Reviewed, UniProtKB/Swiss-Prot P43686 (PRS6B_HUMAN)

Names and origin

Protein names

Recommended name:
    26S protease regulatory subunit 6B
Alternative name(s):
    Proteasome 26S subunit ATPase 4
    MB67-interacting protein
    MIP224
    TAT-binding protein 7
      Short name=TBP-7

Gene names

Name:	PSMC4
Synonyms:	MIP224, TBP7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	418 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex. Ref.9
Subunit structure	Interacts with NR1I3. Interacts with PAAF1. Ref.3 Ref.10
Subcellular location	Cytoplasm. Nucleus.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the AAA ATPase family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
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
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay. Source: HPA proteasome complex Ref.3 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAG2	O95816	1	EBI-743997,EBI-355275
CMYA5	Q8N3K9	1	EBI-743997,EBI-2323272
HTR1E	P28566	1	EBI-743997,EBI-1043151
PAAF1	Q9BRP4	1	EBI-743997,EBI-1056358
PAICS	P22234	1	EBI-743997,EBI-712261
PSMC1	P62191	1	EBI-743997,EBI-357598
PSMC2	P35998	1	EBI-743997,EBI-359710
PSMC3	P17980	1	EBI-743997,EBI-359720
PSMC5	P62195	1	EBI-743997,EBI-357745
PSMD1	Q99460	1	EBI-743997,EBI-357874
PSMD10	O75832	2	EBI-743997,EBI-752185
PSMD11	O00231	1	EBI-743997,EBI-357816
PSMD13	Q9UNM6	1	EBI-743997,EBI-356070
PSMD2	Q13200	1	EBI-743997,EBI-357648
PSMD6	Q15008	1	EBI-743997,EBI-359701
PSMD7	P51665	1	EBI-743997,EBI-357659
RIOK3	O14730	1	EBI-743997,EBI-1047061

Alternative products

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

Isoform 1 (identifier: P43686-1)

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: P43686-2)

The sequence of this isoform differs from the canonical sequence as follows:
     46-76: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 418

418

26S protease regulatory subunit 6B

PRO_0000084686

Regions

Nucleotide binding

206 – 213

8

ATP Potential

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.8 Ref.11

Modified residue

28

1

Phosphoserine Ref.12 Ref.13

Natural variations

Alternative sequence

46 – 76

31

Missing in isoform 2.

VSP_000022

Experimental info

Sequence conflict

73

1

L → F in AAC32612. Ref.4

Sequence conflict

110

1

N → S in AAC32612. Ref.4

Sequence conflict

118

1

T → A Ref.1

Sequence conflict

157

1

D → G in AAC32612. Ref.4

Sequence conflict

185

1

L → V in AAC32612. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

418

Helix Strand Turn

Details...

