Q99460 (PSMD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
26S proteasome non-ATPase regulatory subunit 1

Alternative name(s):
26S proteasome regulatory subunit RPN2
26S proteasome regulatory subunit S1
26S proteasome subunit p112

Gene names

Name:

PSMD1

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	953 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Subunit structure	Interacts with ADRM1. Ref.4 Ref.5
Sequence similarities	Belongs to the proteasome subunit S1 family. Contains 10 PC repeats.
Sequence caution	The sequence AAH01053.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH14013.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH39845.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH47897.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH64398.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH73833.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Cellular component	Proteasome
Coding sequence diversity	Alternative splicing
Domain	Repeat
PTM	Acetylation Phosphoprotein
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 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 protein catabolic process Inferred from electronic annotation. Source: InterPro 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
Molecular_function	enzyme regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q99460-1)

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: Q99460-2)

The sequence of this isoform differs from the canonical sequence as follows:
     797-827: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 953	953	26S proteasome non-ATPase regulatory subunit 1		PRO_0000173801
Regions
	Repeat	403 – 436	34	PC 1
	Repeat	441 – 474	34	PC 2
	Repeat	476 – 510	35	PC 3
	Repeat	511 – 545	35	PC 4
	Repeat	547 – 580	34	PC 5
	Repeat	581 – 616	36	PC 6
	Repeat	617 – 649	33	PC 7
	Repeat	651 – 685	35	PC 8
	Repeat	686 – 726	41	PC 9
	Repeat	729 – 761	33	PC 10
	Compositional bias	936 – 943	8	Poly-Glu
Amino acid modifications
	Modified residue	273	1	Phosphothreonine Ref.6
	Modified residue	290	1	Phosphoserine Ref.6
	Modified residue	310	1	N6-acetyllysine Ref.9
	Modified residue	311	1	Phosphothreonine Ref.6 Ref.7 Ref.8 Ref.12
	Modified residue	315	1	Phosphoserine Ref.6 Ref.7 Ref.8 Ref.12
Natural variations
	Alternative sequence	797 – 827	31	Missing in isoform 2.		VSP_011475
Experimental info
	Sequence conflict	85	1	G → R in BAA07918. Ref.1
	Sequence conflict	616	1	R → S in BAA07918. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 31, 2004. Version 2. Checksum: B8682146082D21FA	FASTA	953	105,836
	10 20 30 40 50 60 MITSAAGIIS LLDEDEPQLK EFALHKLNAV VNDFWAEISE SVDKIEVLYE DEGFRSRQFA 70 80 90 100 110 120 ALVASKVFYH LGAFEESLNY ALGAGDLFNV NDNSEYVETI IAKCIDHYTK QCVENADLPE 130 140 150 160 170 180 GEKKPIDQRL EGIVNKMFQR CLDDHKYKQA IGIALETRRL DVFEKTILES NDVPGMLAYS 190 200 210 220 230 240 LKLCMSLMQN KQFRNKVLRV LVKIYMNLEK PDFINVCQCL IFLDDPQAVS DILEKLVKED 250 260 270 280 290 300 NLLMAYQICF DLYESASQQF LSSVIQNLRT VGTPIASVPG STNTGTVPGS EKDSDSMETE 310 320 330 340 350 360 EKTSSAFVGK TPEASPEPKD QTLKMIKILS GEMAIELHLQ FLIRNNNTDL MILKNTKDAV 370 380 390 400 410 420 RNSVCHTATV IANSFMHCGT TSDQFLRDNL EWLARATNWA