PSMD2

Functionⁱ

Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.1 Publication

Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1.

GO - Molecular functionⁱ

enzyme regulator activity Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

neutrophil degranulation Source: Reactome
post-translational protein modification Source: Reactome
proteasome-mediated ubiquitin-dependent protein catabolic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
protein deubiquitination Source: Reactome
regulation of protein catabolic process Source: InterPro

View the complete GO annotation on QuickGO ...

Enzyme and pathway databases

Reactomeⁱ	R-HSA-1169091 Activation of NF-kappaB in B cells R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha R-HSA-1236974 ER-Phagosome pathway R-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes) R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C R-HSA-174113 SCF-beta-TrCP mediated degradation of Emi1 R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A R-HSA-180534 Vpu mediated degradation of CD4 R-HSA-180585 Vif-mediated degradation of APOBEC3G R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21 R-HSA-195253 Degradation of beta-catenin by the destruction complex R-HSA-202424 Downstream TCR signaling R-HSA-211733 Regulation of activated PAK-2p34 by proteasome mediated degradation R-HSA-2467813 Separation of Sister Chromatids R-HSA-2871837 FCERI mediated NF-kB activation R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1 R-HSA-350562 Regulation of ornithine decarboxylase (ODC) R-HSA-382556 ABC-family proteins mediated transport R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA R-HSA-4608870 Asymmetric localization of PCP proteins R-HSA-4641257 Degradation of AXIN R-HSA-4641258 Degradation of DVL R-HSA-5358346 Hedgehog ligand biogenesis R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling R-HSA-5607764 CLEC7A (Dectin-1) signaling R-HSA-5610780 Degradation of GLI1 by the proteasome R-HSA-5610783 Degradation of GLI2 by the proteasome R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome R-HSA-5632684 Hedgehog 'on' state R-HSA-5658442 Regulation of RAS by GAPs R-HSA-5668541 TNFR2 non-canonical NF-kB pathway R-HSA-5676590 NIK-->noncanonical NF-kB signaling R-HSA-5678895 Defective CFTR causes cystic fibrosis R-HSA-5687128 MAPK6/MAPK4 signaling R-HSA-5689603 UCH proteinases R-HSA-5689880 Ub-specific processing proteases R-HSA-6798695 Neutrophil degranulation R-HSA-68827 CDT1 association with the CDC6:ORC:origin complex R-HSA-68949 Orc1 removal from chromatin R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6 R-HSA-69229 Ubiquitin-dependent degradation of Cyclin D1 R-HSA-69481 G2/M Checkpoints R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs R-HSA-8939902 Regulation of RUNX2 expression and activity R-HSA-8941858 Regulation of RUNX3 expression and activity R-HSA-8948751 Regulation of PTEN stability and activity R-HSA-8951664 Neddylation R-HSA-9010553 Regulation of expression of SLITs and ROBOs R-HSA-9020702 Interleukin-1 signaling R-HSA-9604323 Negative regulation of NOTCH4 signaling R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

Reactomeⁱ

R-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236974 ER-Phagosome pathway
R-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174113 SCF-beta-TrCP mediated degradation of Emi1
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-180534 Vpu mediated degradation of CD4
R-HSA-180585 Vif-mediated degradation of APOBEC3G
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-202424 Downstream TCR signaling
R-HSA-211733 Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-350562 Regulation of ornithine decarboxylase (ODC)
R-HSA-382556 ABC-family proteins mediated transport
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-4608870 Asymmetric localization of PCP proteins
R-HSA-4641257 Degradation of AXIN
R-HSA-4641258 Degradation of DVL
R-HSA-5358346 Hedgehog ligand biogenesis
R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5610780 Degradation of GLI1 by the proteasome
R-HSA-5610783 Degradation of GLI2 by the proteasome
R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684 Hedgehog 'on' state
R-HSA-5658442 Regulation of RAS by GAPs
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-5676590 NIK-->noncanonical NF-kB signaling
R-HSA-5678895 Defective CFTR causes cystic fibrosis
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-6798695 Neutrophil degranulation
R-HSA-68827 CDT1 association with the CDC6:ORC:origin complex
R-HSA-68949 Orc1 removal from chromatin
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69229 Ubiquitin-dependent degradation of Cyclin D1
R-HSA-69481 G2/M Checkpoints
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-9604323 Negative regulation of NOTCH4 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

