Reviewed, UniProtKB/Swiss-Prot Q9UHC3 (ACCN3_HUMAN)

Names and origin

Protein names

Recommended name:
    Amiloride-sensitive cation channel 3
Alternative name(s):
    Neuronal amiloride-sensitive cation channel 3
    Acid-sensing ion channel 3
      Short name=ASIC3
      Short name=hASIC3
    Testis sodium channel 1
      Short name=hTNaC1

Gene names

Name:	ACCN3
Synonyms:	ASIC3, SLNAC1, TNAC1

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

General annotation (Comments)

Function	Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Generates a biphasic current with a fast inactivating and a slow sustained phase. In sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissue. May be involved in hyperalgesia. May play a role in mechanoreception. Heteromeric channel assembly seems to modulate channel properties. Ref.2 Ref.3
Subunit structure	Homotetramer or heterotetramer with other ASIC proteins Probable. Interacts with STOM and DLG4 By similarity. Interacts with LIN7B, MAGI1/BAIAP1, GOPC and ACCN1.
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity. Cytoplasm By similarity. Note: Cell surface expression may be stabilized by interaction with LIN7B and cytoplasmic retention by interaction with DLG4. In part cytoplasmic in cochlea cells By similarity.
Tissue specificity	Expressed by sensory neurons. Strongly expressed in brain, spinal chord, lung, lymph nodes, kidney, pituitary, heart and testis. Ref.3 Ref.1
Developmental stage	Expressed in fetal tissues, expression increases in lung and kidney adult tissues. Ref.3
Domain	The PDZ domain-binding motif is involved in interaction with LIN7A, GOPC and MAGI1.
Post-translational modification	Phosphorylated by PKA. Phosphorylated by PKC. In vitro, PRKCABP/PICK-1 is necessary for PKC phosphorylation and activation of a ACCN3/ASIC3-ACCN1/ASIC2b channel, but does not activate a homomeric ACCN3 channel By similarity.
Miscellaneous	Potentiated by FMRFamide-related neuropeptides. Sensitized and potentiated by NPSF. Regulated by lactate and Ca2+. Inhibited by anti-inflammatory drugs, like salicylic acid By similarity. Sensitized and potentiated by NPFF.
Sequence similarities	Belongs to the amiloride-sensitive sodium channel family.
Sequence caution	The sequence BAA25897.1 differs from that shown. Reason: Frameshift at positions 303, 305 and 313.

Ontologies

Keywords
Biological process	Ion transport Sodium transport Transport
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane
Ligand	Sodium
Molecular function	Ionic channel Sodium channel
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	sensory perception Ref.2 Traceable author statement. Source: ProtInc signal transduction Ref.2 Traceable author statement. Source: ProtInc sodium ion transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc
Molecular function	amiloride-sensitive sodium channel activity Inferred from electronic annotation. Source: InterPro sodium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UHC3-1)

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: Q9UHC3-2)

Also known as: ASIC3b;

The sequence of this isoform differs from the canonical sequence as follows:
     487-531: LQEGLGSHRT...HRTCYLVTQL → TSHPSLCRHQ...AFPSSPQIKS

Isoform 3 (identifier: Q9UHC3-3)

Also known as: ASIC3c;

The sequence of this isoform differs from the canonical sequence as follows:
     506-531: RPPTPPCAVTKTLSASHRTCYLVTQL → STLLCSEDLPPLPVPSPRLSPPPTAPATLSHSSRPAVCVLGAPP

Isoform 4 (identifier: Q9UHC3-4)

Also known as: c;

