P43686 (PRS6B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
26S protease regulatory subunit 6B

Alternative name(s):
26S proteasome AAA-ATPase subunit RPT3
MB67-interacting protein
MIP224
Proteasome 26S subunit ATPase 4
Tat-binding protein 7
Short name=TBP-7

Gene names

Name:	PSMC4
Synonyms:	MIP224, TBP7

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	418 AA.
Sequence status	Complete.
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. Interacts with TRIM5. Ref.3 Ref.10 Ref.18
Subcellular location	Cytoplasm. Nucleus.
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 Complete proteome Direct protein sequencing 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 blastocyst development Inferred from electronic annotation. Source: Compara 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 viral reproduction Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome proteasome accessory complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Traceable author statement PubMed 9473509. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PSMC5	P62195	11	EBI-743997,EBI-357745
PSMC6	P62333	3	EBI-743997,EBI-357669
PSMD10	O75832	8	EBI-743997,EBI-752185

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

Modified residue

21

1

Phosphoserine Ref.14

Modified residue

28

1

Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14 Ref.16

Modified residue

397

1

N6-acetyllysine Ref.15

Modified residue

401

1

N6-acetyllysine Ref.15

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 no nucleotide entry 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 [UniParc]. 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Umbilical cord 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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 SER-21 AND SER-28, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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-397 AND LYS-401, MASS SPECTROMETRY.
[16]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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].
[18]	"TRIM5alpha associates with proteasomal subunits in cells while in complex with HIV-1 virions." Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L., Luban J., Campbell E.M. Retrovirology 8:93-93(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRIM5.
[19]	"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] [Europe PMC] [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

EMBL
GenBank
DDBJ

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. NM_006503.3.
NP_694546.1. NM_153001.2.

UniGene

Hs.211594.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P43686.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29274N.

IntAct

P43686. 15 interactions.

MINT

MINT-5004247.

STRING

9606.ENSP00000157812.

PTM databases

PhosphoSite

P43686.

Polymorphism databases

DMDM

20532409.

2D gel databases

OGP

P43686.

Proteomic databases

PaxDb

P43686.

PRIDE

P43686.

Protocols and materials databases

DNASU

5704.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000157812; ENSP00000157812; ENSG00000013275.
ENST00000455878; ENSP00000413869; ENSG00000013275.

GeneID

5704.

KEGG

hsa:5704.

UCSC

uc002omq.3. human.
uc002omr.3. human.

Organism-specific databases

CTD

5704.

GeneCards

GC19P040477.

HGNC

HGNC:9551. PSMC4.

HPA

HPA002044.
HPA005471.

MIM

602707. gene.

neXtProt

NX_P43686.

PharmGKB

PA33896.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1222.

HOGENOM

HOG000225143.

HOVERGEN

HBG000109.

InParanoid

P43686.

KO

K03063.

OMA

DQTTNVK.

OrthoDB

EOG4KD6M4.

PhylomeDB

P43686.

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

P43686.

Bgee

P43686.

CleanEx

HS_PSMC4.

Genevestigator

P43686.

GermOnline

ENSG00000013275. Homo sapiens.

Family and domain databases

InterPro

IPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
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

ChiTaRS

PSMC4. human.

EvolutionaryTrace

P43686.

GenomeRNAi

5704.

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:	May 1, 2013
This is version 136 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.