Protein family/group databases

MoonDBⁱ	Q13200 Predicted

MoonDBⁱ

Q13200 Predicted

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: 26S proteasome non-ATPase regulatory subunit 2 Alternative name(s): 26S proteasome regulatory subunit RPN1 26S proteasome regulatory subunit S2 26S proteasome subunit p97 Protein 55.11 Tumor necrosis factor type 1 receptor-associated protein 2
Gene namesⁱ	Name:PSMD2 Synonyms:TRAP2
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 3

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000175166.16
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9559 PSMD2
MIMⁱ	606223 gene
neXtProtⁱ	NX_Q13200

Subcellular locationⁱ

GO - Cellular component

Keywords - Cellular componentⁱ

Proteasome

Pathology & Biotechⁱ

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5708
Open Targets More...OpenTargetsⁱ	ENSG00000175166
PharmGKBⁱ	PA33905

Chemistry databases

ChEMBLⁱ	CHEMBL2364701

ChEMBLⁱ

CHEMBL2364701

Polymorphism and mutation databases

BioMutaⁱ	PSMD2
DMDMⁱ	6174930

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000173810	1 – 908	26S proteasome non-ATPase regulatory subunit 2Add BLAST		908

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	1	N-acetylmethionineBy similarity	1
Modified residueⁱ	16	PhosphoserineCombined sources	1
Modified residueⁱ	24	PhosphothreonineCombined sources	1
Modified residueⁱ	29	PhosphoserineCombined sources	1
Modified residueⁱ	147	PhosphoserineCombined sources	1
Modified residueⁱ	194	PhosphotyrosineCombined sources	1
Modified residueⁱ	361	PhosphoserineCombined sources	1
Modified residueⁱ	363	PhosphoserineCombined sources	1
Modified residueⁱ	551	N6-acetyllysineBy similarity	1

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	Q13200
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q13200
PaxDbⁱ	Q13200
PeptideAtlas More...PeptideAtlasⁱ	Q13200
PRIDEⁱ	Q13200
ProteomicsDBⁱ	59219

PTM databases

iPTMnetⁱ	Q13200
PhosphoSitePlusⁱ	Q13200
SwissPalmⁱ	Q13200

Expressionⁱ

Tissue specificityⁱ

Found in skeletal muscle, liver, heart, brain, kidney, pancreas, lung and placenta.

Gene expression databases

Bgeeⁱ	ENSG00000175166 Expressed in 231 organ(s), highest expression level in testis
CleanExⁱ	HS_PSMD2
ExpressionAtlasⁱ	Q13200 baseline and differential
Genevisibleⁱ	Q13200 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA045192

HPAⁱ

HPA045192

Interactionⁱ

Subunit structureⁱ

Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases and few additional components including PSMD2 (PubMed:27428775, PubMed:27342858). Interacts with RPGRIP1L (By similarity).By similarity2 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
	Q53HB3	2	EBI-357648,EBI-9362707
BAG1	Q99933	7	EBI-357648,EBI-1030678
EBNA-LP	Q8AZK7	2	EBI-357648,EBI-1185167	From Epstein-Barr virus (strain B95-8).
Hacd3	Q8K2C9	2	EBI-357648,EBI-8329978	From Mus musculus.
MLF1	P58340	2	EBI-357648,EBI-721328
PSMC1	P62191	16	EBI-357648,EBI-357598
PSMC1	Q53XL8	3	EBI-357648,EBI-10242995
PSMC2	P35998	3	EBI-357648,EBI-359710
PSMC5	P62195	9	EBI-357648,EBI-357745
PSMD4	P55036	3	EBI-357648,EBI-359318
UBLCP1	Q8WVY7	10	EBI-357648,EBI-750011
UCHL5	Q9Y5K5	5	EBI-357648,EBI-1051183

Protein-protein interaction databases

BioGridⁱ	111681, 186 interactors
CORUMⁱ	Q13200
Database of interacting proteins More...DIPⁱ	DIP-38204N
IntActⁱ	Q13200, 158 interactors
Molecular INTeraction database More...MINTⁱ	Q13200
STRINGⁱ	9606.ENSP00000310129

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q13200
SMRⁱ	Q13200
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Repeatⁱ	409 – 442	PC 1Add BLAST	34
Repeatⁱ	443 – 479	PC 2Add BLAST	37
Repeatⁱ	480 – 514	PC 3Add BLAST	35
Repeatⁱ	517 – 551	PC 4Add BLAST	35
Repeatⁱ	560 – 589	PC 5Add BLAST	30
Repeatⁱ	692 – 723	PC 6Add BLAST	32
Repeatⁱ	742 – 757	PC 7Add BLAST	16

