Q12904 (AIMP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aminoacyl tRNA synthase complex-interacting multifunctional protein 1

Alternative name(s):
Multisynthase complex auxiliary component p43

Cleaved into the following chain:

1. Endothelial monocyte-activating polypeptide 2
   Short name=EMAP-2
   Alternative name(s):
   Endothelial monocyte-activating polypeptide II
   Short name=EMAP-II
   Small inducible cytokine subfamily E member 1

Gene names

Name:	AIMP1
Synonyms:	EMAP2, SCYE1

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	312 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	Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7. Ref.5 Ref.7 Ref.8 Ref.9 Ref.13 Ref.18
Subunit structure	Homodimer. Component of the multisynthase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl and aspartyl-tRNA synthases, and three auxiliary proteins, EEF1E1/p18, AIMP2/p38 and AIMP1/p43. Interacts (via N-terminus) with RARS (via N-terminus). Interacts (via C-terminus) with SMURF2. Interacts (via N-terminus) with HSP90B1/gp96 (via C-terminus). Interacts with PSMA7. Ref.5 Ref.7 Ref.12 Ref.13
Subcellular location	Nucleus. Cytoplasm › cytosol. Cytoplasmic vesicle › secretory vesicle By similarity. Secreted By similarity. Endoplasmic reticulum By similarity. Golgi apparatus By similarity. Note: Enriched in secretory vesicles of pancreatic alpha cells and secreted from the pancreas in response to low glucose levels By similarity. Also secreted in response to hypoxia and both apoptotic and necrotic cell death. Ref.6 Ref.10
Post-translational modification	Cleaved by caspase-7 in response to apoptosis to produce EMAP-II.
Involvement in disease	Leukodystrophy, hypomyelinating, 3 (HLD3) [MIM:260600]: A severe autosomal recessive hypomyelinating leukodystrophy characterized by early infantile onset of global developmental delay, lack of development, lack of speech acquisition, and peripheral spasticity associated with decreased myelination in the central nervous system. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14
Sequence similarities	Contains 1 tRNA-binding domain.

Ontologies

Keywords
Biological process	Angiogenesis Apoptosis Carbohydrate metabolism Cell adhesion Glucose metabolism Inflammatory response Protein biosynthesis
Cellular component	Cytoplasm Cytoplasmic vesicle Endoplasmic reticulum Golgi apparatus Nucleus Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Leukodystrophy
Ligand	RNA-binding tRNA-binding
Molecular function	Cytokine
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cell-cell signaling Inferred from direct assay PubMed 11741979. Source: HGNC chemotaxis Traceable author statement PubMed 7545917. Source: ProtInc glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW inflammatory response Traceable author statement PubMed 7545917. Source: ProtInc leukocyte migration Inferred from direct assay Ref.7. Source: HGNC negative regulation of endothelial cell proliferation Inferred from direct assay PubMed 11741979. Source: HGNC signal transduction Non-traceable author statement PubMed 9405472. Source: ProtInc tRNA aminoacylation for protein translation Traceable author statement. Source: Reactome
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell aminoacyl-tRNA synthetase multienzyme complex Inferred from direct assay Ref.10. Source: HGNC cytosol Traceable author statement. Source: Reactome endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Traceable author statement PubMed 7545917. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell transport vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cell surface binding Inferred from direct assay PubMed 11741979. Source: HGNC cytokine activity Inferred from sequence or structural similarity Ref.7. Source: HGNC protein homodimerization activity Inferred from direct assay Ref.7. Source: HGNC tRNA binding Inferred from direct assay Ref.7. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
gag	P04591	3	EBI-1045802,EBI-6179719	From a different organism.

Alternative products

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

Isoform 1 (identifier: Q12904-1)

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: Q12904-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLPAVAVSEPVVLRFMIFCRLLAKM

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 312

312

Aminoacyl tRNA synthase complex-interacting multifunctional protein 1

PRO_0000223394

Chain

147 – 312

166

Endothelial monocyte-activating polypeptide 2

PRO_0000019242

Regions

Domain

151 – 252

102

tRNA-binding

Region

6 – 46

41

Required for fibroblast proliferation

Region

54 – 194

141

Interaction with HSP90B1 By similarity

Region

101 – 114

14

Required for endothelial cell death

Region

114 – 192

79

Required for endothelial cell migration

Natural variations

Alternative sequence

1

1

M → MLPAVAVSEPVVLRFMIFCR LLAKM in isoform 2.

VSP_042197

Natural variant

79

1

P → A. Ref.1
Corresponds to variant rs1134648 [ dbSNP | Ensembl ].

VAR_025212

Natural variant

104

1

T → A.
Corresponds to variant rs2230254 [ dbSNP | Ensembl ].

VAR_029156

Natural variant

117

1

T → A.
Corresponds to variant rs2230255 [ dbSNP | Ensembl ].