KFTATASLGV IHKGHEKEAL 430 440 450 460 470 480 QLMATYLPKD TSPGSAYQEG GGLYALGLIH ANHGGDIIDY LLNQLKNASN DIVRHGGSLG 490 500 510 520 530 540 LGLAAMGTAR QDVYDLLKTN LYQDDAVTGE AAGLALGLVM LGSKNAQAIE DMVGYAQETQ 550 560 570 580 590 600 HEKILRGLAV GIALVMYGRM EEADALIESL CRDKDPILRR SGMYTVAMAY CGSGNNKAIR 610 620 630 640 650 660 RLLHVAVSDV NDDVRRAAVE SLGFILFRTP EQCPSVVSLL SESYNPHVRY GAAMALGICC 670 680 690 700 710 720 AGTGNKEAIN LLEPMTNDPV NYVRQGALIA SALIMIQQTE ITCPKVNQFR QLYSKVINDK 730 740 750 760 770 780 HDDVMAKFGA ILAQGILDAG GHNVTISLQS RTGHTHMPSV VGVLVFTQFW FWFPLSHFLS 790 800 810 820 830 840 LAYTPTCVIG LNKDLKMPKV QYKSNCKPST FAYPAPLEVP KEKEKEKVST AVLSITAKAK 850 860 870 880 890 900 KKEKEKEKKE EEKMEVDEAE KKEEKEKKKE PEPNFQLLDN PARVMPAQLK VLTMPETCRY 910 920 930 940 950 QPFKPLSIGG IIILKDTSED IEELVEPVAA HGPKIEEEEQ EPEPPEPFEY IDD
	Isoform 2 [UniParc]. Checksum: 1F727659749D4871	FASTA	922	102,258
	10 20 30 40 50 60 MITSAAGIIS LLDEDEPQLK EFALHKLNAV VNDFWAEISE SVDKIEVLYE DEGFRSRQFA 70 80 90 100 110 120 ALVASKVFYH LGAFEESLNY ALGAGDLFNV NDNSEYVETI IAKCIDHYTK QCVENADLPE 130 140 150 160 170 180 GEKKPIDQRL EGIVNKMFQR CLDDHKYKQA IGIALETRRL DVFEKTILES NDVPGMLAYS 190 200 210 220 230 240 LKLCMSLMQN KQFRNKVLRV LVKIYMNLEK PDFINVCQCL IFLDDPQAVS DILEKLVKED 250 260 270 280 290 300 NLLMAYQICF DLYESASQQF LSSVIQNLRT VGTPIASVPG STNTGTVPGS EKDSDSMETE 310 320 330 340 350 360 EKTSSAFVGK TPEASPEPKD QTLKMIKILS GEMAIELHLQ FLIRNNNTDL MILKNTKDAV 370 380 390 400 410 420 RNSVCHTATV IANSFMHCGT TSDQFLRDNL EWLARATNWA KFTATASLGV IHKGHEKEAL 430 440 450 460 470 480 QLMATYLPKD TSPGSAYQEG GGLYALGLIH ANHGGDIIDY LLNQLKNASN DIVRHGGSLG 490 500 510 520 530 540 LGLAAMGTAR QDVYDLLKTN LYQDDAVTGE AAGLALGLVM LGSKNAQAIE DMVGYAQETQ 550 560 570 580 590 600 HEKILRGLAV GIALVMYGRM EEADALIESL CRDKDPILRR SGMYTVAMAY CGSGNNKAIR 610 620 630 640 650 660 RLLHVAVSDV NDDVRRAAVE SLGFILFRTP EQCPSVVSLL SESYNPHVRY GAAMALGICC 670 680 690 700 710 720 AGTGNKEAIN LLEPMTNDPV NYVRQGALIA SALIMIQQTE ITCPKVNQFR QLYSKVINDK 730 740 750 760 770 780 HDDVMAKFGA ILAQGILDAG GHNVTISLQS RTGHTHMPSV VGVLVFTQFW FWFPLSHFLS 790 800 810 820 830 840 LAYTPTCVIG LNKDLKVSTA VLSITAKAKK KEKEKEKKEE EKMEVDEAEK KEEKEKKKEP 850 860 870 880 890 900 EPNFQLLDNP ARVMPAQLKV LTMPETCRYQ PFKPLSIGGI IILKDTSEDI EELVEPVAAH 910 920 GPKIEEEEQE PEPPEPFEYI DD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3p." Yokota K., Kagawa S., Shimizu Y., Akioka H., Tsurumi C., Noda C., Fujimuro M., Yokosawa H., Fujiwara T., Takahashi E., Ohba M., Yamasaki M., DeMartino G.N., Slaughter C.A., Toh-e A., Tanaka K. Mol. Biol. Cell 7:853-870(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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] (ISOFORMS 1 AND 2). Tissue: Cervix, Liver, Lymph, Placenta, Testis and Uterus.
[4]	"A novel proteasome-interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes." Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K., Murata S. EMBO J. 25:4524-4536(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ADRM1.
[5]	"Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1." Yao T., Song L., Xu W., DeMartino G.N., Florens L., Swanson S.K., Washburn M.P., Conaway R.C., Conaway J.W., Cohen R.E. Nat. Cell Biol. 8:994-1002(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ADRM1.