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	623 – 641	Glu/Lys-richAdd BLAST		19

Sequence similaritiesⁱ

Belongs to the proteasome subunit S2 family.Curated

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	KOG2005 Eukaryota COG5110 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000074983
HOGENOMⁱ	HOG000176022
HOVERGENⁱ	HBG001842
InParanoidⁱ	Q13200
KEGG Orthology (KO) More...KOⁱ	K03028
OMAⁱ	MVDICAY
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G04TC
PhylomeDBⁱ	Q13200
TreeFamⁱ	TF105739

Family and domain databases

Gene3Dⁱ	1.25.10.10, 1 hit
InterProⁱ	View protein in InterPro IPR016643 26S_Psome_Rpn1 IPR011989 ARM-like IPR016024 ARM-type_fold IPR002015 Proteasome/cyclosome_rpt
PANTHERⁱ	PTHR10943:SF1 PTHR10943:SF1, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01851 PC_rep, 2 hits
PIRSFⁱ	PIRSF015965 26S_Psome_Rpn1, 1 hit
SUPFAMⁱ	SSF48371 SSF48371, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q13200-1) [UniParc]FASTA Add to basket

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.

« Hide

        10         20         30         40         50
MEEGGRDKAP VQPQQSPAAA PGGTDEKPSG KERRDAGDKD KEQELSEEDK 
        60         70         80         90        100
QLQDELEMLV ERLGEKDTSL YRPALEELRR QIRSSTTSMT SVPKPLKFLR 
       110        120        130        140        150
PHYGKLKEIY ENMAPGENKR FAADIISVLA MTMSGERECL KYRLVGSQEE 
       160        170        180        190        200
LASWGHEYVR HLAGEVAKEW QELDDAEKVQ REPLLTLVKE IVPYNMAHNA 
       210        220        230        240        250
EHEACDLLME IEQVDMLEKD IDENAYAKVC LYLTSCVNYV PEPENSALLR 
       260        270        280        290        300
CALGVFRKFS RFPEALRLAL MLNDMELVED IFTSCKDVVV QKQMAFMLGR 
       310        320        330        340        350
HGVFLELSED VEEYEDLTEI MSNVQLNSNF LALARELDIM EPKVPDDIYK 
       360        370        380        390        400
THLENNRFGG SGSQVDSARM NLASSFVNGF VNAAFGQDKL LTDDGNKWLY 
       410        420        430        440        450
KNKDHGMLSA AASLGMILLW DVDGGLTQID KYLYSSEDYI KSGALLACGI 
       460        470        480        490        500
VNSGVRNECD PALALLSDYV LHNSNTMRLG SIFGLGLAYA GSNREDVLTL 
       510        520        530        540        550
LLPVMGDSKS SMEVAGVTAL ACGMIAVGSC NGDVTSTILQ TIMEKSETEL 
       560        570        580        590        600
KDTYARWLPL GLGLNHLGKG EAIEAILAAL EVVSEPFRSF ANTLVDVCAY 
       610        620        630        640        650
AGSGNVLKVQ QLLHICSEHF DSKEKEEDKD KKEKKDKDKK EAPADMGAHQ 
       660        670        680        690        700
GVAVLGIALI AMGEEIGAEM ALRTFGHLLR YGEPTLRRAV PLALALISVS 
       710        720        730        740        750
NPRLNILDTL SKFSHDADPE VSYNSIFAMG MVGSGTNNAR LAAMLRQLAQ 
       760        770        780        790        800
YHAKDPNNLF MVRLAQGLTH LGKGTLTLCP YHSDRQLMSQ VAVAGLLTVL 
       810        820        830        840        850
VSFLDVRNII LGKSHYVLYG LVAAMQPRML VTFDEELRPL PVSVRVGQAV 
       860        870        880        890        900
DVVGQAGKPK TITGFQTHTT PVLLAHGERA ELATEEFLPV TPILEGFVIL 

RKNPNYDL

Length:908

Mass (Da):100,200

Last modified:July 15, 1999 - v3

Checksum:ⁱFAD71E7B26101BE3

GO

Isoform 2 (identifier: Q13200-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-163: MEEGGRDKAP...WGHEYVRHLA → MSMS

