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Q9UNM6 (PSD13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
26S proteasome non-ATPase regulatory subunit 13
Alternative name(s):
26S proteasome regulatory subunit RPN9
26S proteasome regulatory subunit S11
26S proteasome regulatory subunit p40.5
Gene names
Name:PSMD13
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.

Subunit structure

Component of the PA700 complex.

Sequence similarities

Belongs to the proteasome subunit S11 family.

Contains 1 PCI domain.

Ontologies

Keywords
   Cellular componentProteasome
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMAcetylation
   Technical termComplete proteome
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

meiosis I

Inferred from electronic annotation. Source: Ensembl

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_componentcytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

proteasome accessory complex

Inferred from sequence or structural similarity. Source: UniProtKB

proteasome complex

Traceable author statement PubMed 8811196. Source: ProtInc

proteasome regulatory particle

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UNM6-1)

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 2 (identifier: Q9UNM6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     32-69: KLWHQLTLQV...YENFISEFEH → NFMKTLSVNL...RCSKAGGFYF

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 37637626S proteasome non-ATPase regulatory subunit 13
PRO_0000173867

Regions

Domain239 – 33597PCI

Amino acid modifications

Modified residue2981N6-acetyllysine Ref.9

Natural variations

Alternative sequence32 – 6938KLWHQ…SEFEH → NFMKTLSVNLNTGKSLSSVF HFENECIDARRCSKAGGFYF in isoform 2.
VSP_041067
Natural variant131N → S. Ref.2 Ref.3 Ref.4 Ref.7 Ref.8 Ref.11
Corresponds to variant rs1045288 [ dbSNP | Ensembl ].
VAR_024591
Natural variant1501S → L.
Corresponds to variant rs28927679 [ dbSNP | Ensembl ].
VAR_057050
Natural variant2041G → E.
Corresponds to variant rs1794108 [ dbSNP | Ensembl ].
VAR_031094
Natural variant2051L → F.
Corresponds to variant rs1794109 [ dbSNP | Ensembl ].
VAR_031095

Experimental info

Sequence conflict2531T → I in AAC64104. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: E96C99A49CAC5ED3

FASTA37642,945
        10         20         30         40         50         60 
MKDVPGFLQQ SQNSGPGQPA VWHRLEELYT KKLWHQLTLQ VLDFVQDPCF AQGDGLIKLY 

        70         80         90        100        110        120 
ENFISEFEHR VNPLSLVEII LHVVRQMTDP NVALTFLEKT REKVKSSDEA VILCKTAIGA 

       130        140        150        160        170        180 
LKLNIGDLQV TKETIEDVEE MLNNLPGVTS VHSRFYDLSS KYYQTIGNHA SYYKDALRFL 

       190        200        210        220        230        240 
GCVDIKDLPV SEQQERAFTL GLAGLLGEGV FNFGELLMHP VLESLRNTDR QWLIDTLYAF 

       250        260        270        280        290        300 
NSGNVERFQT LKTAWGQQPD LAANEAQLLR KIQLLCLMEM TFTRPANHRQ LTFEEIAKSA 

       310        320        330        340        350        360 
KITVNEVELL VMKALSVGLV KGSIDEVDKR VHMTWVQPRV LDLQQIKGMK DRLEFWCTDV 

       370 
KSMEMLVEHQ AHDILT 

« Hide

Isoform 2 [UniParc].

Checksum: 1826DB496A31D7BB
Show »

FASTA37842,942

References

« Hide 'large scale' references
[1]"cDNA cloning and functional analysis of p28 (Nas6p) and p40.5 (Nas7p), two novel regulatory subunits of the 26S proteasome."
Hori T., Kato S., Saeki M., DeMartino G.N., Slaughter C.A., Takeuchi J., Toh-e A., Tanaka K.
Gene 216:113-122(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning of the human 26S proteasome subunit p40.5."
Ting M.C., Chang L.Y.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-13.
Tissue: Liver.
[3]"Identification, molecular cloning, and characterization of subunit 11 of the human 26S proteasome."
Hoffman L., Gorbea C., Rechsteiner M.
FEBS Lett. 449:88-92(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-13.
[4]"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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-13.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-13.
[8]"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], VARIANT SER-13.
Tissue: Kidney and Lung.
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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].
[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: VARIANT [LARGE SCALE ANALYSIS] SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB009398 mRNA. Translation: BAA33214.1.
AF107837 mRNA. Translation: AAD43442.1.
AF086708 mRNA. Translation: AAC64104.1.
BT007307 mRNA. Translation: AAP35971.1.
AK094775 mRNA. Translation: BAG52927.1.
AC136475 Genomic DNA. No translation available.
CH471278 Genomic DNA. Translation: EAW61234.1.
BC001100 mRNA. Translation: AAH01100.1.
BC001747 mRNA. Translation: AAH01747.1.
CCDSCCDS44504.1. [Q9UNM6-2]
CCDS7692.1. [Q9UNM6-1]
RefSeqNP_002808.3. NM_002817.3. [Q9UNM6-1]
NP_787128.2. NM_175932.2. [Q9UNM6-2]
UniGeneHs.134688.

3D structure databases

ProteinModelPortalQ9UNM6.
SMRQ9UNM6. Positions 16-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111691. 76 interactions.
DIPDIP-27576N.
IntActQ9UNM6. 12 interactions.
MINTMINT-1161305.
STRING9606.ENSP00000396937.

PTM databases

PhosphoSiteQ9UNM6.

Polymorphism databases

DMDM317373273.

Proteomic databases

MaxQBQ9UNM6.
PaxDbQ9UNM6.
PRIDEQ9UNM6.

Protocols and materials databases

DNASU5719.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000431206; ENSP00000396937; ENSG00000185627. [Q9UNM6-2]
ENST00000532097; ENSP00000436186; ENSG00000185627. [Q9UNM6-1]
GeneID5719.
KEGGhsa:5719.
UCSCuc001lol.2. human. [Q9UNM6-1]
uc001loo.2. human. [Q9UNM6-2]

Organism-specific databases

CTD5719.
GeneCardsGC11P000226.
H-InvDBHIX0009340.
HGNCHGNC:9558. PSMD13.
HPAHPA038692.
MIM603481. gene.
neXtProtNX_Q9UNM6.
PharmGKBPA33904.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG272621.
HOGENOMHOG000216633.
HOVERGENHBG053740.
InParanoidQ9UNM6.
KOK03039.
OMAFNSGDVE.
OrthoDBEOG7C5M8X.
PhylomeDBQ9UNM6.
TreeFamTF105612.

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

ArrayExpressQ9UNM6.
BgeeQ9UNM6.
CleanExHS_PSMD13.
GenevestigatorQ9UNM6.

Family and domain databases

InterProIPR000717. PCI_dom.
[Graphical view]
PfamPF01399. PCI. 1 hit.
[Graphical view]
SMARTSM00088. PINT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPSMD13. human.
GeneWikiPSMD13.
GenomeRNAi5719.
NextBio22226.
PROQ9UNM6.
SOURCESearch...

Entry information

Entry namePSD13_HUMAN
AccessionPrimary (citable) accession number: Q9UNM6
Secondary accession number(s): B3KT15 expand/collapse secondary AC list , O75831, Q53XU2, Q9UNV3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 123 of the entry and version 2 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM