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P55036

- PSMD4_HUMAN

UniProt

P55036 - PSMD4_HUMAN

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Protein

26S proteasome non-ATPase regulatory subunit 4

Gene

PSMD4

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

Functioni

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

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

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

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.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PSMD4
Synonyms:MCB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9561. PSMD4.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
  5. proteasome accessory complex Source: UniProtKB
  6. proteasome complex Source: UniProtKB
  7. proteasome regulatory particle, base subcomplex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33907.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 37737726S proteasome non-ATPase regulatory subunit 4PRO_0000173828Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei250 – 2501PhosphothreonineBy similarity
Modified residuei266 – 2661Phosphoserine4 Publications
Modified residuei358 – 3581Phosphoserine1 Publication
Modified residuei361 – 3611Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP55036.
PaxDbiP55036.
PRIDEiP55036.

PTM databases

PhosphoSiteiP55036.

Expressioni

Gene expression databases

BgeeiP55036.
CleanExiHS_PSMD4.
ExpressionAtlasiP55036. baseline and differential.
GenevestigatoriP55036.

Organism-specific databases

HPAiCAB047300.
HPA038807.
HPA039252.

Interactioni

Subunit structurei

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-359318,EBI-359318
ADRM1Q161862EBI-359318,EBI-954387
DSK2P485102EBI-359318,EBI-6174From a different organism.
DSK2BQ9SII83EBI-359318,EBI-4433040From a different organism.
Pax3P246103EBI-359318,EBI-1208116From a different organism.
PSMD2Q132003EBI-359318,EBI-357648
RAD23AP547253EBI-359318,EBI-746453
RAD23AQ84L323EBI-359318,EBI-6394924From a different organism.
RAD23BP5472712EBI-359318,EBI-954531
Rbck1Q629213EBI-359318,EBI-7266339From a different organism.
SCHIP1Q9P0W52EBI-359318,EBI-1397509
UBCP0CG488EBI-359318,EBI-3390054
UBQLN1Q9UMX06EBI-359318,EBI-741480
UBQLN2Q9UHD93EBI-359318,EBI-947187
UCHL5Q9Y5K55EBI-359318,EBI-1051183

Protein-protein interaction databases

BioGridi111683. 290 interactions.
DIPiDIP-38189N.
IntActiP55036. 60 interactions.
MINTiMINT-105366.
STRINGi9606.ENSP00000357879.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi201 – 2033Combined sources
Beta strandi205 – 2084Combined sources
Helixi210 – 2123Combined sources
Helixi214 – 24431Combined sources
Beta strandi245 – 2495Combined sources
Beta strandi268 – 2703Combined sources
Beta strandi273 – 2753Combined sources
Helixi278 – 29417Combined sources
Beta strandi296 – 3005Combined sources
Beta strandi302 – 3043Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P9CNMR-A263-307[»]
1P9DNMR-S263-307[»]
1UELNMR-B263-307[»]
1YX4NMR-A196-306[»]
1YX5NMR-A192-306[»]
1YX6NMR-A196-306[»]
2KDENMR-A196-306[»]
2KDFNMR-A196-306[»]
ProteinModelPortaliP55036.
SMRiP55036. Positions 1-306.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55036.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 188184VWFAPROSITE-ProRule annotationAdd
BLAST
Repeati211 – 23020UIM 1Add
BLAST
Repeati282 – 30120UIM 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni216 – 2205Essential for ubiquitin-binding
Regioni287 – 2915Essential for ubiquitin-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi238 – 2469Poly-Ala

Domaini

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

Sequence similaritiesi

Belongs to the proteasome subunit S5A family.Curated
Contains 2 UIM (ubiquitin-interacting motif) repeats.PROSITE-ProRule annotation
Contains 1 VWFA domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5148.
GeneTreeiENSGT00530000064050.
HOGENOMiHOG000165630.
HOVERGENiHBG000425.
InParanoidiP55036.
KOiK03029.
OrthoDBiEOG70W3DM.
PhylomeDBiP55036.
TreeFamiTF106232.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR027040. Proteasome_su_Rpn10.
IPR003903. Ubiquitin-int_motif.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR10223. PTHR10223. 1 hit.
PfamiPF02809. UIM. 2 hits.
[Graphical view]
SMARTiSM00726. UIM. 2 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
PROSITEiPS50330. UIM. 2 hits.
PS50234. VWFA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform Rpn10A (identifier: P55036-1) [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
MVLESTMVCV DNSEYMRNGD FLPTRLQAQQ DAVNIVCHSK TRSNPENNVG
60 70 80 90 100
LITLANDCEV LTTLTPDTGR ILSKLHTVQP KGKITFCTGI RVAHLALKHR
110 120 130 140 150
QGKNHKMRII AFVGSPVEDN EKDLVKLAKR LKKEKVNVDI INFGEEEVNT
160 170 180 190 200
EKLTAFVNTL NGKDGTGSHL VTVPPGPSLA DALISSPILA GEGGAMLGLG
210 220 230 240 250
ASDFEFGVDP SADPELALAL RVSMEEQRQR QEEEARRAAA ASAAEAGIAT
260 270 280 290 300
TGTEDSDDAL LKMTISQQEF GRTGLPDLSS MTEEEQIAYA MQMSLQGAEF
310 320 330 340 350
GQAESADIDA SSAMDTSEPA KEEDDYDVMQ DPEFLQSVLE NLPGVDPNNE
360 370
AIRNAMGSLA SQATKDGKKD KKEEDKK
Length:377
Mass (Da):40,737
Last modified:October 1, 1996 - v1
Checksum:iEC712EC4DB1CE9AB
GO
Isoform Rpn10E (identifier: P55036-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:268
Mass (Da):28,612
Checksum:i6640BF4CD5C91C6E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei255 – 26814DSDDA…TISQQ → GERGGIRSPGTAGC in isoform Rpn10E. CuratedVSP_005291Add
BLAST
Alternative sequencei269 – 377109Missing in isoform Rpn10E. CuratedVSP_005292Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS991.1. [P55036-1]
PIRiS63671.
RefSeqiNP_002801.1. NM_002810.2. [P55036-1]
UniGeneiHs.505059.

Genome annotation databases

EnsembliENST00000368884; ENSP00000357879; ENSG00000159352. [P55036-1]
GeneIDi5710.
KEGGihsa:5710.
UCSCiuc001exl.3. human. [P55036-1]

Polymorphism databases

DMDMi1709796.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS991.1. [P55036-1 ]
PIRi S63671.
RefSeqi NP_002801.1. NM_002810.2. [P55036-1 ]
UniGenei Hs.505059.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1P9C NMR - A 263-307 [» ]
1P9D NMR - S 263-307 [» ]
1UEL NMR - B 263-307 [» ]
1YX4 NMR - A 196-306 [» ]
1YX5 NMR - A 192-306 [» ]
1YX6 NMR - A 196-306 [» ]
2KDE NMR - A 196-306 [» ]
2KDF NMR - A 196-306 [» ]
ProteinModelPortali P55036.
SMRi P55036. Positions 1-306.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111683. 290 interactions.
DIPi DIP-38189N.
IntActi P55036. 60 interactions.
MINTi MINT-105366.
STRINGi 9606.ENSP00000357879.

PTM databases

PhosphoSitei P55036.

Polymorphism databases

DMDMi 1709796.

Proteomic databases

MaxQBi P55036.
PaxDbi P55036.
PRIDEi P55036.

Protocols and materials databases

DNASUi 5710.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368884 ; ENSP00000357879 ; ENSG00000159352 . [P55036-1 ]
GeneIDi 5710.
KEGGi hsa:5710.
UCSCi uc001exl.3. human. [P55036-1 ]

Organism-specific databases

CTDi 5710.
GeneCardsi GC01P151227.
HGNCi HGNC:9561. PSMD4.
HPAi CAB047300.
HPA038807.
HPA039252.
MIMi 601648. gene.
neXtProti NX_P55036.
PharmGKBi PA33907.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5148.
GeneTreei ENSGT00530000064050.
HOGENOMi HOG000165630.
HOVERGENi HBG000425.
InParanoidi P55036.
KOi K03029.
OrthoDBi EOG70W3DM.
PhylomeDBi P55036.
TreeFami TF106232.

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 PSMD4. human.
EvolutionaryTracei P55036.
GeneWikii PSMD4.
GenomeRNAii 5710.
NextBioi 22186.
PROi P55036.
SOURCEi Search...

Gene expression databases

Bgeei P55036.
CleanExi HS_PSMD4.
ExpressionAtlasi P55036. baseline and differential.
Genevestigatori P55036.

Family and domain databases

Gene3Di 3.40.50.410. 1 hit.
InterProi IPR027040. Proteasome_su_Rpn10.
IPR003903. Ubiquitin-int_motif.
IPR002035. VWF_A.
[Graphical view ]
PANTHERi PTHR10223. PTHR10223. 1 hit.
Pfami PF02809. UIM. 2 hits.
[Graphical view ]
SMARTi SM00726. UIM. 2 hits.
SM00327. VWA. 1 hit.
[Graphical view ]
SUPFAMi SSF53300. SSF53300. 1 hit.
PROSITEi PS50330. UIM. 2 hits.
PS50234. VWFA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  17. 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. 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. 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.

Entry informationi

Entry nameiPSMD4_HUMAN
AccessioniPrimary (citable) accession number: P55036
Secondary accession number(s): D3DV16, Q5VWC5, Q9NS92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 150 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, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3