« Hide

        10         20         30         40         50
MSMSGEVAKE WQELDDAEKV QREPLLTLVK EIVPYNMAHN AEHEACDLLM 
        60         70         80         90        100
EIEQVDMLEK DIDENAYAKV CLYLTSCVNY VPEPENSALL RCALGVFRKF 
       110        120        130        140        150
SRFPEALRLA LMLNDMELVE DIFTSCKDVV VQKQMAFMLG RHGVFLELSE 
       160        170        180        190        200
DVEEYEDLTE IMSNVQLNSN FLALARELDI MEPKVPDDIY KTHLENNRFG 
       210        220        230        240        250
GSGSQVDSAR MNLASSFVNG FVNAAFGQDK LLTDDGNKWL YKNKDHGMLS 
       260        270        280        290        300
AAASLGMILL WDVDGGLTQI DKYLYSSEDY IKSGALLACG IVNSGVRNEC 
       310        320        330        340        350
DPALALLSDY VLHNSNTMRL GSIFGLGLAY AGSNREDVLT LLLPVMGDSK 
       360        370        380        390        400
SSMEVAGVTA LACGMIAVGS CNGDVTSTIL QTIMEKSETE LKDTYARWLP 
       410        420        430        440        450
LGLGLNHLGK GEAIEAILAA LEVVSEPFRS FANTLVDVCA YAGSGNVLKV 
       460        470        480        490        500
QQLLHICSEH FDSKEKEEDK DKKEKKDKDK KEAPADMGAH QGVAVLGIAL 
       510        520        530        540        550
IAMGEEIGAE MALRTFGHLL RYGEPTLRRA VPLALALISV SNPRLNILDT 
       560        570        580        590        600
LSKFSHDADP EVSYNSIFAM GMVGSGTNNA RLAAMLRQLA QYHAKDPNNL 
       610        620        630        640        650
FMVRLAQGLT HLGKGTLTLC PYHSDRQLMS QVAVAGLLTV LVSFLDVRNI 
       660        670        680        690        700
ILGKSHYVLY GLVAAMQPRM LVTFDEELRP LPVSVRVGQA VDVVGQAGKP 
       710        720        730        740 
KTITGFQTHT TPVLLAHGER AELATEEFLP VTPILEGFVI LRKNPNYDL

Note: No experimental confirmation available.

Show »

Length:749

Mass (Da):82,193

Checksum:ⁱ4007D2AAADF807A6

GO

Isoform 3 (identifier: Q13200-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-130: Missing.

« Hide

        10         20         30         40         50
MTMSGERECL KYRLVGSQEE LASWGHEYVR HLAGEVAKEW QELDDAEKVQ 
        60         70         80         90        100
REPLLTLVKE IVPYNMAHNA EHEACDLLME IEQVDMLEKD IDENAYAKVC 
       110        120        130        140        150
LYLTSCVNYV PEPENSALLR CALGVFRKFS RFPEALRLAL MLNDMELVED 
       160        170        180        190        200
IFTSCKDVVV QKQMAFMLGR HGVFLELSED VEEYEDLTEI MSNVQLNSNF 
       210        220        230        240        250
LALARELDIM EPKVPDDIYK THLENNRFGG SGSQVDSARM NLASSFVNGF 
       260        270        280        290        300
VNAAFGQDKL LTDDGNKWLY KNKDHGMLSA AASLGMILLW DVDGGLTQID 
       310        320        330        340        350
KYLYSSEDYI KSGALLACGI VNSGVRNECD PALALLSDYV LHNSNTMRLG 
       360        370        380        390        400
SIFGLGLAYA GSNREDVLTL LLPVMGDSKS SMEVAGVTAL ACGMIAVGSC 
       410        420        430        440        450
NGDVTSTILQ TIMEKSETEL KDTYARWLPL GLGLNHLGKG EAIEAILAAL 
       460        470        480        490        500
EVVSEPFRSF ANTLVDVCAY AGSGNVLKVQ QLLHICSEHF DSKEKEEDKD 
       510        520        530        540        550
KKEKKDKDKK EAPADMGAHQ GVAVLGIALI AMGEEIGAEM ALRTFGHLLR 
       560        570        580        590        600
YGEPTLRRAV PLALALISVS NPRLNILDTL SKFSHDADPE VSYNSIFAMG 
       610        620        630        640        650
MVGSGTNNAR LAAMLRQLAQ YHAKDPNNLF MVRLAQGLTH LGKGTLTLCP 
       660        670        680        690        700
YHSDRQLMSQ VAVAGLLTVL VSFLDVRNII LGKSHYVLYG LVAAMQPRML 
       710        720        730        740        750
VTFDEELRPL PVSVRVGQAV DVVGQAGKPK TITGFQTHTT PVLLAHGERA 
       760        770 
ELATEEFLPV TPILEGFVIL RKNPNYDL

Note: No experimental confirmation available.

