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Protein

26S protease regulatory subunit 8

Gene

PSMC5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi190 – 197ATPSequence analysis8

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • proteasome-activating ATPase activity Source: GO_Central
  • TBP-class protein binding Source: GO_Central
  • thyrotropin-releasing hormone receptor binding Source: UniProtKB
  • transcription cofactor activity Source: ProtInc
  • transcription factor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS01562-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.

Names & Taxonomyi

Protein namesi
Recommended name:
26S protease regulatory subunit 8
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT6
Proteasome 26S subunit ATPase 5
Proteasome subunit p45
Thyroid hormone receptor-interacting protein 1
Short name:
TRIP1
p45/SUG
Gene namesi
Name:PSMC5
Synonyms:SUG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:9552. PSMC5.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB
  • cytosol Source: Reactome
  • cytosolic proteasome complex Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • inclusion body Source: Ensembl
  • membrane Source: UniProtKB
  • nuclear proteasome complex Source: GO_Central
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • proteasome accessory complex Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome regulatory particle, base subcomplex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5705.
OpenTargetsiENSG00000087191.
PharmGKBiPA33897.

Polymorphism and mutation databases

BioMutaiPSMC5.
DMDMi49065819.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000847212 – 40626S protease regulatory subunit 8Add BLAST405

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei120PhosphoserineCombined sources1
Modified residuei222N6-acetyllysineCombined sources1
Isoform 2 (identifier: P62195-2)
Modified residuei1N-acetylmethionineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP62195.
MaxQBiP62195.
PaxDbiP62195.
PeptideAtlasiP62195.
PRIDEiP62195.

PTM databases

iPTMnetiP62195.
PhosphoSitePlusiP62195.
SwissPalmiP62195.

Expressioni

Gene expression databases

BgeeiENSG00000087191.
CleanExiHS_PSMC5.
ExpressionAtlasiP62195. baseline and differential.
GenevisibleiP62195. HS.

Organism-specific databases

HPAiHPA017871.
HPA064293.

Interactioni

Subunit structurei

Component of a complex with USP49 and RUVBL1. Interacts with PRPF19. Interacts with TRIM5. Interacts with NDC80. Interacts with PAAF1. Interacts, in vitro, with the thyroid hormone receptor (in a thyroid hormone T3-dependent manner) and with retinoid X receptor (RXR).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P03255-12EBI-357745,EBI-6692439From a different organism.
Camk2aP112754EBI-357745,EBI-2640645From a different organism.
Camk2bP084133EBI-357745,EBI-916155From a different organism.
ERCC3P194474EBI-357745,EBI-1183307
FOSQ6FG413EBI-357745,EBI-10198738
KRT38O760153EBI-357745,EBI-1047263
KRT40Q6A1623EBI-357745,EBI-10171697
PAAF1Q9BRP42EBI-357745,EBI-1056358
PDCLQ133716EBI-357745,EBI-5772890
PLEKHO1Q53GL010EBI-357745,EBI-949945
PSMC2P3599810EBI-357745,EBI-359710
PSMC4P4368613EBI-357745,EBI-743997
PSMC6P6233310EBI-357745,EBI-357669
PSMD2Q132009EBI-357745,EBI-357648
SKA1Q96BD83EBI-357745,EBI-741854

GO - Molecular functioni

  • TBP-class protein binding Source: GO_Central
  • thyrotropin-releasing hormone receptor binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111678. 212 interactors.
DIPiDIP-36645N.
IntActiP62195. 73 interactors.
MINTiMINT-5004394.
STRINGi9606.ENSP00000310572.

Structurei

Secondary structure

1406
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi322 – 333Combined sources12
Beta strandi336 – 338Combined sources3
Helixi344 – 349Combined sources6
Helixi356 – 372Combined sources17
Beta strandi376 – 378Combined sources3
Helixi380 – 391Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KRKNMR-A320-395[»]
3KW6X-ray2.10A318-395[»]
5GJQelectron microscopy4.50J1-406[»]
5GJRelectron microscopy3.50J/x1-406[»]
5L4Gelectron microscopy4.02J1-406[»]
5T0Celectron microscopy3.80AC/BC1-406[»]
5T0Gelectron microscopy4.40C9-406[»]
5T0Helectron microscopy6.80C9-406[»]
5T0Ielectron microscopy8.00C9-406[»]
5T0Jelectron microscopy8.00C9-406[»]
ProteinModelPortaliP62195.
SMRiP62195.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62195.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni186 – 406May mediate interaction with PRPF9By similarityAdd BLAST221

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiKOG0728. Eukaryota.
COG1222. LUCA.
GeneTreeiENSGT00550000074947.
HOGENOMiHOG000225143.
HOVERGENiHBG000109.
InParanoidiP62195.
KOiK03066.
OMAiNIKVIMC.
OrthoDBiEOG091G096W.
PhylomeDBiP62195.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P62195-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN
60 70 80 90 100
ELNAKVRLLR EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD
110 120 130 140 150
KNIDINDVTP NCRVALRNDS YTLHKILPNK VDPLVSLMMV EKVPDSTYEM
160 170 180 190 200
IGGLDKQIKE IKEVIELPVK HPELFEALGI AQPKGVLLYG PPGTGKTLLA
210 220 230 240 250
RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE HAPSIIFMDE
260 270 280 290 300
IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI
310 320 330 340 350
LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL
360 370 380 390 400
MPGASGAEVK GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS

IKKLWK
Length:406
Mass (Da):45,626
Last modified:June 21, 2004 - v1
Checksum:i29C6410C4A85A7F7
GO
Isoform 2 (identifier: P62195-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: Missing.

