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P55036 (PSMD4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
26S proteasome non-ATPase regulatory subunit 4
Alternative name(s):
26S proteasome regulatory subunit RPN10
26S proteasome regulatory subunit S5A
Antisecretory factor 1
Short name=AF
Short name=ASF
Multiubiquitin chain-binding protein
Gene names
Name:PSMD4
Synonyms:MCB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds and presumably selects ubiquitin-conjugates for destruction. Displays selectivity for longer polyubiquitin chains. Modulates intestinal fluid secretion.

Subunit structure

The 26S proteasome is composed of a core protease, known as the 20S proteasome, capped at one or both ends by the 19S regulatory complex (RC). The RC is composed of at least 18 different subunits in two subcomplexes, the base and the lid, which form the portions proximal and distal to the 20S proteolytic core, respectively. Directly interacts with NUB1. Interacts with SQSTM1. Interacts with UBQLN4. Interacts with UBE3A. Ref.11 Ref.13 Ref.14 Ref.21

Domain

The 2 UIM motifs are involved in the binding to a multi-ubiquitin chain in a cooperative way. Ref.23 Ref.24

Sequence similarities

Belongs to the proteasome subunit S5A family.

Contains 2 UIM (ubiquitin-interacting motif) repeats.

Contains 1 VWFA domain.

Ontologies

Keywords
   Cellular componentProteasome
   Coding sequence diversityAlternative splicing
   DomainRepeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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

RNA metabolic process

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

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Traceable author statement. Source: Reactome

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

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

proteasome accessory complex

Inferred from sequence or structural similarity. Source: UniProtKB

proteasome complex

Traceable author statement PubMed 8811196. Source: ProtInc

proteasome regulatory particle, base subcomplex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 16990800PubMed 19931242. Source: IntAct

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform Rpn10A (identifier: P55036-1)

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 Rpn10E (identifier: P55036-2)

The sequence of this isoform differs from the canonical sequence as follows:
     255-268: DSDDALLKMTISQQ → GERGGIRSPGTAGC
     269-377: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 37737726S proteasome non-ATPase regulatory subunit 4
PRO_0000173828

Regions

Domain5 – 188184VWFA
Repeat211 – 23020UIM 1
Repeat282 – 30120UIM 2
Region216 – 2205Essential for ubiquitin-binding
Region287 – 2915Essential for ubiquitin-binding
Compositional bias238 – 2469Poly-Ala

Amino acid modifications

Modified residue2501Phosphothreonine By similarity
Modified residue2661Phosphoserine Ref.16 Ref.17 Ref.18 Ref.20
Modified residue3581Phosphoserine Ref.15
Modified residue3611Phosphoserine Ref.15

Natural variations

Alternative sequence255 – 26814DSDDA…TISQQ → GERGGIRSPGTAGC in isoform Rpn10E.
VSP_005291
Alternative sequence269 – 377109Missing in isoform Rpn10E.
VSP_005292

Secondary structure

.................... 377
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Rpn10A [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: EC712EC4DB1CE9AB

FASTA37740,737
        10         20         30         40         50         60 
MVLESTMVCV DNSEYMRNGD FLPTRLQAQQ DAVNIVCHSK TRSNPENNVG LITLANDCEV 

        70         80         90        100        110        120 
LTTLTPDTGR ILSKLHTVQP KGKITFCTGI RVAHLALKHR QGKNHKMRII AFVGSPVEDN 

       130        140        150        160        170        180 
EKDLVKLAKR LKKEKVNVDI INFGEEEVNT EKLTAFVNTL NGKDGTGSHL VTVPPGPSLA 

       190        200        210        220        230        240 
DALISSPILA GEGGAMLGLG ASDFEFGVDP SADPELALAL RVSMEEQRQR QEEEARRAAA 

       250        260        270        280        290        300 
ASAAEAGIAT TGTEDSDDAL LKMTISQQEF GRTGLPDLSS MTEEEQIAYA MQMSLQGAEF 

       310        320        330        340        350        360 
GQAESADIDA SSAMDTSEPA KEEDDYDVMQ DPEFLQSVLE NLPGVDPNNE AIRNAMGSLA 

       370 
SQATKDGKKD KKEEDKK 

« Hide

Isoform Rpn10E [UniParc].

Checksum: 6640BF4CD5C91C6E
Show »

