQLLGG PEIFLGFLKA YVEKFSYKSI 430 440 450 460 470 480 TTDDWKDFLY SYFKDKVDVL NQVDWNAWLY SPGLPPIKPN YDMTLTNACI ALSQRWITAK 490 500 510 520 530 EDDLNSFNAT DLKDLSSHQL NEFLAQTLQR APLPLGHIKR MQEVYNFNAI NNSEIRF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a cDNA coding for human leukotriene A4 hydrolase. Complete primary structure of an enzyme involved in eicosanoid synthesis." Minami M., Ohno S., Kawasaki H., Raedmark O., Samuelsson B., Joernvall H., Shimizu T., Seyama Y., Suzuki K. J. Biol. Chem. 262:13873-13876(1987) [PubMed: 3654641] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Molecular cloning and amino acid sequence of leukotriene A4 hydrolase." Funk C.D., Raadmark O., Fu J.Y., Matsumoto T., Joernvall H., Shimizu T., Samuelsson B. Proc. Natl. Acad. Sci. U.S.A. 84:6677-6681(1987) [PubMed: 2821541] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[3]	"Cloning and characterization of the human leukotriene A4 hydrolase gene." Mancini J.A., Evans J.F. Eur. J. Biochem. 231:65-71(1995) [PubMed: 7628486] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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 (JUL-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] (ISOFORM 1). Tissue: Eye.
[7]	"Leukotriene A4 hydrolase in the human B-lymphocytic cell line Raji: indications of catalytically divergent forms of the enzyme." Odlander B., Claesson H.E., Bergman T., Radmark O., Joernvall H., Haeggstrom J.Z. Arch. Biochem. Biophys. 287:167-174(1991) [PubMed: 1897988] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-22, FUNCTION, CATALYTIC ACTIVITY. Tissue: B-cell.
[8]	"Leukotriene A4 hydrolase in human leukocytes. Purification and properties." Radmark O., Shimizu T., Joernvall H., Samuelsson B. J. Biol. Chem. 259:12339-12345(1984) [PubMed: 6490615] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16.
[9]	"The human leukotriene A4 hydrolase gene is expressed in two alternatively spliced mRNA forms." Jendraschak E., Kaminski W.E., Kiefl R., von Schacky C. Biochem. J. 314:733-737(1996) [PubMed: 8615763] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 511-611, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
[10]	"Molecular evolution and zinc ion binding motif of leukotriene A4 hydrolase." Toh H., Minami M., Shimizu T. Biochem. Biophys. Res. Commun. 171:216-221(1990) [PubMed: 1975494] [Abstract] Cited for: ZINC-BINDING, FUNCTION AS A PEPTIDASE, SIMILARITY TO ZINC PROTEASES.
[11]	"Leukotriene A4 hydrolase: a zinc metalloenzyme." Haeggstroem J.Z., Wetterholm A., Shapiro R., Vallee B.L., Samuelsson B. Biochem. Biophys. Res. Commun. 172:965-970(1990) [PubMed: 2244921] [Abstract] Cited for: ZINC-BINDING, FUNCTION AS A PEPTIDASE.
[12]	"Leukotriene A4 hydrolase: determination of the three zinc-binding ligands by site-directed mutagenesis and zinc analysis." Medina J.F., Wetterholm A., Raadmark O., Shapiro R., Haeggstroem J.Z., Vallee B.L., Samuelsson B. Proc. Natl. Acad. Sci. U.S.A. 88:7620-7624(1991) [PubMed: 1881903] [Abstract] Cited for: MUTAGENESIS OF ZINC LIGANDS.
[13]	"Leukotriene A4 hydrolase, a bifunctional enzyme. Distinction of leukotriene A4 hydrolase and aminopeptidase activities by site-directed mutagenesis at Glu-297." Minami M., Bito H., Ohishi N., Tsuge H., Miyano M., Mori M., Wada H., Mutoh H., Shimada S., Izumi T., Abe K., Shimuzu T. FEBS Lett. 309:353-357(1992) [PubMed: 1516710] [Abstract] Cited for: MUTAGENESIS OF GLU-297.
[14]	"Leukotriene A4 hydrolase: abrogation of the peptidase activity by mutation of glutamic acid-296." Wetterholm A., Medina J.F., Raadmark O., Shapiro R., Haeggstroem J.Z., Vallee B.L., Samuelsson B. Proc. Natl. Acad. Sci. U.S.A. 89:9141-9145(1992) [PubMed: 1357660] [Abstract] Cited for: MUTAGENESIS OF GLU-297.
[15]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]	"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-73; LYS-337; LYS-414 AND LYS-573, MASS SPECTROMETRY.
[17]	"Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation." Thunnissen M.M.G.M., Nordlund P., Haeggstroem J.Z. Nat. Struct. Biol. 8:131-135(2001) [PubMed: 11175901] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[18]	"Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms." Rudberg P.C., Tholander F., Thunnissen M.M.G.M., Haeggstroem J.Z. J. Biol. Chem. 277:1398-1404(2002) [PubMed: 11675384] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT GLN-272, MUTAGENESIS OF GLN-137; GLY-270; MET-271; GLU-272 AND ASN-273.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J03459 mRNA. Translation: AAA36176.1.
J02959 mRNA. Translation: AAA36177.1.
U27293 , U27275, U27276, U27277, U27278, U27279, U27280, U27281, U27282, U27283, U27284, U27285, U27286, U27287, U27288, U27289, U27290, U27291, U27292 Genomic DNA. Translation: AAA89077.1.
CR457068 mRNA. Translation: CAG33349.1.
CH471054 Genomic DNA. Translation: EAW97559.1.
BC032528 mRNA. Translation: AAH32528.1.
U43410 Genomic DNA. No translation available.
U43411 Genomic DNA. No translation available.