The sequence of this isoform differs from the canonical sequence as follows:
     356-407: DAMLRKDSCA...NRSEAYIAEN → GRTCWPWTSS...GPACSPSSRS
     408-531: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 531	531	Amiloride-sensitive cation channel 3		PRO_0000181301
Regions
	Topological domain	1 – 43	43	Cytoplasmic Potential
	Transmembrane	44 – 61	18	Potential
	Topological domain	62 – 441	380	Extracellular Potential
	Transmembrane	442 – 460	19	Potential
	Topological domain	461 – 531	71	Cytoplasmic Potential
	Motif	528 – 531	4	PDZ-binding
Sites
	Site	26	1	Potassium ion selectivity and permeability By similarity
Amino acid modifications
	Modified residue	375	1	Phosphotyrosine Ref.12
	Modified residue	521	1	Phosphoserine By similarity
	Glycosylation	175	1	N-linked (GlcNAc...) Potential
	Glycosylation	398	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	356 – 407	52	DAMLR…YIAEN → GRTCWPWTSSLRPSTMRPWS RRRPMRCQSCLVTLGARWGC SSGPACSPSSRS in isoform 4.		VSP_015600
	Alternative sequence	408 – 531	124	Missing in isoform 4.		VSP_015601
	Alternative sequence	487 – 531	45	LQEGL…LVTQL → TSHPSLCRHQDSLRLPPHLL PCHTALDLLSVSSEPRPDIL DMPSLHVAFPSSPQIKS in isoform 2.		VSP_015602
	Alternative sequence	506 – 531	26	RPPTP…LVTQL → STLLCSEDLPPLPVPSPRLS PPPTAPATLSHSSRPAVCVL GAPP in isoform 3.		VSP_015603
	Natural variant	228	1	N → S: dbSNP rs1864545.		VAR_052037
Experimental info
	Mutagenesis	528	1	V → A: No effect on interaction with LIN7B, MAGI1 and GOPC. Ref.11
	Mutagenesis	529	1	T → A: Loss of interaction with LIN7B, MAGI1. Ref.11
	Mutagenesis	530	1	Q → A: Loss of interaction with GOPC. No effect on interaction LIN7B and MAGI1. Ref.11
	Mutagenesis	531	1	L → A: Loss of interaction with LIN7B, MAGI1 and GOPC. Ref.11
	Sequence conflict	13	1	P → Q Ref.1
	Sequence conflict	13	1	P → Q Ref.3
	Sequence conflict	14	1	A → P Ref.3
	Sequence conflict	85	1	I → V in AAC62935. Ref.3
	Sequence conflict	243 – 244	2	SQ → GH in BAA25897. Ref.1
	Sequence conflict	358	1	M → I in AAC62935. Ref.3
	Sequence conflict	397	1	L → F in BAA25897. Ref.1
	Sequence conflict	400	1	S → R in BAA25897. Ref.1
	Sequence conflict	518	1	L → F in BAA25897. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 13, 2005. Version 2. Checksum: A46DD64590EC4871	FASTA	531	58,905
	10 20 30 40 50 60 MKPTSGPEEA RRPASDIRVF ASNCSMHGLG HVFGPGSLSL RRGMWAAAVV LSVATFLYQV 70 80 90 100 110 120 AERVRYYREF HHQTALDERE SHRLIFPAVT LCNINPLRRS RLTPNDLHWA GSALLGLDPA 130 140 150 160 170 180 EHAAFLRALG RPPAPPGFMP SPTFDMAQLY ARAGHSLDDM LLDCRFRGQP CGPENFTTIF 190 200 210 220 230 240 TRMGKCYTFN SGADGAELLT TTRGGMGNGL DIMLDVQQEE YLPVWRDNEE TPFEVGIRVQ 250 260 270 280 290 300 IHSQEEPPII DQLGLGVSPG YQTFVSCQQQ QLSFLPPPWG DCSSASLNPN YEPEPSDPLG 310 320 330 340 350 360 SPSPSPSPPY TLMGCRLACE TRYVARKCGC RMVYMPGDVP VCSPQQYKNC AHPAIDAMLR 370 380 390 400 410 420 KDSCACPNPC ASTRYAKELS MVRIPSRAAA RFLARKLNRS EAYIAENVLA LDIFFEALNY 430 440 450 460 470 480 ETVEQKKAYE MSELLGDIGG QMGLFIGASL LTILEILDYL CEVFRDKVLG YFWNRQHSQR 490 500 510 520 530 HSSTNLLQEG LGSHRTQVPH LSLGPRPPTP PCAVTKTLSA SHRTCYLVTQ L
	Isoform 2 (ASIC3b). Checksum: 9411BD1485BA93F1	FASTA	543	60,332