[6]	"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 THR-273; SER-290; THR-311 AND SER-315, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"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 THR-311 AND SER-315, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[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-310, MASS SPECTROMETRY.
[10]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"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].
[12]	"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 THR-311 AND SER-315, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D44466 mRNA. Translation: BAA07918.1. AC009407 Genomic DNA. Translation: AAX93127.1. BC001053 mRNA. Translation: AAH01053.1. Sequence problems. BC014013 mRNA. Translation: AAH14013.1. Sequence problems. BC039845 mRNA. Translation: AAH39845.1. Sequence problems. BC047897 mRNA. Translation: AAH47897.1. Sequence problems. BC064398 mRNA. Translation: AAH64398.1. Sequence problems. BC073833 mRNA. Translation: AAH73833.1. Sequence problems. BC094720 mRNA. Translation: AAH94720.1. BC112344 mRNA. Translation: AAI12345.1. BC114434 mRNA. Translation: AAI14435.1.
IPI	IPI00299608. IPI00456695.
RefSeq	NP_001177966.1. NM_001191037.1. NP_002798.2. NM_002807.3.
UniGene	Hs.3887.
3D structure databases
ProteinModelPortal	Q99460.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27548N.
IntAct	Q99460. 19 interactions.
MINT	MINT-1160606.
PTM databases
PhosphoSite	Q99460.
Polymorphism databases
DMDM	51704332.
Proteomic databases
PaxDb	Q99460.
PRIDE	Q99460.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000308696; ENSP00000309474; ENSG00000173692. ENST00000373635; ENSP00000362738; ENSG00000173692. ENST00000409643; ENSP00000386932; ENSG00000173692.
GeneID	5707.
KEGG	hsa:5707.
UCSC	uc002vrm.2. human. uc002vrn.2. human.
Organism-specific databases
CTD	5707.
GeneCards	GC02P231921.
HGNC	HGNC:9554. PSMD1.
HPA	CAB021092.
neXtProt	NX_Q99460.
PharmGKB	PA33899.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5116.
HOVERGEN	HBG007543.
InParanoid	Q99460.
KO	K03032.
OMA	CVENAEL.
OrthoDB	EOG4X97GG.
PhylomeDB	Q99460.
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	Q99460.
Bgee	Q99460.
CleanEx	HS_PSMD1.
Genevestigator	Q99460.
GermOnline	ENSG00000173692. Homo sapiens.
Family and domain databases
Gene3D	1.25.10.10. 2 hits.
InterPro	IPR016642. 26S_Psome_Rpn2. IPR002015. APC_proteasome. IPR011989. ARM-like. IPR016024. ARM-type_fold. [Graphical view]
Pfam	PF01851. PC_rep. 3 hits. [Graphical view]
PIRSF	PIRSF015947. 26S_Psome_Rpn2. 1 hit.
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
ProtoNet	Search...
Other
ChEMBL	CHEMBL1934.
ChiTaRS	PSMD1. human.
DrugBank	DB00188. Bortezomib.
GenomeRNAi	5707.
NextBio	22174.

Entry information

Entry name

PSMD1_HUMAN

Accession

Primary (citable) accession number: Q99460
Secondary accession number(s): B8ZZH9 , Q24JU0, Q53TI2, Q6GMU5, Q6P2P4, Q6PJM7, Q6PKG9, Q86VU1, Q8IV79

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 31, 2004
Last modified:	May 1, 2013
This is version 121 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.