Q9UNM6 (PSD13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Proteasome
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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 M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle 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, TAP-dependent Traceable author statement. Source: Reactome apoptotic 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: Compara 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 small molecule metabolic process Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 376	376	26S proteasome non-ATPase regulatory subunit 13		PRO_0000173867
Regions
	Domain	239 – 335	97	PCI
Amino acid modifications
	Modified residue	298	1	N6-acetyllysine Ref.9
Natural variations
	Alternative sequence	32 – 69	38	KLWHQ…SEFEH → NFMKTLSVNLNTGKSLSSVF HFENECIDARRCSKAGGFYF in isoform 2.		VSP_041067
	Natural variant	13	1	N → S. Ref.2 Ref.3 Ref.4 Ref.7 Ref.8 Ref.11 Corresponds to variant rs1045288 [ dbSNP | Ensembl ].		VAR_024591
	Natural variant	150	1	S → L. Corresponds to variant rs28927679 [ dbSNP | Ensembl ].		VAR_057050
	Natural variant	204	1	G → E. Corresponds to variant rs1794108 [ dbSNP | Ensembl ].		VAR_031094
	Natural variant	205	1	L → F. Corresponds to variant rs1794109 [ dbSNP | Ensembl ].		VAR_031095
Experimental info
	Sequence conflict	253	1	T → I in AAC64104. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2011. Version 2. Checksum: E96C99A49CAC5ED3	FASTA	376	42,945
	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
	Isoform 2 [UniParc]. Checksum: 1826DB496A31D7BB	FASTA	378	42,942
	10 20 30 40 50 60 MKDVPGFLQQ SQNSGPGQPA VWHRLEELYT KNFMKTLSVN LNTGKSLSSV FHFENECIDA 70 80 90 100 110 120 RRCSKAGGFY FRVNPLSLVE IILHVVRQMT DPNVALTFLE KTREKVKSSD EAVILCKTAI 130 140 150 160 170 180 GALKLNIGDL QVTKETIEDV EEMLNNLPGV TSVHSRFYDL SSKYYQTIGN HASYYKDALR 190 200 210 220 230 240 FLGCVDIKDL PVSEQQERAF TLGLAGLLGE GVFNFGELLM HPVLESLRNT DRQWLIDTLY 250 260 270 280 290 300 AFNSGNVERF QTLKTAWGQQ PDLAANEAQL LRKIQLLCLM EMTFTRPANH RQLTFEEIAK 310 320 330 340 350 360 SAKITVNEVE LLVMKALSVG LVKGSIDEVD KRVHMTWVQP RVLDLQQIKG MKDRLEFWCT 370 DVKSMEMLVE HQAHDILT

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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.
IPI	IPI00375380. IPI00549672.
RefSeq	NP_002808.3. NM_002817.3. NP_787128.2. NM_175932.2.
UniGene	Hs.134688.
3D structure databases
ProteinModelPortal	Q9UNM6.
SMR	Q9UNM6. Positions 16-331.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27576N.
IntAct	Q9UNM6. 7 interactions.
MINT	MINT-1161305.
STRING	9606.ENSP00000396937.
PTM databases
PhosphoSite	Q9UNM6.
Polymorphism databases
DMDM	20978558.
Proteomic databases
PaxDb	Q9UNM6.
PRIDE	Q9UNM6.
Protocols and materials databases
DNASU	5719.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000431206; ENSP00000396937; ENSG00000185627. ENST00000532097; ENSP00000436186; ENSG00000185627.
GeneID	5719.
KEGG	hsa:5719.
UCSC	uc001lol.2. human. uc001loo.2. human.
Organism-specific databases
CTD	5719.
GeneCards	GC11P000226.
H-InvDB	HIX0009340.
HGNC	HGNC:9558. PSMD13.
HPA	HPA038692.
MIM	603481. gene.
neXtProt	NX_Q9UNM6.
PharmGKB	PA33904.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG272621.
HOGENOM	HOG000216633.
HOVERGEN	HBG053740.
InParanoid	Q9UNM6.
KO	K03039.
OMA	INQVEQV.
OrthoDB	EOG42JNRJ.
PhylomeDB	Q9UNM6.
Enzyme and pathway databases
Reactome	REACT_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
ArrayExpress	Q9UNM6.
Bgee	Q9UNM6.
CleanEx	HS_PSMD13.
Genevestigator	Q9UNM6.
GermOnline	ENSG00000185627. Homo sapiens.
Family and domain databases
InterPro	IPR000717. PCI_dom. [Graphical view]
Pfam	PF01399. PCI. 1 hit. [Graphical view]
SMART	SM00088. PINT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PSMD13. human.
GenomeRNAi	5719.
NextBio	22226.
SOURCE	Search...

Entry information

Entry name

PSD13_HUMAN

Accession

Primary (citable) accession number: Q9UNM6
Secondary accession number(s): B3KT15 , O75831, Q53XU2, Q9UNV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2002
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.