Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

26S proteasome non-ATPase regulatory subunit 11

Gene

PSMD11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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. In the complex, PSMD11 is required for proteasome assembly. Plays a key role in increased proteasome activity in embryonic stem cells (ESCs): its high expression in ESCs promotes enhanced assembly of the 26S proteasome, followed by higher proteasome activity.2 Publications

GO - Molecular functioni

  • structural molecule activity Source: GO_Central

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-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

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 11
Alternative name(s):
26S proteasome regulatory subunit RPN6
26S proteasome regulatory subunit S9
26S proteasome regulatory subunit p44.5
Gene namesi
Name:PSMD11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000108671.9
HGNCiHGNC:9556 PSMD11
MIMi604449 gene
neXtProtiNX_O00231

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi14S → A: Does not affect phosphorylation by AMPK; when associated with A-79 and A-272. 1 Publication1
Mutagenesisi79S → A: Does not affect phosphorylation by AMPK; when associated with A-14 and A-272. 1 Publication1
Mutagenesisi272S → A: Does not affect phosphorylation by AMPK; when associated with A14- and A-79. 1 Publication1

Organism-specific databases

DisGeNETi5717
OpenTargetsiENSG00000108671
PharmGKBiPA33902

Chemistry databases

ChEMBLiCHEMBL2364701

Polymorphism and mutation databases

BioMutaiPSMD11

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00001738572 – 42226S proteasome non-ATPase regulatory subunit 11Add BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei14PhosphoserineCombined sources1
Modified residuei23PhosphoserineCombined sources1
Cross-linki274Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

Phosphorylated by AMPK.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO00231
MaxQBiO00231
PaxDbiO00231
PeptideAtlasiO00231
PRIDEiO00231
ProteomicsDBi47796

2D gel databases

OGPiO00231

PTM databases

iPTMnetiO00231
PhosphoSitePlusiO00231
SwissPalmiO00231

Expressioni

Tissue specificityi

Highly expressed in embryonic stem cells (ESCs). Expression decreases as ESCs differentiate.1 Publication

Inductioni

By FOXO4; expression in embryonic stem cells (ESCs) is mediated by FOXO4.1 Publication

Gene expression databases

BgeeiENSG00000108671 Expressed in 232 organ(s), highest expression level in testis
CleanExiHS_PSMD11
ExpressionAtlasiO00231 baseline and differential
GenevisibleiO00231 HS

Organism-specific databases

HPAiHPA042275
HPA067433

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 including PSMD11, a base containing 6 ATPases and few additional components.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PRMT6Q96LA82EBI-357816,EBI-912440

Protein-protein interaction databases

BioGridi111689, 156 interactors
CORUMiO00231
IntActiO00231, 70 interactors
MINTiO00231
STRINGi9606.ENSP00000261712

Structurei

3D structure databases

ProteinModelPortaliO00231
SMRiO00231
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini224 – 392PCIPROSITE-ProRule annotationAdd BLAST169

Sequence similaritiesi

Belongs to the proteasome subunit S9 family.Curated

Phylogenomic databases

eggNOGiKOG1463 Eukaryota
COG5159 LUCA
GeneTreeiENSGT00530000063301
HOGENOMiHOG000210093
HOVERGENiHBG053738
InParanoidiO00231
KOiK03036
OMAiDKVFYGV
OrthoDBiEOG091G0B4C
PhylomeDBiO00231
TreeFamiTF106230

Family and domain databases

InterProiView protein in InterPro
IPR000717 PCI_dom
IPR035295 PSMD11
IPR011990 TPR-like_helical_dom_sf
IPR036390 WH_DNA-bd_sf
PANTHERiPTHR10678:SF6 PTHR10678:SF6, 1 hit
PfamiView protein in Pfam
PF01399 PCI, 1 hit
SMARTiView protein in SMART
SM00088 PINT, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF48452 SSF48452, 1 hit
PROSITEiView protein in PROSITE
PS50250 PCI, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O00231-1) [UniParc]FASTAAdd 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
MAAAAVVEFQ RAQSLLSTDR EASIDILHSI VKRDIQENDE EAVQVKEQSI
60 70 80 90 100
LELGSLLAKT GQAAELGGLL KYVRPFLNSI SKAKAARLVR SLLDLFLDME
110 120 130 140 150
AATGQEVELC LECIEWAKSE KRTFLRQALE ARLVSLYFDT KRYQEALHLG
160 170 180 190 200
SQLLRELKKM DDKALLVEVQ LLESKTYHAL SNLPKARAAL TSARTTANAI
210 220 230 240 250
YCPPKLQATL DMQSGIIHAA EEKDWKTAYS YFYEAFEGYD SIDSPKAITS
260 270 280 290 300
LKYMLLCKIM LNTPEDVQAL VSGKLALRYA GRQTEALKCV AQASKNRSLA
310 320 330 340 350
DFEKALTDYR AELRDDPIIS THLAKLYDNL LEQNLIRVIE PFSRVQIEHI
360 370 380 390 400
SSLIKLSKAD VERKLSQMIL DKKFHGILDQ GEGVLIIFDE PPVDKTYEAA
410 420
LETIQNMSKV VDSLYNKAKK LT
Length:422
Mass (Da):47,464
Last modified:January 23, 2007 - v3
Checksum:iCE113054CBEBDB05
GO
Isoform 2 (identifier: O00231-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     375-375: H → HA