	10 20 30 40 50 60 MKPTSGPEEA RRPASDIRVF ASNCSMHGLG HVFGPGSLSL RRGMWAAAVV LSVATFLYQV 70 80 90 100 110 120 AERVRYYREF HHQTALDERE SHRLIFPAVT LCNINPLRRS RLTPNDLHWA GSALLGLDPA 130 140 150 160 170 180 EHAAFLRALG RPPAPPGFMP SPTFDMAQLY ARAGHSLDDM LLDCRFRGQP CGPENFTTIF 190 200 210 220 230 240 TRMGKCYTFN SGADGAELLT TTRGGMGNGL DIMLDVQQEE YLPVWRDNEE TPFEVGIRVQ 250 260 270 280 290 300 IHSQEEPPII DQLGLGVSPG YQTFVSCQQQ QLSFLPPPWG DCSSASLNPN YEPEPSDPLG 310 320 330 340 350 360 SPSPSPSPPY TLMGCRLACE TRYVARKCGC RMVYMPGDVP VCSPQQYKNC AHPAIDAMLR 370 380 390 400 410 420 KDSCACPNPC ASTRYAKELS MVRIPSRAAA RFLARKLNRS EAYIAENVLA LDIFFEALNY 430 440 450 460 470 480 ETVEQKKAYE MSELLGDIGG QMGLFIGASL LTILEILDYL CEVFRDKVLG YFWNRQHSQR 490 500 510 520 530 540 HSSTNLTSHP SLCRHQDSLR LPPHLLPCHT ALDLLSVSSE PRPDILDMPS LHVAFPSSPQ IKS
	Isoform 3 (ASIC3c). Checksum: ED2C4D628AF9E18F	FASTA	549	60,491
	10 20 30 40 50 60 MKPTSGPEEA RRPASDIRVF ASNCSMHGLG HVFGPGSLSL RRGMWAAAVV LSVATFLYQV 70 80 90 100 110 120 AERVRYYREF HHQTALDERE SHRLIFPAVT LCNINPLRRS RLTPNDLHWA GSALLGLDPA 130 140 150 160 170 180 EHAAFLRALG RPPAPPGFMP SPTFDMAQLY ARAGHSLDDM LLDCRFRGQP CGPENFTTIF 190 200 210 220 230 240 TRMGKCYTFN SGADGAELLT TTRGGMGNGL DIMLDVQQEE YLPVWRDNEE TPFEVGIRVQ 250 260 270 280 290 300 IHSQEEPPII DQLGLGVSPG YQTFVSCQQQ QLSFLPPPWG DCSSASLNPN YEPEPSDPLG 310 320 330 340 350 360 SPSPSPSPPY TLMGCRLACE TRYVARKCGC RMVYMPGDVP VCSPQQYKNC AHPAIDAMLR 370 380 390 400 410 420 KDSCACPNPC ASTRYAKELS MVRIPSRAAA RFLARKLNRS EAYIAENVLA LDIFFEALNY 430 440 450 460 470 480 ETVEQKKAYE MSELLGDIGG QMGLFIGASL LTILEILDYL CEVFRDKVLG YFWNRQHSQR 490 500 510 520 530 540 HSSTNLLQEG LGSHRTQVPH LSLGPSTLLC SEDLPPLPVP SPRLSPPPTA PATLSHSSRP AVCVLGAPP
	Isoform 4 (c). Checksum: 0C6D7DCF3F525596	FASTA	407	44,999
	10 20 30 40 50 60 MKPTSGPEEA RRPASDIRVF ASNCSMHGLG HVFGPGSLSL RRGMWAAAVV LSVATFLYQV 70 80 90 100 110 120 AERVRYYREF HHQTALDERE SHRLIFPAVT LCNINPLRRS RLTPNDLHWA GSALLGLDPA 130 140 150 160 170 180 EHAAFLRALG RPPAPPGFMP SPTFDMAQLY ARAGHSLDDM LLDCRFRGQP CGPENFTTIF 190 200 210 220 230 240 TRMGKCYTFN SGADGAELLT TTRGGMGNGL DIMLDVQQEE YLPVWRDNEE TPFEVGIRVQ 250 260 270 280 290 300 IHSQEEPPII DQLGLGVSPG YQTFVSCQQQ QLSFLPPPWG DCSSASLNPN YEPEPSDPLG 310 320 330 340 350 360 SPSPSPSPPY TLMGCRLACE TRYVARKCGC RMVYMPGDVP VCSPQQYKNC AHPAIGRTCW 370 380 390 400 PWTSSLRPST MRPWSRRRPM RCQSCLVTLG ARWGCSSGPA CSPSSRS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a DEG/ENaC sodium channel cDNA from human testis." Ishibashi K., Marumo F. Biochem. Biophys. Res. Commun. 245:589-593(1998) [PubMed: 9571199] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Testis.
[2]	"Identification, functional expression and chromosomal localisation of a sustained human proton-gated cation channel." de Weille J.R., Bassilana F., Lazdunski M., Waldmann R. FEBS Lett. 433:257-260(1998) [PubMed: 9744806] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION. Tissue: Embryo.
[3]	"Molecular cloning and regional distribution of a human proton receptor subunit with biphasic functional properties." Babinski K., Le K.-T., Seguela P. J. Neurochem. 72:51-57(1999) [PubMed: 9886053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION. Tissue: Fetal brain.
[4]	"ASIC3b and ASIC3c, new modulatory subunits of the acid sensing ion channel family." Renard S., Besnard F., Partiseti M., Graham D. Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
[5]	"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] (ISOFORM 2). Tissue: Brain.