VAR_050124

Experimental info

Sequence conflict

138

1

Q → R in BAG64889. Ref.3

Secondary structure

1

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312

Helix Strand Turn

Details...

Helix

152 – 154

3

Beta strand

157 – 168

12

Beta strand

171 – 180

10

Beta strand

182 – 185

4

Beta strand

187 – 191

5

Turn

194 – 196

3

Helix

199 – 202

4

Beta strand

205 – 210

6

Beta strand

216 – 220

5

Beta strand

221 – 223

3

Beta strand

229 – 232

4

Beta strand

235 – 238

4

Beta strand

262 – 264

3

Turn

266 – 268

3

Helix

271 – 274

4

Helix

275 – 277

3

Beta strand

278 – 280

3

Beta strand

284 – 288

5

Turn

296 – 298

3

Beta strand

310 – 312

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 24, 2006. Version 2. Checksum: 5F0BF73E58810C60	FASTA	312	34,353
	10 20 30 40 50 60 MANNDAVLKR LEQKGAEADQ IIEYLKQQVS LLKEKAILQA TLREEKKLRV ENAKLKKEIE 70 80 90 100 110 120 ELKQELIQAE IQNGVKQIPF PSGTPLHANS MVSENVIQST AVTTVSSGTK EQIKGGTGDE 130 140 150 160 170 180 KKAKEKIEKK GEKKEKKQQS IAGSADSKPI DVSRLDLRIG CIITARKHPD ADSLYVEEVD 190 200 210 220 230 240 VGEIAPRTVV SGLVNHVPLE QMQNRMVILL CNLKPAKMRG VLSQAMVMCA SSPEKIEILA 250 260 270 280 290 300 PPNGSVPGDR ITFDAFPGEP DKELNPKKKI WEQIQPDLHT NDECVATYKG VPFEVKGKGV 310 CRAQTMSNSG IK
	Isoform 2 [UniParc]. Checksum: C4D804F0180FD7D4	FASTA	336	37,039
	10 20 30 40 50 60 MLPAVAVSEP VVLRFMIFCR LLAKMANNDA VLKRLEQKGA EADQIIEYLK QQVSLLKEKA 70 80 90 100 110 120 ILQATLREEK KLRVENAKLK KEIEELKQEL IQAEIQNGVK QIPFPSGTPL HANSMVSENV 130 140 150 160 170 180 IQSTAVTTVS SGTKEQIKGG TGDEKKAKEK IEKKGEKKEK KQQSIAGSAD SKPIDVSRLD 190 200 210 220 230 240 LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQMQNRM VILLCNLKPA 250 260 270 280 290 300 KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP 310 320 330 DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a novel tumor-derived cytokine. Endothelial-monocyte activating polypeptide II." Kao J., Houck K., Fan Y., Haehnel I., Libutti S.K., Kayton M.L., Grikscheit T., Chabot J., Nowygrod R., Greenberg S., Kuang W.J., Leung D.W., Hayward J.R., Kisiel W., Heath M., Brett J., Stern D.M. J. Biol. Chem. 269:25106-25119(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-79.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
[4]	"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] (ISOFORM 1). Tissue: Pancreas.
[5]	"Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase." Park S.G., Jung K.H., Lee J.S., Jo Y.J., Motegi H., Kim S., Shiba K. J. Biol. Chem. 274:16673-16676(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RARS.
[6]	"Prostate adenocarcinoma cells release the novel proinflammatory polypeptide EMAP-II in response to stress." Barnett G., Jakobsen A.-M., Tas M., Rice K., Carmichael J., Murray J.C. Cancer Res. 60:2850-2857(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, CLEAVAGE.
[7]	"The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component." Shalak V., Kaminska M., Mitnacht-Kraus R., Vandenabeele P., Clauss M., Mirande M. J. Biol. Chem. 276:23769-23776(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[8]	"Dose-dependent biphasic activity of tRNA synthetase-associating factor, p43, in angiogenesis." Park S.G., Kang Y.-S., Ahn Y.H., Lee S.H., Kim K.-R., Kim K.-W., Koh G.Y., Ko Y.-G., Kim S. J. Biol. Chem. 277:45243-45248(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Monocyte cell adhesion induced by a human aminoacyl-tRNA synthetase-associated factor, p43: identification of the related adhesion molecules and signal pathways." Park H., Park S.G., Lee J.-W., Kim T., Kim G., Ko Y.-G., Kim S. J. Leukoc. Biol. 71:223-230(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Isolation and characterization of human nuclear and cytosolic multisynthetase complexes and the intracellular distribution of p43/EMAPII." Wolfe C.L., Warrington J.A., Davis S., Green S., Norcum M.T. Protein Sci. 12:2282-2290(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[11]	"Structural separation of different extracellular activities in aminoacyl-tRNA synthetase-interacting multi-functional protein, p43/AIMP1." Han J.M., Park S.G., Lee Y., Kim S. Biochem. Biophys. Res. Commun. 342:113-118(2006) [PubMed] [Europe PMC] [Abstract] Cited for: REGIONS INVOLVED IN FIBROBLAST PROLIFERATION; ENDOTHELIAL CELL DEATH AND ENDOTHELIAL MIGRATION.
[12]	"Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines." Bottoni A., Vignali C., Piccin D., Tagliati F., Luchin A., Zatelli M.C., Uberti E.C. J. Cell. Physiol. 212:293-297(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RARS.
[13]	"Endothelial monocyte activating polypeptide-II modulates endothelial cell responses by degrading hypoxia-inducible factor-1alpha through interaction with PSMA7, a component of the proteasome." Tandle A.T., Calvani M., Uranchimeg B., Zahavi D., Melillo G., Libutti S.K. Exp. Cell Res. 315:1850-1859(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PSMA7.
[14]	"Pelizaeus-Merzbacher-like disease caused by AIMP1/p43 homozygous mutation." Feinstein M., Markus B., Noyman I., Shalev H., Flusser H., Shelef I., Liani-Leibson K., Shorer Z., Cohen I., Khateeb S., Sivan S., Birk O.S. Am. J. Hum. Genet. 87:820-828(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN HLD3.
[15]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[16]	"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].
[17]	"A novel anti-tumor cytokine contains an RNA binding motif present in aminoacyl-tRNA synthetases." Kim Y., Shin J., Li R., Cheong C., Kim K., Kim S. J. Biol. Chem. 275:27062-27068(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 147-312.
[18]	"Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry." Renault L., Kerjan P., Pasqualato S., Menetrey J., Robinson J.-C., Kawaguchi S., Vassylyev D.G., Yokoyama S., Mirande M., Cherfils J. EMBO J. 20:570-578(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 148-312, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U10117 mRNA. Translation: AAA62202.1.
CR542281 mRNA. Translation: CAG47076.1.
AK095951 mRNA. Translation: BAG53174.1.
AK303965 mRNA. Translation: BAG64889.1.
BC014051 mRNA. Translation: AAH14051.1.