Show »

Length:778

Mass (Da):85,606

Checksum:ⁱ5564271C57A5959D

GO

Computationally mapped potential isoform sequencesⁱ

There are 4 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

C9JPC0	C9JPC0_HUMAN	26S proteasome non-ATPase regulator... 26S proteasome non-ATPase regulatory subunit 2	PSMD2	217	Annotation score:
H7C1H2	H7C1H2_HUMAN	26S proteasome non-ATPase regulator... 26S proteasome non-ATPase regulatory subunit 2	PSMD2	203	Annotation score:
H7C2Q3	H7C2Q3_HUMAN	26S proteasome non-ATPase regulator... 26S proteasome non-ATPase regulatory subunit 2	PSMD2	143	Annotation score:
F8WBS8	F8WBS8_HUMAN	26S proteasome non-ATPase regulator... 26S proteasome non-ATPase regulatory subunit 2	PSMD2	59	Annotation score:

Sequence cautionⁱ

The sequence AAA87705 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	10	P → R in CAA60167 (PubMed:7601280).Curated	1
Sequence conflictⁱ	21	P → S (PubMed:9126987).Curated	1
Sequence conflictⁱ	32	E → G (PubMed:9126987).Curated	1
Sequence conflictⁱ	43	Q → L (PubMed:9126987).Curated	1
Sequence conflictⁱ	57	E → V (PubMed:9126987).Curated	1
Sequence conflictⁱ	60	V → A in BAA11226 (PubMed:8774743).Curated	1
Sequence conflictⁱ	226	Y → S in AAA87705 (PubMed:9126987).Curated	1
Sequence conflictⁱ	260	S → T in CAA60167 (PubMed:7601280).Curated	1
Sequence conflictⁱ	281 – 283	IFT → SS in AAA87705 (PubMed:9126987).Curated	3
Sequence conflictⁱ	415	G → A in BAA11226 (PubMed:8774743).Curated	1
Sequence conflictⁱ	731	M → MGM (PubMed:9126987).Curated	1
Sequence conflictⁱ	776	L → P in BAG63219 (PubMed:14702039).Curated	1
Sequence conflictⁱ	900 – 908	LRKNPNYDL → FGRTPIMISK (PubMed:15489334).Curated	9
Sequence conflictⁱ	900 – 908	LRKNPNYDL → FGRTPIMISK (PubMed:7601280).Curated	9

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_051554	176	A → T. Corresponds to variant dbSNP:rs11545172Ensembl.	1
Natural variantⁱVAR_051555	313	E → D1 PublicationCorresponds to variant dbSNP:rs11545169Ensembl.	1
Natural variantⁱVAR_067451	724	N → Y2 PublicationsCorresponds to variant dbSNP:rs17856236Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_055065	1 – 163	MEEGG…VRHLA → MSMS in isoform 2. 1 PublicationAdd BLAST		163
Alternative sequenceⁱVSP_055066	1 – 130	Missing in isoform 3. 1 PublicationAdd BLAST		130

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	D78151 mRNA Translation: BAA11226.1 BT009736 mRNA Translation: AAP88738.1 AK301759 mRNA Translation: BAG63219.1 AK302177 mRNA Translation: BAG63543.1 AC078797 Genomic DNA No translation available. BC002368 mRNA Translation: AAH02368.1 BC002997 mRNA Translation: AAH02997.1 BC007897 mRNA Translation: AAH07897.1 U12596 mRNA Translation: AAA87705.1 Different initiation. X86446 mRNA Translation: CAA60167.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS3258.1 [Q13200-1] CCDS63853.1 [Q13200-3] CCDS63854.1 [Q13200-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_001265637.1, NM_001278708.1 [Q13200-3] NP_001265638.1, NM_001278709.1 [Q13200-2] NP_002799.3, NM_002808.4 [Q13200-1]
UniGeneⁱ	Hs.518464