Show »
Length:398
Mass (Da):44,784
Checksum:i450BB51DA8C9381D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti61E → R in BAA07919 (PubMed:7729537).Curated1
Sequence conflicti127 – 128LP → ML in AAB88187 (PubMed:9110174).Curated2
Sequence conflicti266D → S in AAC41735 (PubMed:7776974).Curated1
Sequence conflicti272T → Q in AAC41735 (PubMed:7776974).Curated1
Sequence conflicti300I → M in AAC41735 (PubMed:7776974).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03590160R → Q in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_048119258R → W.Corresponds to variant rs11543211dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0454411 – 8Missing in isoform 2. 1 Publication8

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D44467 mRNA. Translation: BAA07919.1.
L38810 mRNA. Translation: AAC41735.1.
AK290758 mRNA. Translation: BAF83447.1.
AK291878 mRNA. Translation: BAF84567.1.
AC015651 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94270.1.
CH471109 Genomic DNA. Translation: EAW94271.1.
CH471109 Genomic DNA. Translation: EAW94272.1.
BC001932 mRNA. Translation: AAH01932.1.
BC002367 mRNA. Translation: AAH02367.3.
AF035309 mRNA. Translation: AAB88187.1.
CCDSiCCDS11645.1. [P62195-1]
CCDS56043.1. [P62195-2]
PIRiS60343.
S65536.
RefSeqiNP_001186092.1. NM_001199163.1. [P62195-2]
NP_002796.4. NM_002805.5. [P62195-1]
UniGeneiHs.79387.

Genome annotation databases

EnsembliENST00000310144; ENSP00000310572; ENSG00000087191. [P62195-1]
ENST00000375812; ENSP00000364970; ENSG00000087191. [P62195-2]
ENST00000580864; ENSP00000462495; ENSG00000087191. [P62195-2]
ENST00000581882; ENSP00000463938; ENSG00000087191. [P62195-2]
GeneIDi5705.
KEGGihsa:5705.
UCSCiuc002jcb.4. human. [P62195-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D44467 mRNA. Translation: BAA07919.1.
L38810 mRNA. Translation: AAC41735.1.
AK290758 mRNA. Translation: BAF83447.1.
AK291878 mRNA. Translation: BAF84567.1.
AC015651 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94270.1.
CH471109 Genomic DNA. Translation: EAW94271.1.
CH471109 Genomic DNA. Translation: EAW94272.1.
BC001932 mRNA. Translation: AAH01932.1.
BC002367 mRNA. Translation: AAH02367.3.
AF035309 mRNA. Translation: AAB88187.1.
CCDSiCCDS11645.1. [P62195-1]
CCDS56043.1. [P62195-2]
PIRiS60343.
S65536.
RefSeqiNP_001186092.1. NM_001199163.1. [P62195-2]
NP_002796.4. NM_002805.5. [P62195-1]
UniGeneiHs.79387.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KRKNMR-A320-395[»]
3KW6X-ray2.10A318-395[»]
5GJQelectron microscopy4.50J1-406[»]
5GJRelectron microscopy3.50J/x1-406[»]
5L4Gelectron microscopy4.02J1-406[»]
5T0Celectron microscopy3.80AC/BC1-406[»]
5T0Gelectron microscopy4.40C9-406[»]
5T0Helectron microscopy6.80C9-406[»]
5T0Ielectron microscopy8.00C9-406[»]
5T0Jelectron microscopy8.00C9-406[»]
ProteinModelPortaliP62195.
SMRiP62195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111678. 212 interactors.
DIPiDIP-36645N.
IntActiP62195. 73 interactors.
MINTiMINT-5004394.
STRINGi9606.ENSP00000310572.

PTM databases

iPTMnetiP62195.
PhosphoSitePlusiP62195.
SwissPalmiP62195.

Polymorphism and mutation databases

BioMutaiPSMC5.
DMDMi49065819.

Proteomic databases

EPDiP62195.
MaxQBiP62195.
PaxDbiP62195.
PeptideAtlasiP62195.
PRIDEiP62195.

Protocols and materials databases

DNASUi5705.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310144; ENSP00000310572; ENSG00000087191. [P62195-1]
ENST00000375812; ENSP00000364970; ENSG00000087191. [P62195-2]
ENST00000580864; ENSP00000462495; ENSG00000087191. [P62195-2]
ENST00000581882; ENSP00000463938; ENSG00000087191. [P62195-2]
GeneIDi5705.
KEGGihsa:5705.
UCSCiuc002jcb.4. human. [P62195-1]

Organism-specific databases

CTDi5705.
DisGeNETi5705.
GeneCardsiPSMC5.
HGNCiHGNC:9552. PSMC5.
HPAiHPA017871.
HPA064293.
MIMi601681. gene.
neXtProtiNX_P62195.
OpenTargetsiENSG00000087191.
PharmGKBiPA33897.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0728. Eukaryota.
COG1222. LUCA.
GeneTreeiENSGT00550000074947.
HOGENOMiHOG000225143.
HOVERGENiHBG000109.
InParanoidiP62195.
KOiK03066.
OMAiNIKVIMC.
OrthoDBiEOG091G096W.
PhylomeDBiP62195.

Enzyme and pathway databases

BioCyciZFISH:HS01562-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

ChiTaRSiPSMC5. human.
EvolutionaryTraceiP62195.
GeneWikiiPSMC5.
GenomeRNAii5705.
PROiP62195.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000087191.
CleanExiHS_PSMC5.
ExpressionAtlasiP62195. baseline and differential.
GenevisibleiP62195. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRS8_HUMAN
AccessioniPrimary (citable) accession number: P62195
Secondary accession number(s): A8K3Z3
, A8K763, O35051, O43208, P47210, P52915, P52916
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: November 30, 2016
This is version 138 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. 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.