IPI

IPI00006252.

PIR

B55053.

RefSeq

NP_001135887.1. NM_001142415.1.
NP_001135888.1. NM_001142416.1.
NP_004748.2. NM_004757.3.

UniGene

Hs.591680.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E7Z	X-ray	2.05	A	148-312	[»]
1EUJ	X-ray	1.80	A/B	147-312	[»]
1FL0	X-ray	1.50	A	150-312	[»]

ProteinModelPortal

Q12904.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q12904. 3 interactions.

STRING

9606.ENSP00000378191.

PTM databases

PhosphoSite

Q12904.

Polymorphism databases

DMDM

85700432.

Proteomic databases

PaxDb

Q12904.

PRIDE

Q12904.

Protocols and materials databases

DNASU

9255.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000358008; ENSP00000350699; ENSG00000164022.
ENST00000394701; ENSP00000378191; ENSG00000164022.
ENST00000442366; ENSP00000405248; ENSG00000164022.

GeneID

9255.

KEGG

hsa:9255.

UCSC

uc003hyg.3. human.

Organism-specific databases

CTD

9255.

GeneCards

GC04P107236.

HGNC

HGNC:10648. AIMP1.

HPA

CAB017618.
HPA018476.

MIM

260600. phenotype.
603605. gene.

neXtProt

NX_Q12904.

Orphanet

280293. Pelizaeus-Merzbacher-like due to AIMP1 mutation.

PharmGKB

PA35578.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0073.

HOGENOM

HOG000230584.

HOVERGEN

HBG019053.

InParanoid

Q12904.

KO

K15437.

OMA

NDAVLKR.

PhylomeDB

Q12904.

Enzyme and pathway databases

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q12904.

Bgee

Q12904.

CleanEx

HS_SCYE1.

Genevestigator

Q12904.

GermOnline

ENSG00000164022. Homo sapiens.

Family and domain databases

Gene3D

2.40.50.140. 1 hit.

InterPro

IPR012340. NA-bd_OB-fold.
IPR002547. tRNA-bd_dom.
[Graphical view]

Pfam

PF01588. tRNA_bind. 1 hit.
[Graphical view]

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.

PROSITE

PS50886. TRBD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

AIMP1. human.

EvolutionaryTrace

Q12904.

GenomeRNAi

9255.

NextBio

34695.

SOURCE

Search...

Entry information

Entry name

AIMP1_HUMAN

Accession

Primary (citable) accession number: Q12904
Secondary accession number(s): B3KTR2 , B4E1S7, Q6FG28, Q96CQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
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.