Genome annotation databases

Ensemblⁱ	ENST00000310118; ENSP00000310129; ENSG00000175166 [Q13200-1] ENST00000435761; ENSP00000402618; ENSG00000175166 [Q13200-2] ENST00000439383; ENSP00000416028; ENSG00000175166 [Q13200-3]
GeneIDⁱ	5708
KEGGⁱ	hsa:5708
UCSC genome browser More...UCSCⁱ	uc003fnn.3 human [Q13200-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Protein	Similar proteins		Species	Score	Length	Source
Q13200	26S proteasome non-ATPase regulatory subunit 2		PANTR		908	UniRef100_Q13200
26S proteasome non-ATPase regulatory subunit 2		PANPA		908
26S proteasome non-ATPase regulatory subunit 2		MANLE		882
Uncharacterized protein DKFZp564A2282 (Fragment)		HUMAN		632
UPI000B9D4F83		HUMAN		848
Q13200-2	26S proteasome non-ATPase regulatory subunit 2		PANTR		749	UniRef100_A0A2J8M5F7
Q13200-3	26S proteasome non-ATPase regulatory subunit 2		RABIT		1051	UniRef100_G1SSA2
26S proteasome non-ATPase regulatory subunit 2		PANTR		778
UPI000B9D4F84		HUMAN		784
UPI0000D4E737		MANLE		851
UPI0001C62FEB		RABIT		908

Protein	Similar proteins		Species	Score	Length	Source
Q13200	26S proteasome non-ATPase regulatory subunit 2	)	RAT		908	UniRef90_Q13200
26S proteasome non-ATPase regulatory subunit 2		PONAB		908
26S proteasome non-ATPase regulatory subunit 2		MOUSE		908
26S proteasome non-ATPase regulatory subunit 2		BOVIN		908
26S proteasome non-ATPase regulatory subunit 2		PANTR		908
+241
Q13200-2	26S proteasome non-ATPase regulatory subunit 2		LEPWE		749	UniRef90_A0A2U3Z6N5
26S proteasome non-ATPase regulatory subunit 2		PONAB		749
26S proteasome non-ATPase regulatory subunit 2		PANTR		749
26S proteasome non-ATPase regulatory subunit 2		ODORO		749
Uncharacterized protein (Fragment)		MICCO		118
+7

Protein	Similar proteins		Species	Score	Length	Source
Q13200	26S proteasome non-ATPase regulatory subunit 2		BOVIN		908	UniRef50_Q13200
26S proteasome non-ATPase regulatory subunit 2		PONAB		908
26S proteasome non-ATPase regulatory subunit 2		MOUSE		908
26S proteasome non-ATPase regulatory subunit 2	)	RAT		908
26S proteasome non-ATPase regulatory subunit 2		PANTR		908
+829

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	D78151 mRNA Translation: BAA11226.1 BT009736 mRNA Translation: AAP88738.1 AK301759 mRNA Translation: BAG63219.1 AK302177 mRNA Translation: BAG63543.1 AC078797 Genomic DNA No translation available. BC002368 mRNA Translation: AAH02368.1 BC002997 mRNA Translation: AAH02997.1 BC007897 mRNA Translation: AAH07897.1 U12596 mRNA Translation: AAA87705.1 Different initiation. X86446 mRNA Translation: CAA60167.1
CCDSⁱ	CCDS3258.1 [Q13200-1] CCDS63853.1 [Q13200-3] CCDS63854.1 [Q13200-2]
RefSeqⁱ	NP_001265637.1, NM_001278708.1 [Q13200-3] NP_001265638.1, NM_001278709.1 [Q13200-2] NP_002799.3, NM_002808.4 [Q13200-1]
UniGeneⁱ	Hs.518464