Note: No experimental confirmation available.
Show »
Length:423
Mass (Da):47,535
Checksum:iBDE786518637385D
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3QS13J3QS13_HUMAN
26S proteasome non-ATPase regulator...
PSMD11
90Annotation score:
J3KSW3J3KSW3_HUMAN
26S proteasome non-ATPase regulator...
PSMD11
45Annotation score:
J3QRY4J3QRY4_HUMAN
26S proteasome non-ATPase regulator...
PSMD11
187Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti113C → S in AAB58732 (PubMed:9119060).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_044400375H → HA in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001212 mRNA Translation: AAB58732.1
AB003102 mRNA Translation: BAA19748.1
AK290602 mRNA Translation: BAF83291.1
AK223196 mRNA Translation: BAD96916.1
CH471147 Genomic DNA Translation: EAW80229.1
CH471147 Genomic DNA Translation: EAW80230.1
BC000437 mRNA Translation: AAH00437.1
BC004430 mRNA Translation: AAH04430.1
CCDSiCCDS11272.1 [O00231-1]
PIRiJC6524
RefSeqiNP_001257411.1, NM_001270482.1 [O00231-1]
NP_002806.2, NM_002815.3 [O00231-1]
UniGeneiHs.443379

Genome annotation databases

EnsembliENST00000261712; ENSP00000261712; ENSG00000108671 [O00231-1]
ENST00000457654; ENSP00000393185; ENSG00000108671 [O00231-1]
GeneIDi5717
KEGGihsa:5717
UCSCiuc002hhm.5 human [O00231-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001212 mRNA Translation: AAB58732.1
AB003102 mRNA Translation: BAA19748.1
AK290602 mRNA Translation: BAF83291.1
AK223196 mRNA Translation: BAD96916.1
CH471147 Genomic DNA Translation: EAW80229.1
CH471147 Genomic DNA Translation: EAW80230.1
BC000437 mRNA Translation: AAH00437.1
BC004430 mRNA Translation: AAH04430.1
CCDSiCCDS11272.1 [O00231-1]
PIRiJC6524
RefSeqiNP_001257411.1, NM_001270482.1 [O00231-1]
NP_002806.2, NM_002815.3 [O00231-1]
UniGeneiHs.443379

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GJQelectron microscopy4.50Q1-422[»]
5GJRelectron microscopy3.504/Q1-422[»]
5L4Kelectron microscopy4.50Q1-422[»]
5LN3electron microscopy6.80Q1-422[»]
5M32electron microscopy3.80l1-422[»]
5T0Celectron microscopy3.80AX/BX1-422[»]
5T0Gelectron microscopy4.40X1-422[»]
5T0Helectron microscopy6.80X1-422[»]
5T0Ielectron microscopy8.00X1-422[»]
5T0Jelectron microscopy8.00X1-422[»]
5VFPelectron microscopy4.20X43-422[»]
5VFQelectron microscopy4.20X43-422[»]
5VFRelectron microscopy4.90X43-422[»]
5VFSelectron microscopy3.60X43-422[»]
5VFTelectron microscopy7.00X43-422[»]
5VFUelectron microscopy5.80X43-422[»]
5VGZelectron microscopy3.70X38-422[»]
5VHFelectron microscopy5.70X38-422[»]
5VHHelectron microscopy6.10X38-422[»]
5VHIelectron microscopy6.80X38-422[»]
5VHSelectron microscopy8.80X38-422[»]
ProteinModelPortaliO00231
SMRiO00231
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111689, 156 interactors
CORUMiO00231
IntActiO00231, 70 interactors
MINTiO00231
STRINGi9606.ENSP00000261712

Chemistry databases

ChEMBLiCHEMBL2364701

PTM databases

iPTMnetiO00231
PhosphoSitePlusiO00231
SwissPalmiO00231

Polymorphism and mutation databases

BioMutaiPSMD11

2D gel databases

OGPiO00231

Proteomic databases

EPDiO00231
MaxQBiO00231
PaxDbiO00231
PeptideAtlasiO00231
PRIDEiO00231
ProteomicsDBi47796

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261712; ENSP00000261712; ENSG00000108671 [O00231-1]
ENST00000457654; ENSP00000393185; ENSG00000108671 [O00231-1]
GeneIDi5717
KEGGihsa:5717
UCSCiuc002hhm.5 human [O00231-1]

Organism-specific databases

CTDi5717
DisGeNETi5717
EuPathDBiHostDB:ENSG00000108671.9
GeneCardsiPSMD11
HGNCiHGNC:9556 PSMD11
HPAiHPA042275
HPA067433
MIMi604449 gene
neXtProtiNX_O00231
OpenTargetsiENSG00000108671
PharmGKBiPA33902
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1463 Eukaryota
COG5159 LUCA
GeneTreeiENSGT00530000063301
HOGENOMiHOG000210093
HOVERGENiHBG053738
InParanoidiO00231
KOiK03036
OMAiDKVFYGV
OrthoDBiEOG091G0B4C
PhylomeDBiO00231
TreeFamiTF106230

Enzyme and pathway databases

ReactomeiR-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

ChiTaRSiPSMD11 human
GeneWikiiPSMD11
GenomeRNAii5717
PROiPR:O00231
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000108671 Expressed in 232 organ(s), highest expression level in testis
CleanExiHS_PSMD11
ExpressionAtlasiO00231 baseline and differential
GenevisibleiO00231 HS

Family and domain databases

InterProiView protein in InterPro
IPR000717 PCI_dom
IPR035295 PSMD11
IPR011990 TPR-like_helical_dom_sf
IPR036390 WH_DNA-bd_sf
PANTHERiPTHR10678:SF6 PTHR10678:SF6, 1 hit
PfamiView protein in Pfam
PF01399 PCI, 1 hit
SMARTiView protein in SMART
SM00088 PINT, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF48452 SSF48452, 1 hit
PROSITEiView protein in PROSITE
PS50250 PCI, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPSD11_HUMAN
AccessioniPrimary (citable) accession number: O00231
Secondary accession number(s): A8K3I7
, E1P663, O00495, Q53FT5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 177 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

  1. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again