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P49721

- PSB2_HUMAN

UniProt

P49721 - PSB2_HUMAN

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Protein
Proteasome subunit beta type-2
Gene
PSMB2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. This subunit has a trypsin-like activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  2. G1/S transition of mitotic cell cycle Source: Reactome
  3. RNA metabolic process Source: Reactome
  4. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  5. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  6. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  7. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  8. apoptotic process Source: Reactome
  9. cellular nitrogen compound metabolic process Source: Reactome
  10. gene expression Source: Reactome
  11. mRNA metabolic process Source: Reactome
  12. mitotic cell cycle Source: Reactome
  13. negative regulation of apoptotic process Source: Reactome
  14. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  15. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  16. protein polyubiquitination Source: Reactome
  17. regulation of apoptotic process Source: Reactome
  18. regulation of cellular amino acid metabolic process Source: Reactome
  19. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  20. response to organic cyclic compound Source: Ensembl
  21. response to organonitrogen compound Source: Ensembl
  22. small molecule metabolic process Source: Reactome
  23. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Protein family/group databases

MEROPSiT01.984.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-2 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C7-I
Multicatalytic endopeptidase complex subunit C7-I
Proteasome component C7-I
Gene namesi
Name:PSMB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9539. PSMB2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProt
  5. proteasome complex Source: ProtInc
  6. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33884.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Proteasome subunit beta type-2
PRO_0000148043Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP49721.
PaxDbiP49721.
PeptideAtlasiP49721.
PRIDEiP49721.

2D gel databases

OGPiP49721.
REPRODUCTION-2DPAGEIPI00028006.
P49721.

PTM databases

PhosphoSiteiP49721.

Expressioni

Inductioni

Up-regulated in ovarian cancer cell lines.1 Publication

Gene expression databases

BgeeiP49721.
CleanExiHS_PSMB2.
GenevestigatoriP49721.

Organism-specific databases

HPAiHPA026322.
HPA026324.

Interactioni

Subunit structurei

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 protein.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMB3P497204EBI-359335,EBI-603340

Protein-protein interaction databases

BioGridi111663. 70 interactions.
IntActiP49721. 19 interactions.
MINTiMINT-1144735.
STRINGi9606.ENSP00000362334.

Structurei

3D structure databases

ProteinModelPortaliP49721.
SMRiP49721. Positions 1-199.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000188743.
HOVERGENiHBG000815.
KOiK02734.
OMAiHFVRGEL.
OrthoDBiEOG7N63NQ.
PhylomeDBiP49721.
TreeFamiTF106219.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49721-1 [UniParc]FASTAAdd to Basket

« Hide

MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA    50
GDTVQFAEYI QKNVQLYKMR NGYELSPTAA ANFTRRNLAD CLRSRTPYHV 100
NLLLAGYDEH EGPALYYMDY LAALAKAPFA AHGYGAFLTL SILDRYYTPT 150
ISRERAVELL RKCLEELQKR FILNLPTFSV RIIDKNGIHD LDNISFPKQG 200
S 201
Length:201
Mass (Da):22,836
Last modified:October 1, 1996 - v1
Checksum:i04D085D7BAA76130
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D26599 mRNA. Translation: BAA05646.1.
CR456862 mRNA. Translation: CAG33143.1.
BT007137 mRNA. Translation: AAP35801.1.
AL354864, AL157951, AL357035 Genomic DNA. Translation: CAC36031.2.
AL357035, AL354864, AL157951 Genomic DNA. Translation: CAI22074.1.
AL157951, AL354864, AL357035 Genomic DNA. Translation: CAI23521.1.
CH471059 Genomic DNA. Translation: EAX07406.1.
CH471059 Genomic DNA. Translation: EAX07407.1.
BC101836 mRNA. Translation: AAI01837.1.
BC105126 mRNA. Translation: AAI05127.1.
BC107901 mRNA. Translation: AAI07902.1.
CCDSiCCDS394.1.
PIRiS55040.
RefSeqiNP_002785.1. NM_002794.4.
UniGeneiHs.471441.