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	5GJQ	electron microscopy	4.50	Z	1-908	[»]
	5GJR	electron microscopy	3.50	AC/Z	1-908	[»]
	5L4K	electron microscopy	4.50	Z	1-908	[»]
	5LN3	electron microscopy	6.80	Z	1-908	[»]
	5T0C	electron microscopy	3.80	Af/Bf	1-908	[»]
	5T0G	electron microscopy	4.40	f	164-908	[»]
	5T0H	electron microscopy	6.80	f	164-908	[»]
	5T0I	electron microscopy	8.00	f	164-908	[»]
	5T0J	electron microscopy	8.00	f	164-908	[»]
	5VFP	electron microscopy	4.20	f	1-908	[»]
	5VFQ	electron microscopy	4.20	f	1-908	[»]
	5VFR	electron microscopy	4.90	f	1-908	[»]
	5VFS	electron microscopy	3.60	f	6-853	[»]
	5VFT	electron microscopy	7.00	f	1-908	[»]
	5VFU	electron microscopy	5.80	f	1-908	[»]
	5VHF	electron microscopy	5.70	f	6-853	[»]
	5VHH	electron microscopy	6.10	f	6-853	[»]
	5VHI	electron microscopy	6.80	f	6-853	[»]
	5VHJ	electron microscopy	8.50	f	70-853	[»]
	5VHM	electron microscopy	8.30	f	6-853	[»]
	5VHN	electron microscopy	7.30	f	6-853	[»]
	5VHO	electron microscopy	8.30	f	6-853	[»]
	5VHP	electron microscopy	7.90	f	70-853	[»]
	5VHQ	electron microscopy	8.90	f	6-853	[»]
	5VHR	electron microscopy	7.70	f	6-853	[»]
	5VHS	electron microscopy	8.80	f	70-853	[»]
ProteinModelPortalⁱ	Q13200
SMRⁱ	Q13200
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	111681, 186 interactors
CORUMⁱ	Q13200
DIPⁱ	DIP-38204N
IntActⁱ	Q13200, 158 interactors
MINTⁱ	Q13200
STRINGⁱ	9606.ENSP00000310129

Chemistry databases

ChEMBLⁱ	CHEMBL2364701

ChEMBLⁱ

CHEMBL2364701

Protein family/group databases

MoonDBⁱ	Q13200 Predicted

MoonDBⁱ

Q13200 Predicted

PTM databases

iPTMnetⁱ	Q13200
PhosphoSitePlusⁱ	Q13200
SwissPalmⁱ	Q13200

Polymorphism and mutation databases

BioMutaⁱ	PSMD2
DMDMⁱ	6174930

Proteomic databases

EPDⁱ	Q13200
MaxQBⁱ	Q13200
PaxDbⁱ	Q13200
PeptideAtlasⁱ	Q13200
PRIDEⁱ	Q13200
ProteomicsDBⁱ	59219

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	5708
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000310118; ENSP00000310129; ENSG00000175166 [Q13200-1] ENST00000435761; ENSP00000402618; ENSG00000175166 [Q13200-2] ENST00000439383; ENSP00000416028; ENSG00000175166 [Q13200-3]
GeneIDⁱ	5708
KEGGⁱ	hsa:5708
UCSCⁱ	uc003fnn.3 human [Q13200-1]

Organism-specific databases

CTDⁱ	5708
DisGeNETⁱ	5708
EuPathDBⁱ	HostDB:ENSG00000175166.16
GeneCardsⁱ	PSMD2
HGNCⁱ	HGNC:9559 PSMD2
HPAⁱ	HPA045192
MIMⁱ	606223 gene
neXtProtⁱ	NX_Q13200
OpenTargetsⁱ	ENSG00000175166
PharmGKBⁱ	PA33905
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2005 Eukaryota COG5110 LUCA
GeneTreeⁱ	ENSGT00550000074983
HOGENOMⁱ	HOG000176022
HOVERGENⁱ	HBG001842
InParanoidⁱ	Q13200
KOⁱ	K03028
OMAⁱ	MVDICAY
OrthoDBⁱ	EOG091G04TC
PhylomeDBⁱ	Q13200
TreeFamⁱ	TF105739

