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Protein

Proteasome subunit beta type-4

Gene

PSMB4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Mediates the lipopolysaccharide-induced signal macrophage proteasome (By similarity). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1.By similarity1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei46NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:HS08395-MONOMER.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-382556. ABC-family proteins mediated transport.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5678895. Defective CFTR causes cystic fibrosis.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-5689603. UCH proteinases.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiT01.987.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PSMB4
Synonyms:PROS26
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9541. PSMB4.

Subcellular locationi

  • Cytoplasm PROSITE-ProRule annotation
  • Nucleus By similarity

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5692.
OpenTargetsiENSG00000159377.
PharmGKBiPA33886.

Chemistry databases

ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Polymorphism and mutation databases

BioMutaiPSMB4.
DMDMi116242733.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000265791 – 452 PublicationsAdd BLAST45
ChainiPRO_000002658046 – 264Proteasome subunit beta type-4Add BLAST219

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei26PhosphoserineCombined sources1
Modified residuei102PhosphotyrosineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein, Zymogen

Proteomic databases

EPDiP28070.
MaxQBiP28070.
PaxDbiP28070.
PeptideAtlasiP28070.
PRIDEiP28070.
TopDownProteomicsiP28070.

2D gel databases

DOSAC-COBS-2DPAGEP28070.
OGPiP28070.
REPRODUCTION-2DPAGEIPI00555956.
SWISS-2DPAGEP28070.

PTM databases

iPTMnetiP28070.
PhosphoSitePlusiP28070.

Expressioni

Inductioni

Up-regulated in fibrolamellar carcinomas.1 Publication

Gene expression databases

BgeeiENSG00000159377.
CleanExiHS_PSMB4.
ExpressionAtlasiP28070. baseline and differential.
GenevisibleiP28070. HS.

Organism-specific databases

HPAiHPA006700.

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 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.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FSD2A1L4K13EBI-603350,EBI-5661036
PSMA3P257883EBI-603350,EBI-348380

Protein-protein interaction databases

BioGridi111665. 97 interactors.
DIPiDIP-33844N.
IntActiP28070. 32 interactors.
MINTiMINT-1192686.
STRINGi9606.ENSP00000290541.

Chemistry databases

BindingDBiP28070.

Structurei

Secondary structure

1264
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi51 – 53Combined sources3
Beta strandi56 – 61Combined sources6
Beta strandi64 – 70Combined sources7
Beta strandi73 – 75Combined sources3
Beta strandi78 – 81Combined sources4
Beta strandi87 – 91Combined sources5
Beta strandi94 – 101Combined sources8
Helixi102 – 122Combined sources21
Helixi130 – 146Combined sources17
Beta strandi153 – 161Combined sources9
Beta strandi164 – 170Combined sources7
Beta strandi172 – 174Combined sources3
Beta strandi176 – 178Combined sources3
Beta strandi180 – 183Combined sources4
Helixi187 – 190Combined sources4
Helixi192 – 201Combined sources10
Helixi207 – 224Combined sources18
Beta strandi232 – 238Combined sources7
Beta strandi241 – 248Combined sources8
Helixi255 – 258Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.602/N46-262[»]
4R67X-ray2.892/N/b/p46-262[»]
5A0Qelectron microscopy3.50N/b46-264[»]
5GJQelectron microscopy4.50g/u1-264[»]
5GJRelectron microscopy3.50g/u1-264[»]
5L4Gelectron microscopy4.024/X1-264[»]
5LE5X-ray1.80M/a46-264[»]
5LEXX-ray2.20M/a46-264[»]
5LEYX-ray1.90M/a46-264[»]
5LEZX-ray2.19M/a46-264[»]
5LF0X-ray2.41M/a46-264[»]
5LF1X-ray2.00M/a46-264[»]
5LF3X-ray2.10M/a46-264[»]
5LF4X-ray1.99M/a46-264[»]
5LF6X-ray2.07M/a46-264[»]
5LF7X-ray2.00M/a46-264[»]
5T0Celectron microscopy3.80AT/BT2-264[»]
5T0Gelectron microscopy4.40T2-264[»]
5T0Helectron microscopy6.80T2-264[»]
5T0Ielectron microscopy8.00T2-264[»]
5T0Jelectron microscopy8.00T2-264[»]
ProteinModelPortaliP28070.
SMRiP28070.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0185. Eukaryota.
ENOG410YAMA. LUCA.
GeneTreeiENSGT00390000000698.
HOGENOMiHOG000181719.
HOVERGENiHBG018194.
InParanoidiP28070.
KOiK02736.
OMAiRIMRVND.
OrthoDBiEOG091G0JV7.
PhylomeDBiP28070.
TreeFamiTF106220.