Genome annotation databases

EnsembliENST00000373237; ENSP00000362334; ENSG00000126067.
GeneIDi5690.
KEGGihsa:5690.
UCSCiuc001bzf.2. human.

Polymorphism databases

DMDMi1709762.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D26599 mRNA. Translation: BAA05646.1 .
CR456862 mRNA. Translation: CAG33143.1 .
BT007137 mRNA. Translation: AAP35801.1 .
AL354864 , AL157951 , AL357035 Genomic DNA. Translation: CAC36031.2 .
AL357035 , AL354864 , AL157951 Genomic DNA. Translation: CAI22074.1 .
AL157951 , AL354864 , AL357035 Genomic DNA. Translation: CAI23521.1 .
CH471059 Genomic DNA. Translation: EAX07406.1 .
CH471059 Genomic DNA. Translation: EAX07407.1 .
BC101836 mRNA. Translation: AAI01837.1 .
BC105126 mRNA. Translation: AAI05127.1 .
BC107901 mRNA. Translation: AAI07902.1 .
CCDSi CCDS394.1.
PIRi S55040.
RefSeqi NP_002785.1. NM_002794.4.
UniGenei Hs.471441.

3D structure databases

ProteinModelPortali P49721.
SMRi P49721. Positions 1-199.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111663. 70 interactions.
IntActi P49721. 19 interactions.
MINTi MINT-1144735.
STRINGi 9606.ENSP00000362334.

Chemistry

BindingDBi P49721.
ChEMBLi CHEMBL3492.
DrugBanki DB00188. Bortezomib.

Protein family/group databases

MEROPSi T01.984.

PTM databases

PhosphoSitei P49721.

Polymorphism databases

DMDMi 1709762.

2D gel databases

OGPi P49721.
REPRODUCTION-2DPAGE IPI00028006.
P49721.

Proteomic databases

MaxQBi P49721.
PaxDbi P49721.
PeptideAtlasi P49721.
PRIDEi P49721.

Protocols and materials databases

DNASUi 5690.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373237 ; ENSP00000362334 ; ENSG00000126067 .
GeneIDi 5690.
KEGGi hsa:5690.
UCSCi uc001bzf.2. human.

Organism-specific databases

CTDi 5690.
GeneCardsi GC01M036042.
HGNCi HGNC:9539. PSMB2.
HPAi HPA026322.
HPA026324.
MIMi 602175. gene.
neXtProti NX_P49721.
PharmGKBi PA33884.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000188743.
HOVERGENi HBG000815.
KOi K02734.
OMAi HFVRGEL.
OrthoDBi EOG7N63NQ.
PhylomeDBi P49721.
TreeFami TF106219.

Enzyme and pathway databases

Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

ChiTaRSi PSMB2. human.
GeneWikii PSMB2.
GenomeRNAii 5690.
NextBioi 22102.
PROi P49721.
SOURCEi Search...

Gene expression databases

Bgeei P49721.
CleanExi HS_PSMB2.
Genevestigatori P49721.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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].
  2. "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].
  3. "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].
  4. "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].
  5. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  7. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 71-85 AND 171-181, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  8. "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 172-177 AND 186-193.
    Tissue: Keratinocyte.
  9. "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 72-85.
    Tissue: Placenta.
  10. "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.
  11. "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.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Screening for genetic abnormalities involved in ovarian carcinogenesis using retroviral expression libraries."
    Wada T., Yamashita Y., Saga Y., Takahashi K., Koinuma K., Choi Y.L., Kaneda R., Fujiwara S., Soda M., Watanabe H., Kurashina K., Hatanaka H., Enomoto M., Takada S., Mano H., Suzuki M.
    Int. J. Oncol. 35:973-976(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  14. "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.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSB2_HUMAN
AccessioniPrimary (citable) accession number: P49721
Secondary accession number(s): D3DPS0, P31145, Q9BWZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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