Helix

338 – 348

11

Turn

349 – 351

3

Helix

361 – 364

4

Helix

372 – 388

17

Beta strand

392 – 394

3

Helix

396 – 406

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2002. Version 2. Checksum: 80F9523C61B88F0C	FASTA	418	47,366
	10 20 30 40 50 60 MEEIGILVEK AQDEIPALSV SRPQTGLSFL GPEPEDLEDL YSRYKKLQQE LEFLEVQEEY 70 80 90 100 110 120 IKDEQKNLKK EFLHAQEEVK RIQSIPLVIG QFLEAVDQNT AIVGSTTGSN YYVRILSTID 130 140 150 160 170 180 RELLKPNASV ALHKHSNALV DVLPPEADSS IMMLTSDQKP DVMYADIGGM DIQKQEVREA 190 200 210 220 230 240 VELPLTHFEL YKQIGIDPPR GVLMYGPPGC GKTMLAKAVA HHTTAAFIRV VGSEFVQKYL 250 260 270 280 290 300 GEGPRMVRDV FRLAKENAPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFD 310 320 330 340 350 360 QNVNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLIFSTITS KMNLSEEVDL 370 380 390 400 410 EDYVARPDKI SGADINSICQ ESGMLAVREN RYIVLAKDFE KAYKTVIKKD EQEHEFYK
	Isoform 2. Checksum: FA64D44EE00E9A7B	FASTA	387	43,508
	10 20 30 40 50 60 MEEIGILVEK AQDEIPALSV SRPQTGLSFL GPEPEDLEDL YSRYKEEVKR IQSIPLVIGQ 70 80 90 100 110 120 FLEAVDQNTA IVGSTTGSNY YVRILSTIDR ELLKPNASVA LHKHSNALVD VLPPEADSSI 130 140 150 160 170 180 MMLTSDQKPD VMYADIGGMD IQKQEVREAV ELPLTHFELY KQIGIDPPRG VLMYGPPGCG 190 200 210 220 230 240 KTMLAKAVAH HTTAAFIRVV GSEFVQKYLG EGPRMVRDVF RLAKENAPAI IFIDEIDAIA 250 260 270 280 290 300 TKRFDAQTGA DREVQRILLE LLNQMDGFDQ NVNVKVIMAT NRADTLDPAL LRPGRLDRKI 310 320 330 340 350 360 EFPLPDRRQK RLIFSTITSK MNLSEEVDLE DYVARPDKIS GADINSICQE SGMLAVRENR 370 380 YIVLAKDFEK AYKTVIKKDE QEHEFYK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genes." Ohana B., Moore P.A., Ruben S.M., Southgate C.D., Green M.R., Rosen C.A. Proc. Natl. Acad. Sci. U.S.A. 90:138-142(1993) [PubMed: 8419915] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Human 26S proteasome ATPase subunit gene expressed in hematopoietic progenitor CD34+ cell." Zhang Q., Mao M., Huang Q., Zhou J., Fu G., Wu J., Wang Y., Chen S., Chen Z. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Blood.
[3]	"A component of the 26S proteasome binds on orphan member of the nuclear hormone receptor superfamily." Choi H.S., Seol W., Moore D.D. J. Steroid Biochem. Mol. Biol. 56:23-30(1996) [PubMed: 8603043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH NR1I3.
[4]	"Cloning and expression analysis of a novel human gene homologous to mouse proteasomal ATPase (Tat-binding protein 7)." Bi A., Yu L., Zheng L. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"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).
[6]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Lung, Pancreas and Skin.
[8]	Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-10; 218-229; 307-313 AND 343-369, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: Hepatoma.
[9]	"Tat-binding protein 7 is a subunit of the 26S protease." Dubiel W., Ferrell K., Rechsteiner M. Biol. Chem. Hoppe-Seyler 375:237-240(1994) [PubMed: 8060531] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION.
[10]	"Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases." Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B. Mol. Cell. Biol. 25:3842-3853(2005) [PubMed: 15831487] [Abstract] Cited for: INTERACTION WITH PAAF1.
[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: 17323924] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.
[12]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, MASS SPECTROMETRY.
[13]	"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 SER-28, MASS SPECTROMETRY.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]	"Structure of the oncoprotein gankyrin in complex with S6 ATPase of the 26S proteasome." Nakamura Y., Nakano K., Umehara T., Kimura M., Hayashizaki Y., Tanaka A., Horikoshi M., Padmanabhan B., Yokoyama S. Structure 15:179-189(2007) [PubMed: 17292836] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 337-418 IN COMPLEX WITH MOUSE PSMD10.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF038965 mRNA. Translation: AAC26843.1.
U27515 mRNA. Translation: AAC99817.1.
AF020736 mRNA. Translation: AAC32612.1.
BT007232 mRNA. Translation: AAP35896.1.
AC007842 Genomic DNA. Translation: AAD39267.1.
BC000343 mRNA. Translation: AAH00343.1.
BC010396 mRNA. Translation: AAH10396.1.
BC014488 mRNA. Translation: AAH14488.1.

IPI

IPI00020042.
IPI00216770.

RefSeq

NP_006494.1.
NP_694546.1.

UniGene

Hs.211594

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DVW	X-ray	2.30	B	337-418	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P43686. 25 interactions.

PTM databases

PhosphoSite

P43686.

2-D gel databases

OGP

P43686.

Proteomic databases

PRIDE

P43686.

Genome annotation databases

Ensembl

ENSG00000013275. Homo sapiens. [Contig view]

GeneID

5704.

KEGG

hsa:5704.

Organism-specific databases

GeneCards

GC19P045168.
GC19P045169.

H-InvDB

HIX0015127.

HGNC

HGNC:9551. PSMC4.

HPA

HPA002044.
HPA005471.

MIM

602707. gene.

PharmGKB

PA33896.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P43686.

HOVERGEN

P43686.

OMA

P43686. FRLAREN.

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

P43686.

Bgee

P43686.

CleanEx

HS_PSMC4.

GermOnline

ENSG00000013275. Homo sapiens.

Family and domain databases

InterPro

IPR005937. 26S_Psome_P45.
IPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
[Graphical view]

Pfam

PF00004. AAA. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01242. 26Sp45. 1 hit.

PROSITE

PS00674. AAA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

22160.

SOURCE

Search...

Entry information

Entry name

PRS6B_HUMAN

Accession

Primary (citable) accession number: P43686
Secondary accession number(s): Q96FV5, Q9UBM3, Q9UEX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	May 10, 2002
Last modified:	June 16, 2009
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)