Family and domain databases

CDDicd03760. proteasome_beta_type_4. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28070-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAFLGSRSG LWAGGPAPGQ FYRIPSTPDS FMDPASALYR GPITRTQNPM
60 70 80 90 100
VTGTSVLGVK FEGGVVIAAD MLGSYGSLAR FRNISRIMRV NNSTMLGASG
110 120 130 140 150
DYADFQYLKQ VLGQMVIDEE LLGDGHSYSP RAIHSWLTRA MYSRRSKMNP
160 170 180 190 200
LWNTMVIGGY ADGESFLGYV DMLGVAYEAP SLATGYGAYL AQPLLREVLE
210 220 230 240 250
KQPVLSQTEA RDLVERCMRV LYYRDARSYN RFQIATVTEK GVEIEGPLST
260
ETNWDIAHMI SGFE
Length:264
Mass (Da):29,204
Last modified:October 17, 2006 - v4
Checksum:iB8701C565069F563
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti264E → D in CAG33101 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01207295M → I.Corresponds to variant rs1804241dbSNPEnsembl.1
Natural variantiVAR_075255212 – 214Missing Found in a patient with Nakajo syndrome; unknown pathological significance; patients' cells show proteasome assembly defects. 1 Publication3
Natural variantiVAR_013115234I → T.5 PublicationsCorresponds to variant rs4603dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS996.1.
PIRiS08186.
S45719.
S50147.
RefSeqiNP_002787.2. NM_002796.2.
UniGeneiHs.89545.

Genome annotation databases

EnsembliENST00000290541; ENSP00000290541; ENSG00000159377.
GeneIDi5692.
KEGGihsa:5692.
UCSCiuc001eyc.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS996.1.
PIRiS08186.
S45719.
S50147.
RefSeqiNP_002787.2. NM_002796.2.
UniGeneiHs.89545.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.602/N46-262[»]
4R67X-ray2.892/N/b/p46-262[»]
5A0Qelectron microscopy3.50N/b46-264[»]
5GJQelectron microscopy4.50g/u1-264[»]
5GJRelectron microscopy3.50g/u1-264[»]
5L4Gelectron microscopy4.024/X1-264[»]
5LE5X-ray1.80M/a46-264[»]
5LEXX-ray2.20M/a46-264[»]
5LEYX-ray1.90M/a46-264[»]
5LEZX-ray2.19M/a46-264[»]
5LF0X-ray2.41M/a46-264[»]
5LF1X-ray2.00M/a46-264[»]
5LF3X-ray2.10M/a46-264[»]
5LF4X-ray1.99M/a46-264[»]
5LF6X-ray2.07M/a46-264[»]
5LF7X-ray2.00M/a46-264[»]
5T0Celectron microscopy3.80AT/BT2-264[»]
5T0Gelectron microscopy4.40T2-264[»]
5T0Helectron microscopy6.80T2-264[»]
5T0Ielectron microscopy8.00T2-264[»]
5T0Jelectron microscopy8.00T2-264[»]
ProteinModelPortaliP28070.
SMRiP28070.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111665. 97 interactors.
DIPiDIP-33844N.
IntActiP28070. 32 interactors.
MINTiMINT-1192686.
STRINGi9606.ENSP00000290541.

Chemistry databases

BindingDBiP28070.
ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Protein family/group databases

MEROPSiT01.987.

PTM databases

iPTMnetiP28070.
PhosphoSitePlusiP28070.

Polymorphism and mutation databases

BioMutaiPSMB4.
DMDMi116242733.

2D gel databases

DOSAC-COBS-2DPAGEP28070.
OGPiP28070.
REPRODUCTION-2DPAGEIPI00555956.
SWISS-2DPAGEP28070.

Proteomic databases

EPDiP28070.
MaxQBiP28070.
PaxDbiP28070.
PeptideAtlasiP28070.
PRIDEiP28070.
TopDownProteomicsiP28070.

Protocols and materials databases

DNASUi5692.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000290541; ENSP00000290541; ENSG00000159377.
GeneIDi5692.
KEGGihsa:5692.
UCSCiuc001eyc.2. human.

Organism-specific databases

CTDi5692.
DisGeNETi5692.
GeneCardsiPSMB4.
HGNCiHGNC:9541. PSMB4.
HPAiHPA006700.
MIMi602177. gene.
neXtProtiNX_P28070.
OpenTargetsiENSG00000159377.
PharmGKBiPA33886.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0185. Eukaryota.
ENOG410YAMA. LUCA.
GeneTreeiENSGT00390000000698.
HOGENOMiHOG000181719.
HOVERGENiHBG018194.
InParanoidiP28070.
KOiK02736.
OMAiRIMRVND.
OrthoDBiEOG091G0JV7.
PhylomeDBiP28070.
TreeFamiTF106220.

Enzyme and pathway databases

BioCyciZFISH:HS08395-MONOMER.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-382556. ABC-family proteins mediated transport.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5678895. Defective CFTR causes cystic fibrosis.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-5689603. UCH proteinases.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPSMB4. human.
GeneWikiiPSMB4.
GenomeRNAii5692.
PROiP28070.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000159377.
CleanExiHS_PSMB4.
ExpressionAtlasiP28070. baseline and differential.
GenevisibleiP28070. HS.

Family and domain databases

CDDicd03760. proteasome_beta_type_4. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPSB4_HUMAN
AccessioniPrimary (citable) accession number: P28070
Secondary accession number(s): B2R9L3
, P31148, Q5SZS5, Q6IBI4, Q969L6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 191 of the entry and version 4 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

Caution

A report observed N-glycosylation at Asn-83 (PubMed:19139490). However, as the protein does not localize in an extracellular compartment of the cell, additional evidences are required to confirm this result.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.