[6]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Brain.
[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]	"Mammalian ASIC2a and ASIC3 subunits co-assemble into heteromeric proton-gated channels sensitive to Gd3+." Babinski K., Catarsi S., Biagini G., Seguela P. J. Biol. Chem. 275:28519-28525(2000) [PubMed: 10842183] [Abstract] Cited for: INTERACTION WITH ACCN1.
[9]	"Selective modulation of heteromeric ASIC proton-gated channels by neuropeptide FF." Catarsi S., Babinski K., Seguela P. Neuropharmacology 41:592-600(2001) [PubMed: 11587714] [Abstract] Cited for: REGULATION BY NPFF.
[10]	"cAMP-dependent protein kinase phosphorylation of the acid-sensing ion channel-1 regulates its binding to the protein interacting with C-kinase-1." Leonard A.S., Yermolaieva O., Hruska-Hageman A., Askwith C.C., Price M.P., Wemmie J.A., Welsh M.J. Proc. Natl. Acad. Sci. U.S.A. 100:2029-2034(2003) [PubMed: 12578970] [Abstract] Cited for: PHOSPHORYLATION BY PKA.
[11]	"PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current." Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J. J. Biol. Chem. 279:46962-46968(2004) [PubMed: 15317815] [Abstract] Cited for: INTERACTION WITH LIN7B; MAGI1 AND GOPC, MUTAGENESIS OF VAL-528; THR-529; GLN-530 AND LEU-531.
[12]	"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction." Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R. Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-375, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB010575 mRNA. Translation: BAA25897.1. Frameshift. AF095897 mRNA. Translation: AAC64188.1. AF057711 mRNA. Translation: AAC62935.1. AF195024 mRNA. Translation: AAF19817.1. AF195025 mRNA. Translation: AAF19818.1. AK313926 mRNA. Translation: BAG36647.1. AB209421 mRNA. Translation: BAD92658.1. Different initiation. CH471173 Genomic DNA. Translation: EAW54052.1.
IPI	IPI00025345. IPI00220064. IPI00295344. IPI00556174.
PIR	JE0091.
RefSeq	NP_004760.1. NP_064717.1. NP_064718.1.
UniGene	Hs.647113
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9UHC3.
Proteomic databases
PRIDE	Q9UHC3.
Genome annotation databases
Ensembl	ENST00000349064; ENSP00000344838; ENSG00000213199; Homo sapiens. [Genome view]
GeneID	9311.
KEGG	hsa:9311.
UCSC	uc003win.2. human. uc003wio.2. human. uc003wip.2. human.
Organism-specific databases
CTD	9311.
GeneCards	GC07P150357.
H-InvDB	HIX0058417.
HGNC	HGNC:101. ACCN3.
MIM	611741. gene.
PharmGKB	PA24435.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q9UHC3.
OMA	GHALEDM.
Gene expression databases
ArrayExpress	Q9UHC3.
Bgee	Q9UHC3.
CleanEx	HS_ACCN3.
Genevestigator	Q9UHC3.
GermOnline	ENSG00000197150. Homo sapiens.
Family and domain databases
InterPro	IPR004724. EnaC. IPR001873. Na+channel_ASC. [Graphical view]
PANTHER	PTHR11690. Na+channel_ASC. 1 hit.
Pfam	PF00858. ASC. 1 hit. [Graphical view]
PRINTS	PR01078. AMINACHANNEL.
PROSITE	PS01206. ASC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	34875.
SOURCE	Search...

Entry information

Entry name

ACCN3_HUMAN

Accession

Primary (citable) accession number: Q9UHC3
Secondary accession number(s): B2R9V0 , O60263, O75906, Q59FN9, Q9UER8, Q9UHC4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	September 13, 2005
Last modified:	December 15, 2009
This is version 73 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.