P28070 (PSB4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteasome subunit beta type-4
EC=3.4.25.1

Alternative name(s):
26 kDa prosomal protein
Short name=HsBPROS26
Short name=PROS-26
Macropain beta chain
Multicatalytic endopeptidase complex beta chain
Proteasome beta chain
Proteasome chain 3
Short name=HsN3

Gene names

Name:	PSMB4
Synonyms:	PROS26

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	264 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	The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Mediates the lipopolysaccharide-induced signal macrophage proteasome By similarity. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. Ref.15
Catalytic activity	Cleavage of peptide bonds with very broad specificity.
Subunit structure	The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with HIV-1 TAT and HIV-1 NEF proteins. Interaction with HTLV-1 TAX protein favors NFKB1 activation. Interacts with bacterial lipopolysaccharide (LPS) By similarity. Forms a ternary complex with SMAD1 and OAZ1 before PSMB4 is incorporated into the 20S proteasome. Interacts with PRPF19. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Induction	Up-regulated in fibrolamellar carcinomas. Ref.20
Sequence similarities	Belongs to the peptidase T1B family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protease Threonine protease
PTM	Phosphoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Traceable author statement. Source: Reactome apoptotic process Traceable author statement. Source: Reactome gene expression Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome negative regulation of inflammatory response to antigenic stimulus Inferred from electronic annotation. Source: Compara negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome protein polyubiquitination Traceable author statement. Source: Reactome regulation of apoptotic process Traceable author statement. Source: Reactome regulation of cellular amino acid metabolic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome proteasome core complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	lipopolysaccharide binding Inferred from electronic annotation. Source: Compara threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 45	45			PRO_0000026579
	Chain	46 – 264	219	Proteasome subunit beta type-4		PRO_0000026580
Amino acid modifications
	Modified residue	102	1	Phosphotyrosine Ref.18
Natural variations
	Natural variant	95	1	M → I. Corresponds to variant rs1804241 [ dbSNP | Ensembl ].		VAR_012072
	Natural variant	234	1	I → T. Ref.1 Ref.2 Ref.4 Ref.6 Ref.7 Corresponds to variant rs4603 [ dbSNP | Ensembl ].		VAR_013115
Experimental info
	Sequence conflict	264	1	E → D in CAG33101. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P28070 [UniParc]. Last modified October 17, 2006. Version 4. Checksum: B8701C565069F563	FASTA	264	29,204
	10 20 30 40 50 60 MEAFLGSRSG LWAGGPAPGQ FYRIPSTPDS FMDPASALYR GPITRTQNPM VTGTSVLGVK 70 80 90 100 110 120 FEGGVVIAAD MLGSYGSLAR FRNISRIMRV NNSTMLGASG DYADFQYLKQ VLGQMVIDEE 130 140 150 160 170 180 LLGDGHSYSP RAIHSWLTRA MYSRRSKMNP LWNTMVIGGY ADGESFLGYV DMLGVAYEAP 190 200 210 220 230 240 SLATGYGAYL AQPLLREVLE KQPVLSQTEA RDLVERCMRV LYYRDARSYN RFQIATVTEK 250 260 GVEIEGPLST ETNWDIAHMI SGFE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analyses and inter-species comparisons of three novel human proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine potential proteolytic active-site residues." Nothwang H.G., Tamura T., Tanaka K., Ichihara A. Biochim. Biophys. Acta 1219:361-368(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-234.
[2]	"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], VARIANT THR-234. Tissue: Brain.
[3]	"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].
[4]	"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], VARIANT THR-234.
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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], VARIANT THR-234.
[7]	"Cloning and expression of a human pro(tea)some beta-subunit cDNA: a homologue of the yeast PRE4-subunit essential for peptidylglutamyl-peptide hydrolase activity." Gerards W.L., Hop F.W., Hendriks I.L., Bloemendal H. FEBS Lett. 346:151-155(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-264, VARIANT THR-234.
[8]	"Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome)." Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N., Slaughter C.A. Biochim. Biophys. Acta 1037:178-185(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 46-73.
[9]	Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J. Submitted (JUN-1992) to UniProtKB Cited for: PROTEIN SEQUENCE OF 46-57. Tissue: Liver.
[10]	"Human proteasome subunits from 2-dimensional gels identified by partial sequencing." Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B. Biochem. Biophys. Res. Commun. 205:1785-1789(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 132-139; 220-224 AND 241-259.