IPI

IPI00219077.
IPI00514090.

PIR

S65947.

RefSeq

NP_000886.1.

UniGene

Hs.190783
Hs.524648

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GW6	X-ray	2.20	A	2-611	[»]
1H19	X-ray	2.10	A	1-611	[»]
1HS6	X-ray	1.95	A	1-611	[»]
1SQM	X-ray	2.30	A	2-610	[»]
2R59	X-ray	1.89	A	2-611	[»]
2VJ8	X-ray	1.80	A	1-611	[»]
3B7R	X-ray	1.81	L	2-611	[»]
3B7S	X-ray	1.47	A	2-611	[»]
3B7T	X-ray	2.30	A	2-611	[»]
3B7U	X-ray	1.90	X	2-611	[»]
3CHO	X-ray	1.80	A	2-611	[»]
3CHP	X-ray	2.10	A	2-611	[»]
3CHQ	X-ray	2.09	A	2-611	[»]
3CHR	X-ray	2.20	A	2-611	[»]
3CHS	X-ray	2.55	A	2-611	[»]
3FTS	X-ray	2.33	A	1-611	[»]
3FTU	X-ray	1.90	A	1-611	[»]
3FTV	X-ray	1.70	A	1-611	[»]
3FTW	X-ray	1.85	A	1-611	[»]
3FTX	X-ray	1.96	A	1-611	[»]
3FTY	X-ray	2.15	A	1-611	[»]
3FU0	X-ray	1.80	A	1-611	[»]
3FU3	X-ray	2.00	A	1-611	[»]
3FU5	X-ray	2.30	A	1-611	[»]
3FU6	X-ray	2.05	A	1-611	[»]
3FUD	X-ray	2.20	A	1-611	[»]
3FUE	X-ray	2.38	A	1-611	[»]
3FUF	X-ray	2.60	A	1-611	[»]
3FUH	X-ray	1.80	A	1-611	[»]
3FUI	X-ray	2.20	A	1-611	[»]
3FUJ	X-ray	1.90	A	1-611	[»]
3FUK	X-ray	1.95	A	1-611	[»]
3FUM	X-ray	2.15	A	1-611	[»]
3FUN	X-ray	1.58	A	1-611	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P09960. 7 interactions.

STRING

P09960.

PTM databases

PhosphoSite

P09960.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00219077.

Proteomic databases

PRIDE

P09960.

Genome annotation databases

Ensembl

ENST00000228740; ENSP00000228740; ENSG00000111144; Homo sapiens. [Genome view]
ENST00000393070; ENSP00000376789; ENSG00000111144; Homo sapiens. [Genome view]
ENST00000413268; ENSP00000395051; ENSG00000111144; Homo sapiens. [Genome view]

GeneID

4048.

KEGG

hsa:4048.

UCSC

uc001ten.1. human.

Organism-specific databases

CTD

4048.

GeneCards

GC12M094897.

H-InvDB

HIX0010902.

HGNC

HGNC:6710. LTA4H.

HPA

CAB015221.
HPA008399.
HPA017017.

MIM

151570. gene.

PharmGKB

PA24345.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P09960.

HOVERGEN

P09960.

OMA

GQEVKYT.

Enzyme and pathway databases

BRENDA

3.3.2.6. 247.

Reactome

REACT_15314. Hormone biosynthesis.

Gene expression databases

ArrayExpress

P09960.

Bgee

P09960.

CleanEx

HS_LTA4H.

Genevestigator

P09960.

GermOnline

ENSG00000111144. Homo sapiens.

Family and domain databases

InterPro

IPR012777. Leuk_A4_hydro_aminopept.
IPR006025. Pept_M_Zn_BS.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]

PANTHER

PTHR11533. Peptidase_M1. 1 hit.

Pfam

PF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]

PRINTS

PR00756. ALADIPTASE.

TIGRFAMs

TIGR02411. leuko_A4_hydro. 1 hit.

PROSITE

PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

15856.

SOURCE

Search...

Entry information

Entry name

LKHA4_HUMAN

Accession

Primary (citable) accession number: P09960
Secondary accession number(s): Q6IAT6, Q9UCT7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 127 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.