Enzyme and pathway databases

Reactomeⁱ	R-HSA-1169091 Activation of NF-kappaB in B cells R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha R-HSA-1236974 ER-Phagosome pathway R-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes) R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C R-HSA-174113 SCF-beta-TrCP mediated degradation of Emi1 R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A R-HSA-180534 Vpu mediated degradation of CD4 R-HSA-180585 Vif-mediated degradation of APOBEC3G R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21 R-HSA-195253 Degradation of beta-catenin by the destruction complex R-HSA-202424 Downstream TCR signaling R-HSA-211733 Regulation of activated PAK-2p34 by proteasome mediated degradation R-HSA-2467813 Separation of Sister Chromatids R-HSA-2871837 FCERI mediated NF-kB activation R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1 R-HSA-350562 Regulation of ornithine decarboxylase (ODC) R-HSA-382556 ABC-family proteins mediated transport R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA R-HSA-4608870 Asymmetric localization of PCP proteins R-HSA-4641257 Degradation of AXIN R-HSA-4641258 Degradation of DVL R-HSA-5358346 Hedgehog ligand biogenesis R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling R-HSA-5607764 CLEC7A (Dectin-1) signaling R-HSA-5610780 Degradation of GLI1 by the proteasome R-HSA-5610783 Degradation of GLI2 by the proteasome R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome R-HSA-5632684 Hedgehog 'on' state R-HSA-5658442 Regulation of RAS by GAPs R-HSA-5668541 TNFR2 non-canonical NF-kB pathway R-HSA-5676590 NIK-->noncanonical NF-kB signaling R-HSA-5678895 Defective CFTR causes cystic fibrosis R-HSA-5687128 MAPK6/MAPK4 signaling R-HSA-5689603 UCH proteinases R-HSA-5689880 Ub-specific processing proteases R-HSA-6798695 Neutrophil degranulation R-HSA-68827 CDT1 association with the CDC6:ORC:origin complex R-HSA-68949 Orc1 removal from chromatin R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6 R-HSA-69229 Ubiquitin-dependent degradation of Cyclin D1 R-HSA-69481 G2/M Checkpoints R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs R-HSA-8939902 Regulation of RUNX2 expression and activity R-HSA-8941858 Regulation of RUNX3 expression and activity R-HSA-8948751 Regulation of PTEN stability and activity R-HSA-8951664 Neddylation R-HSA-9010553 Regulation of expression of SLITs and ROBOs R-HSA-9020702 Interleukin-1 signaling R-HSA-9604323 Negative regulation of NOTCH4 signaling R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

Reactomeⁱ

R-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236974 ER-Phagosome pathway
R-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174113 SCF-beta-TrCP mediated degradation of Emi1
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-180534 Vpu mediated degradation of CD4
R-HSA-180585 Vif-mediated degradation of APOBEC3G
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-202424 Downstream TCR signaling
R-HSA-211733 Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-350562 Regulation of ornithine decarboxylase (ODC)
R-HSA-382556 ABC-family proteins mediated transport
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-4608870 Asymmetric localization of PCP proteins
R-HSA-4641257 Degradation of AXIN
R-HSA-4641258 Degradation of DVL
R-HSA-5358346 Hedgehog ligand biogenesis
R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5610780 Degradation of GLI1 by the proteasome
R-HSA-5610783 Degradation of GLI2 by the proteasome
R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684 Hedgehog 'on' state
R-HSA-5658442 Regulation of RAS by GAPs
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-5676590 NIK-->noncanonical NF-kB signaling
R-HSA-5678895 Defective CFTR causes cystic fibrosis
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-6798695 Neutrophil degranulation
R-HSA-68827 CDT1 association with the CDC6:ORC:origin complex
R-HSA-68949 Orc1 removal from chromatin
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69229 Ubiquitin-dependent degradation of Cyclin D1
R-HSA-69481 G2/M Checkpoints
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-9604323 Negative regulation of NOTCH4 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

ChiTaRSⁱ	PSMD2 human
GeneWikiⁱ	PSMD2
GenomeRNAiⁱ	5708
Protein Ontology More...PROⁱ	PR:Q13200
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000175166 Expressed in 231 organ(s), highest expression level in testis
CleanExⁱ	HS_PSMD2
ExpressionAtlasⁱ	Q13200 baseline and differential
Genevisibleⁱ	Q13200 HS

Family and domain databases

Gene3Dⁱ	1.25.10.10, 1 hit
InterProⁱ	View protein in InterPro IPR016643 26S_Psome_Rpn1 IPR011989 ARM-like IPR016024 ARM-type_fold IPR002015 Proteasome/cyclosome_rpt
PANTHERⁱ	PTHR10943:SF1 PTHR10943:SF1, 1 hit
Pfamⁱ	View protein in Pfam PF01851 PC_rep, 2 hits
PIRSFⁱ	PIRSF015965 26S_Psome_Rpn1, 1 hit
SUPFAMⁱ	SSF48371 SSF48371, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PSMD2_HUMAN
Accessionⁱ	Q13200Primary (citable) accession number: Q13200 Secondary accession number(s): B4DX07 Q96I12
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	July 15, 1999
	Last modified:	November 7, 2018
	This is version 193 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human chromosome 3
Human chromosome 3: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q13200 (PSMD2_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

26S proteasome non-ATPase regulatory subunit 2

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytosol

Extracellular region or secreted

Nucleus

Other locations

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Compositional bias

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