Reviewed, UniProtKB/Swiss-Prot Q99460 (PSMD1_HUMAN)

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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	953 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.6 Ref.8
Sequence similarities	Belongs to the proteasome subunit S1 family. Contains 10 PC repeats.
Sequence caution	The sequence AAH01053.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence. The sequence AAH14013.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence. The sequence AAH39845.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence. The sequence AAH47897.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence. The sequence AAH64398.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence. The sequence AAH73833.1 differs from that shown. Reason: Miscellaneous discrepancy. 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
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome regulation of protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-KW proteasome regulatory particle Ref.1 Traceable author statement. Source: ProtInc
Molecular function	enzyme regulator activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HLA-B	P30480	1	EBI-357874,EBI-1054175
PAAF1	Q9BRP4	1	EBI-357874,EBI-1056358
PSMC4	P43686	1	EBI-357874,EBI-743997
PSMD10	O75832	1	EBI-357874,EBI-752185
PSMD6	Q15008	1	EBI-357874,EBI-359701

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	1	1	N-acetylmethionine; partial Ref.9
	Modified residue	49	1	Phosphotyrosine Ref.5
	Modified residue	273	1	Phosphothreonine Ref.4 Ref.10
	Modified residue	296	1	Phosphoserine Ref.10
	Modified residue	311	1	Phosphothreonine Ref.9 Ref.4 Ref.10 Ref.7
	Modified residue	315	1	Phosphoserine Ref.9 Ref.4 Ref.10 Ref.7
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. 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: 8816993] [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: 15815621] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Cervix, Liver, Lymph, Placenta, Testis and Uterus.
[4]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273; THR-311 AND SER-315, MASS SPECTROMETRY. Tissue: Epithelium.
[5]	"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC." Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J. Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-49, MASS SPECTROMETRY. Tissue: Hepatocyte.
[6]	"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: 16990800] [Abstract] Cited for: INTERACTION WITH ADRM1.
[7]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"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: 16906146] [Abstract] Cited for: INTERACTION WITH ADRM1.
[9]	"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: 17323924] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, ACETYLATION AT MET-1, MASS SPECTROMETRY.
[10]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273; SER-296; THR-311 AND SER-315, MASS SPECTROMETRY.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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_002798.2.
UniGene	Hs.3887
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:27548N.
IntAct	Q99460. 17 interactions.
PTM databases
PhosphoSite	Q99460.
Proteomic databases
PRIDE	Q99460.
Genome annotation databases
Ensembl	ENSG00000173692. Homo sapiens. [Contig view]
GeneID	5707.
KEGG	hsa:5707.
NMPDR	fig|9606.3.peg.19493.
UCSC	uc002vrn.1. human.
Organism-specific databases
GeneCards	GC02P231629.
H-InvDB	HIX0029913.
HGNC	HGNC:9554. PSMD1.
PharmGKB	PA33899.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q99460.
OMA	Q99460. XVNQFRQ.
Enzyme and pathway databases
Reactome	REACT_11045. Signaling by Wnt. REACT_13. Metabolism of amino acids. REACT_13635. Regulation of activated PAK-2p34 by proteasome mediated degradation. REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_383. DNA Replication. REACT_578. Apoptosis. REACT_6185. HIV Infection. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.
Gene expression databases
ArrayExpress	Q99460.
Bgee	Q99460.
CleanEx	HS_PSMD1.
GermOnline	ENSG00000173692. Homo sapiens.
Family and domain databases
InterPro	IPR016642. 26S_Psome_Rpn2. IPR002015. APC_proteasome. IPR011989. ARM-like. [Graphical view]
Gene3D	G3DSA:1.25.10.10. ARM-like. 1 hit.
Pfam	PF01851. PC_rep. 8 hits. [Graphical view]
PIRSF	PIRSF015947. 26S_Psome_Rpn2. 1 hit.
ProtoNet	Search...
Other Resources
DrugBank	DB00188. Bortezomib.
NextBio	22174.

Entry information

Entry name

PSMD1_HUMAN

Accession

Primary (citable) accession number: Q99460
Secondary accession number(s): 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:	July 7, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)