[11]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 232-237 AND 241-253. Tissue: Keratinocyte.
[12]	"Effects on NF-kappa B1/p105 processing of the interaction between the HTLV-1 transactivator Tax and the proteasome." Rousset R., Desbois C., Bantignies F., Jalinot P. Nature 381:328-331(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX.
[13]	"HsN3 proteasomal subunit as a target for human immunodeficiency virus type 1 Nef protein." Rossi F., Evstafieva A., Pedrali-Noy G., Gallina A., Milanesi G. Virology 237:33-45(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 NEF.
[14]	"Proteasomal degradation of Smad1 induced by bone morphogenetic proteins." Gruendler C., Lin Y., Farley J., Wang T. J. Biol. Chem. 276:46533-46543(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH SMAD1 AND OAZ1.
[15]	"A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs)." Lin Y., Martin J., Gruendler C., Farley J., Meng X., Li B.-Y., Lechleider R., Huff C., Kim R.H., Grasser W.A., Paralkar V., Wang T. BMC Cell Biol. 3:15-15(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH SMAD1 AND OAZ1, FUNCTION.
[16]	"Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits." Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E. FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[17]	"Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of the 20 S proteasome." Loescher M., Fortschegger K., Ritter G., Wostry M., Voglauer R., Schmid J.A., Watters S., Rivett A.J., Ajuh P., Lamond A.I., Katinger H., Grillari J. Biochem. J. 388:593-603(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRPF19.
[18]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-102, MASS SPECTROMETRY.
[19]	"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex." Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L. Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[20]	"Fibrolamellar carcinomas show overexpression of genes in the RAS, MAPK, PIK3, and xenobiotic degradation pathways." Kannangai R., Vivekanandan P., Martinez-Murillo F., Choti M., Torbenson M. Hum. Pathol. 38:639-644(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[21]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D26600 mRNA. Translation: BAA05647.1. AK313825 mRNA. Translation: BAG36560.1. CR456820 mRNA. Translation: CAG33101.1. BT006917 mRNA. Translation: AAP35563.1. AL589764 Genomic DNA. Translation: CAI16806.1. CH471121 Genomic DNA. Translation: EAW53442.1. S71381 mRNA. Translation: AAB31085.1.
IPI	IPI00555956.
PIR	S08186. S45719. S50147.
RefSeq	NP_002787.2. NM_002796.2.
UniGene	Hs.89545.
3D structure databases
ProteinModelPortal	P28070.
ModBase	Search...
Protein-protein interaction databases
IntAct	P28070. 10 interactions.
MINT	MINT-1192686.
STRING	9606.ENSP00000290541.
Protein family/group databases
MEROPS	T01.987.
PTM databases
PhosphoSite	P28070.
Polymorphism databases
DMDM	116242733.
2D gel databases
DOSAC-COBS-2DPAGE	P28070.
OGP	P28070.
REPRODUCTION-2DPAGE	IPI00555956.
SWISS-2DPAGE	P28070.
Proteomic databases
PaxDb	P28070.
PeptideAtlas	P28070.
PRIDE	P28070.
Protocols and materials databases
DNASU	5692.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000290541; ENSP00000290541; ENSG00000159377.
GeneID	5692.
KEGG	hsa:5692.
UCSC	uc001eyc.1. human.
Organism-specific databases
CTD	5692.
GeneCards	GC01P151372.
HGNC	HGNC:9541. PSMB4.
HPA	HPA006700.
MIM	602177. gene.
neXtProt	NX_P28070.
PharmGKB	PA33886.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0638.
HOGENOM	HOG000181719.
HOVERGEN	HBG018194.
InParanoid	P28070.
KO	K02736.
OMA	RIMRVND.
OrthoDB	EOG4F1X3R.
PhylomeDB	P28070.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_115566. Cell Cycle. REACT_116125. Disease. REACT_13505. Proteasome mediated degradation of PAK-2p34. REACT_21257. Metabolism of RNA. REACT_21300. Mitotic M-M/G1 phases. REACT_383. DNA Replication. REACT_578. Apoptosis. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_6900. Immune System. REACT_71. Gene Expression.
Gene expression databases
Bgee	P28070.
CleanEx	HS_PSMB4.
Genevestigator	P28070.
GermOnline	ENSG00000159377. Homo sapiens.
Family and domain databases
InterPro	IPR016050. Proteasome_bsu_CS. IPR016295. Proteasome_endopept_cplx_B. IPR001353. Proteasome_sua/b. IPR023333. Proteasome_suB-type. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. [Graphical view]
PIRSF	PIRSF001213. Psome_endopept_beta. 1 hit.
PROSITE	PS00854. PROTEASOME_B_1. 1 hit. PS51476. PROTEASOME_B_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PSMB4. human.
GenomeRNAi	5692.
NextBio	22110.
SOURCE	Search...

Entry information

Entry name

PSB4_HUMAN

Accession

Primary (citable) accession number: P28070
Secondary accession number(s): B2R9L3 , P31148, Q5SZS5, Q6IBI4, Q969L6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 151 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.