FASTA26828,612

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of a pituitary gland protein modulating intestinal fluid secretion."
Johansson E., Loennroth I., Lange S., Jonson I., Jennische E., Loennroth C.
J. Biol. Chem. 270:20615-20620(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 63-75 AND 130-140.
Tissue: Pituitary.
[2]Loennroth I.
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Molecular cloning and expression of a multiubiquitin chain binding subunit of the human 26S protease."
Ferrell K., Deveraux Q., van Nocker S., Rechsteiner M.
FEBS Lett. 381:143-148(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[4]"Developmentally regulated, alternative splicing of the Rpn10 gene generates multiple forms of 26S proteasomes."
Kawahara H., Kasahara M., Nishiyama A., Ohsumi K., Goto T., Kishimoto T., Saeki Y., Yokosawa H., Shimbara N., Murata S., Chiba T., Suzuki K., Tanaka K.
EMBO J. 19:4144-4153(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
Tissue: Fetal brain.
[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. expand/collapse author list , 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. expand/collapse author list , 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].
[7]"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: Liver and Lung.
[8]"Proteolysis of presenilin 1 is associated with the 26S proteasome and is altered in Alzheimer's disease."
Fraser P.E., Levesque G., Rogaeva E.A., Yu G., St George-Hyslop P.H.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 70-377.
Tissue: Brain.
[9]"Purification and characterization of the antisecretory factor: a protein in the central nervous system and in the gut which inhibits intestinal hypersecretion induced by cholera toxin."
Loennroth I., Lange S.
Biochim. Biophys. Acta 883:138-144(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[10]"Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a."
Young P., Deveraux Q., Beal R.E., Pickart C.M., Rechsteiner M.
J. Biol. Chem. 273:5461-5467(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYUBIQUITIN BINDING SITES.
[11]"Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1."
Kamitani T., Kito K., Fukuda-Kamitani T., Yeh E.T.H.
J. Biol. Chem. 276:46655-46660(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NUB1.
[12]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[13]"The effects of the polyglutamine repeat protein ataxin-1 on the UbL-UBA protein A1Up."
Riley B.E., Xu Y., Zoghbi H.Y., Orr H.T.
J. Biol. Chem. 279:42290-42301(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBQLN4.
[14]"Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation."
Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R., Wooten M.W.
Mol. Cell. Biol. 24:8055-8068(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1.
[15]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[16]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Identification and proteomic analysis of distinct UBE3A/E6AP protein complexes."
Martinez-Noel G., Galligan J.T., Sowa M.E., Arndt V., Overton T.M., Harper J.W., Howley P.M.
Mol. Cell. Biol. 32:3095-3106(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBE3A.
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Structural determinants for the binding of ubiquitin-like domains to the proteasome."
Mueller T.D., Feigon J.
EMBO J. 22:4634-4645(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 263-306 IN COMPLEX WITH HR23A UBIQUITIN-LIKE DOMAIN.
[24]"Structure of the ubiquitin-interacting motif of S5a bound to the ubiquitin-like domain of HR23B."
Fujiwara K., Tenno T., Sugasawa K., Jee J.-G., Ohki I., Kojima C., Tochio H., Hiroaki H., Hanaoka F., Shirakawa M.
J. Biol. Chem. 279:4760-4767(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 260-307 IN COMPLEX WITH HR23B UBIQUITIN-LIKE DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U51007 mRNA. Translation: AAC50433.1.
U24704 mRNA. Translation: AAB54057.1.
AB033605 mRNA. Translation: BAA97581.1.
AL391069, AL592424 Genomic DNA. Translation: CAH70329.1.
AL592424, AL391069 Genomic DNA. Translation: CAI16390.1.
CH471121 Genomic DNA. Translation: EAW53457.1.
CH471121 Genomic DNA. Translation: EAW53458.1.
BC002365 mRNA. Translation: AAH02365.1.
BC072008 mRNA. Translation: AAH72008.1.
U72664 mRNA. Translation: AAB68598.1.
PIRS63671.
RefSeqNP_002801.1. NM_002810.2.
UniGeneHs.505059.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P9CNMR-A263-307[»]
1P9DNMR-S263-307[»]
1UELNMR-B263-307[»]
1YX4NMR-A196-306[»]
1YX5NMR-A196-306[»]
1YX6NMR-A196-306[»]
2KDENMR-A196-306[»]
2KDFNMR-A196-306[»]
ProteinModelPortalP55036.
SMRP55036. Positions 1-193, 196-306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111683. 287 interactions.
DIPDIP-38189N.
IntActP55036. 59 interactions.
MINTMINT-105366.
STRING9606.ENSP00000357879.

PTM databases

PhosphoSiteP55036.

Polymorphism databases

DMDM1709796.

Proteomic databases

PaxDbP55036.
PRIDEP55036.

Protocols and materials databases

DNASU5710.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368884; ENSP00000357879; ENSG00000159352. [P55036-1]
GeneID5710.
KEGGhsa:5710.
UCSCuc001exl.3. human. [P55036-1]

Organism-specific databases

CTD5710.
GeneCardsGC01P151227.
HGNCHGNC:9561. PSMD4.
HPACAB047300.
HPA038807.
HPA039252.
MIM601648. gene.
neXtProtNX_P55036.
PharmGKBPA33907.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5148.
HOGENOMHOG000165630.
HOVERGENHBG000425.
KOK03029.
OrthoDBEOG70W3DM.
PhylomeDBP55036.
TreeFamTF106232.

Enzyme and pathway databases

ReactomeREACT_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

ArrayExpressP55036.
BgeeP55036.
CleanExHS_PSMD4.
GenevestigatorP55036.

Family and domain databases

Gene3D3.40.50.410. 1 hit.
InterProIPR027040. Proteasome_su_Rpn10.
IPR003903. Ubiquitin-int_motif.
IPR002035. VWF_A.
[Graphical view]
PANTHERPTHR10223. PTHR10223. 1 hit.
PfamPF02809. UIM. 2 hits.
[Graphical view]
SMARTSM00726. UIM. 2 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF53300. SSF53300. 1 hit.
PROSITEPS50330. UIM. 2 hits.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPSMD4. human.
EvolutionaryTraceP55036.
GeneWikiPSMD4.
GenomeRNAi5710.
NextBio22186.
PROP55036.
SOURCESearch...

Entry information

Entry namePSMD4_HUMAN
AccessionPrimary (citable) accession number: P55036
Secondary accession number(s): D3DV16, Q5VWC5, Q9NS92
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM