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Protein

Endoribonuclease ZC3H12A

Gene

ZC3H12A

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

Functioni

Endoribonuclease involved in various biological functions such as cellular inflammatory response and immune homeostasis, glial differentiation of neuroprogenitor cells, cell death of cardiomyocytes, adipogenesis and angiogenesis. Functions as an endoribonuclease involved in mRNA decay (PubMed:19909337). Modulates the inflammatory response by promoting the degradation of a set of translationally active cytokine-induced inflammation-related mRNAs, such as IL6 and IL12B, during the early phase of inflammation (PubMed:26320658). Prevents aberrant T-cell-mediated immune reaction by degradation of multiple mRNAs controlling T-cell activation, such as those encoding cytokines (IL6 and IL2), cell surface receptors (ICOS, TNFRSF4 and TNFR2) and transcription factor (REL) (By similarity). Inhibits cooperatively with ZC3H12A the differentiation of helper T cells Th17 in lungs. They repress target mRNA encoding the Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A (By similarity). Self regulates by destabilizing its own mRNA (By similarity). Cleaves mRNA harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-dependent manner (PubMed:19909337, PubMed:26320658, PubMed:26134560, PubMed:22561375). Plays a role in the inhibition of microRNAs (miRNAs) biogenesis (PubMed:22055188). Cleaves the terminal loop of a set of precursor miRNAs (pre-miRNAs) important for the regulation of the inflammatory response leading to their degradation, and thus preventing the biosynthesis of mature miRNAs (PubMed:22055188). Plays also a role in promoting angiogenesis in response to inflammatory cytokines by inhibiting the production of antiangiogenic microRNAs via its anti-dicer RNase activity (PubMed:24048733). Affects the overall ubiquitination of cellular proteins (By similarity). Positively regulates deubiquitinase activity promoting the cleavage at 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains on TNF receptor-associated factors (TRAFs), preventing JNK and NF-kappa-B signaling pathway activation, and hence negatively regulating macrophage-mediated inflammatory response and immune homeostasis (By similarity). Induces also deubiquitination of the transcription factor HIF1A, probably leading to its stabilization and nuclear import, thereby positively regulating the expression of proangiogenic HIF1A-targeted genes (PubMed:24048733). Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation through the deubiquitination of IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage (PubMed:25861989). Prevents stress granule (SGs) formation and promotes macrophage apoptosis under stress conditions, including arsenite-induced oxidative stress, heat shock and energy deprivation (By similarity). Plays a role in the regulation of macrophage polarization; promotes IL4-induced polarization of macrophages M1 into anti-inflammatory M2 state (By similarity). May also act as a transcription factor that regulates the expression of multiple genes involved in inflammatory response, angiogenesis, adipogenesis and apoptosis (PubMed:16574901, PubMed:18364357). Functions as a positive regulator of glial differentiation of neuroprogenitor cells through an amyloid precursor protein (APP)-dependent signaling pathway (PubMed:19185603). Attenuates septic myocardial contractile dysfunction in response to lipopolysaccharide (LPS) by reducing I-kappa-B-kinase (IKK)-mediated NF-kappa-B activation, and hence myocardial proinflammatory cytokine production (By similarity).By similarity10 Publications
(Microbial infection) Binds to Japanese encephalitis virus (JEV) and Dengue virus (DEN) RNAs.1 Publication
(Microbial infection) Exhibits antiviral activity against HIV-1 in lymphocytes by decreasing the abundance of HIV-1 viral RNA species.1 Publication

Caution

Was originally proposed to bind to DNA and act as transcription factor.1 Publication

Cofactori

Mg2+1 PublicationNote: Mg2+ is required for RNase activity (PubMed:22561375).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi226Magnesium1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri301 – 324C3H1-typeAdd BLAST24

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein, DNA-binding, Endonuclease, Hydrolase, Nuclease, Repressor, RNA-binding
Biological processAngiogenesis, Antiviral defense, Apoptosis, Differentiation, DNA damage, Immunity, Inflammatory response, Neurogenesis, Stress response, Transcription, Transcription regulation
LigandMagnesium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Endoribonuclease ZC3H12ACurated (EC:3.1.-.-1 Publication)
Alternative name(s):
Monocyte chemotactic protein-induced protein 11 Publication
Short name:
MCP-induced protein 11 Publication
Short name:
MCPIP-11 Publication
Regnase-11 Publication
Short name:
Reg1By similarity
Zinc finger CCCH domain-containing protein 12AImported
Gene namesi
Name:ZC3H12AImported
Synonyms:MCPIP1 Publication, MCPIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000163874.8
HGNCiHGNC:26259 ZC3H12A
MIMi610562 gene
neXtProtiNX_Q5D1E8

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, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Increased expression of ZC3H12A is associated with ischemic heart disease (PubMed:16574901).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi141D → N: Abolishes RNase activity. 1 Publication1
Mutagenesisi141D → N: Loss of pre-miRNA RNase activity. Attenuates strongly miRNA silencing activity. Loss of interleukin IL17A and IL6 mRNA instabilities. Reduces angiogenic differentiation. Loss of RNase activity on JEV and DEN viral RNAs and antiviral effects. Loss of HIV-1 antiviral activity. Loss of IL1B mRNA instability; when associated with A-226. 6 Publications1
Mutagenesisi144N → A: No change in RNase activity. 1 Publication1
Mutagenesisi157C → A: Does not inhibit antiviral effects. 1 Publication1
Mutagenesisi214R → A: Abolishes RNase activity. 1 Publication1
Mutagenesisi225D → A: Loss of pre-miRNA RNase activity, IL17A mRNA instability and antiviral effects; when associated with A-226. 3 Publications1
Mutagenesisi226D → A: Loss of pre-miRNA RNase activity, IL17A mRNA instability and antiviral effects; when associated with A-225. Loss of IL1B mRNA instability; when associated with N-141. 4 Publications1
Mutagenesisi306C → R: Loss of interleukin IL17A mRNA instability. Reduces weakly pre-miRNA RNase activity. Attenuates miRNA silencing activity. Does not inhibits binding to Japanese encephalitis virus (JEV) and dengue virus (DEN) RNAs and weakly attenuates antiviral effects. Loss of HIV-1 antiviral activity. 4 Publications1
Mutagenesisi311K → G: Inhibits transcriptional activity; when associated with G-312. 1 Publication1
Mutagenesisi312C → G: Inhibits transcriptional activity; when associated with G-311. 1 Publication1
Mutagenesisi317K → G: Inhibits transcriptional activity; when associated with G-318. 1 Publication1
Mutagenesisi318C → G: Inhibits transcriptional activity; when associated with G-317. 1 Publication1

Organism-specific databases

DisGeNETi80149
OpenTargetsiENSG00000163874
PharmGKBiPA142670537

Polymorphism and mutation databases

BioMutaiZC3H12A
DMDMi190479827

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003415121 – 599Endoribonuclease ZC3H12AAdd BLAST599

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei99PhosphoserineCombined sources1
Modified residuei344PhosphoserineCombined sources1
Modified residuei438PhosphoserineBy similarity1
Modified residuei442PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated by IRAK1; phosphorylation is necessary for subsequent phosphorylation by the I-kappa-B-kinase (IKK) complex. Phosphorylated by I-kappa-B-kinase (IKK) subunits IKBKB/IKKB and CHUK/IKKA at Ser-438 and Ser-442; these phosphorylations promote ubiquitin proteasome-mediated degradation of ZC3H12A and hence facilitates rapid and robust production of IL-6 mRNA in response to toll-like receptor (TLR) or IL-1 receptor stimuli (By similarity).By similarity
(Microbial infection) Rapidly degraded in activated T-cells in response to phorbol 13-acetate 12-myristate (PMA) during HIV-1 viral infection (PubMed:24191027).1 Publication
Ubiquitinated; ubiquitination is induced in response to interleukin IL1 receptor stimuli in a IKBKB/IKKB and IRAK1-dependent manner, leading to proteasome-mediated degradation (By similarity).By similarity
Proteolytically cleaved between Arg-111 and Arg-214 by MALT1 in activated T-cells; cleavage at Arg-111 is critical for promoting ZC3H12A degradation in response to T-cell receptor (TCR) stimulation, and hence is necessary for prolonging the stability of a set of mRNAs controlling T-cell activation and Th17 cell differentiation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ5D1E8
MaxQBiQ5D1E8
PaxDbiQ5D1E8
PeptideAtlasiQ5D1E8
PRIDEiQ5D1E8
ProteomicsDBi62741

PTM databases

iPTMnetiQ5D1E8
PhosphoSitePlusiQ5D1E8

Expressioni

Tissue specificityi

Expressed in heart, placenta, spleen, kidney, liver and lung (PubMed:19909337). Expressed in leukocytes (PubMed:19909337). Expressed in monocyte (PubMed:16574901).2 Publications

Inductioni

Up-regulated by the transcription factor ELK1 in a interleukin IL1B-dependent manner through activation of the NF-kappa-B and ERK signaling pathways (PubMed:19747262, PubMed:20137095, PubMed:22037600). Up-regulated by chemokine CCL2 in endothelial cells and in peripheral blood monocytes (PubMed:16574901, PubMed:18364357). Up-regulated in activated T lymphocytes (PubMed:23185455). Up-regulated by phorbol 12-myristate 13-acetate (PMA) in primary T lymphocytes (PubMed:19909337, PubMed:23185455). Up-regulated by interleukin IL17 in keratinocytes (PubMed:26320658). Up-regulated by lipopolysaccharide (LPS) (PubMed:19909337). Up-regulated by tumor necrosis factor TNF-alpha and interleukin IL1 in acute monocytic leukemia cell line THP-1 cells (PubMed:18178554, PubMed:19909337). Up-regulated by amyloid precursor protein (APP) (PubMed:19185603).10 Publications
(Microbial infection) Up-regulated in response to Japanese encephalitis virus (JEV) and dengue virus (DEN) infections (PubMed:23355615).1 Publication

Gene expression databases

BgeeiENSG00000163874 Expressed in 131 organ(s), highest expression level in right adrenal gland
CleanExiHS_ZC3H12A
ExpressionAtlasiQ5D1E8 baseline and differential
GenevisibleiQ5D1E8 HS

Organism-specific databases

HPAiHPA032052
HPA032053

Interactioni

Subunit structurei

Oligomer (PubMed:22055188, PubMed:23355615). Found in a deubiquitination complex with TANK, USP10 and ZC3H12A; this complex inhibits genotoxic stress- or interleukin-1-beta-mediated NF-kappaB activation by promoting IKBKG or TRAF6 deubiquitination (PubMed:25861989). Interacts with IKBKG; this interaction increases in response to DNA damage (PubMed:25861989). Interacts with TANK; this interaction increases in response to DNA damage and serves as a bridge to anchor both TANK and USP10 into a deubiquitinating complex (PubMed:25861989). Interacts with TRAF6; this interaction increases in response to DNA damage and is stimulated by TANK (PubMed:25861989). Interacts with USP10; this interaction increases in response to DNA damage and serves as a bridge to anchor both TANK and USP10 into a deubiquitinating complex (PubMed:25861989). Interacts with ZC3H12D (PubMed:26134560). Interacts with TNRC6A (PubMed:26134560). Interacts with IKBKB/IKKB (PubMed:22037600). Interacts with IKBKB/IKKB. Interacts with BTRC; the interaction occurs when ZC3H12A is phosphorylated in a IKBKB/IKKB-dependent manner (By similarity). Interacts with IRAK1; this interaction increases the interaction between ZC3H12A and IKBKB/IKKB (By similarity). Interacts with UPF1; this interaction occurs in a mRNA translationally active- and termination-dependent manner and is essential for ZC3H12A-mediated degradation of target mRNAs (By similarity). Associates with ribosomes (By similarity). Interacts with ubiquitin (By similarity).By similarity5 Publications
(Microbial infection) Oligomerization is necessary for antiviral activity (PubMed:23355615).1 Publication

Binary interactionsi

Protein-protein interaction databases

BioGridi123141, 23 interactors
CORUMiQ5D1E8
IntActiQ5D1E8, 16 interactors
MINTiQ5D1E8
STRINGi9606.ENSP00000362174

Structurei

Secondary structure

1599
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ5D1E8
SMRiQ5D1E8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 87Ubiquitin association domainBy similarityAdd BLAST46
Regioni81 – 150Necessary for interaction with TANK1 PublicationAdd BLAST70
Regioni112 – 297RNase1 PublicationAdd BLAST186
Regioni214 – 220RNA binding1 Publication7
Regioni301 – 457Necessary for interaction with ZC3H12D1 PublicationAdd BLAST157

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi458 – 536Pro-richSequence analysisAdd BLAST79

Domaini

The C3H1-type zinc finger domain and C-terminal region are necessary for pre-miRNA binding (PubMed:22055188). The C-terminal region and proline-rich domain are necessary for oligomerization (PubMed:22055188).1 Publication
(Microbial infection) The C3H1-type zinc finger domain is necessary for JEV and DEN viral RNA-binding and antiviral activity (PubMed:23355615).1 Publication

Sequence similaritiesi

Belongs to the ZC3H12 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri301 – 324C3H1-typeAdd BLAST24

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3777 Eukaryota
ENOG410ZNK1 LUCA
GeneTreeiENSGT00750000117218
HOGENOMiHOG000060218
HOVERGENiHBG108758
InParanoidiQ5D1E8
KOiK18668
OMAiFPPREYW
OrthoDBiEOG091G03B2
PhylomeDBiQ5D1E8
TreeFamiTF315783

Family and domain databases

InterProiView protein in InterPro
IPR021869 RNase_Zc3h12_NYN
PfamiView protein in Pfam
PF11977 RNase_Zc3h12a, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q5D1E8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGPCGEKPV LEASPTMSLW EFEDSHSRQG TPRPGQELAA EEASALELQM
60 70 80 90 100
KVDFFRKLGY SSTEIHSVLQ KLGVQADTNT VLGELVKHGT ATERERQTSP
110 120 130 140 150
DPCPQLPLVP RGGGTPKAPN LEPPLPEEEK EGSDLRPVVI DGSNVAMSHG
160 170 180 190 200
NKEVFSCRGI LLAVNWFLER GHTDITVFVP SWRKEQPRPD VPITDQHILR
210 220 230 240 250
ELEKKKILVF TPSRRVGGKR VVCYDDRFIV KLAYESDGIV VSNDTYRDLQ
260 270 280 290 300
GERQEWKRFI EERLLMYSFV NDKFMPPDDP LGRHGPSLDN FLRKKPLTLE
310 320 330 340 350
HRKQPCPYGR KCTYGIKCRF FHPERPSCPQ RSVADELRAN ALLSPPRAPS
360 370 380 390 400
KDKNGRRPSP SSQSSSLLTE SEQCSLDGKK LGAQASPGSR QEGLTQTYAP
410 420 430 440 450
SGRSLAPSGG SGSSFGPTDW LPQTLDSLPY VSQDCLDSGI GSLESQMSEL
460 470 480 490 500
WGVRGGGPGE PGPPRAPYTG YSPYGSELPA TAAFSAFGRA MGAGHFSVPA
510 520 530 540 550
DYPPAPPAFP PREYWSEPYP LPPPTSVLQE PPVQSPGAGR SPWGRAGSLA
560 570 580 590
KEQASVYTKL CGVFPPHLVE AVMGRFPQLL DPQQLAAEIL SYKSQHPSE
Length:599
Mass (Da):65,699
Last modified:February 5, 2008 - v1
Checksum:i9213139FA7DCA443
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
R4GN17R4GN17_HUMAN
Endoribonuclease ZC3H12A
ZC3H12A
131Annotation score:
A0A1W2PQC8A0A1W2PQC8_HUMAN
Endoribonuclease ZC3H12A
ZC3H12A
283Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti248D → G in CAG33645 (Ref. 3) Curated1
Sequence conflicti599E → D in CAG33645 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052968240V → M. Corresponds to variant dbSNP:rs16824179Ensembl.1
Natural variantiVAR_044082547G → D3 PublicationsCorresponds to variant dbSNP:rs17849897Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY920403 mRNA Translation: AAX14017.1
AK026884 mRNA Translation: BAB15581.1
CR457364 mRNA Translation: CAG33645.1
AL034379 Genomic DNA No translation available.
AL449284 Genomic DNA No translation available.
CH471059 Genomic DNA Translation: EAX07346.1
CH471059 Genomic DNA Translation: EAX07347.1
BC005001 mRNA Translation: AAH05001.1
CCDSiCCDS417.1
RefSeqiNP_001310479.1, NM_001323550.1
NP_079355.2, NM_025079.2
UniGeneiHs.656294

Genome annotation databases

EnsembliENST00000373087; ENSP00000362179; ENSG00000163874
GeneIDi80149
KEGGihsa:80149
UCSCiuc001cbb.5 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY920403 mRNA Translation: AAX14017.1
AK026884 mRNA Translation: BAB15581.1
CR457364 mRNA Translation: CAG33645.1
AL034379 Genomic DNA No translation available.
AL449284 Genomic DNA No translation available.
CH471059 Genomic DNA Translation: EAX07346.1
CH471059 Genomic DNA Translation: EAX07347.1
BC005001 mRNA Translation: AAH05001.1
CCDSiCCDS417.1
RefSeqiNP_001310479.1, NM_001323550.1
NP_079355.2, NM_025079.2
UniGeneiHs.656294

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3V32X-ray2.00A/B112-296[»]
3V33X-ray2.00A/B112-334[»]
3V34X-ray2.00A/B112-296[»]
ProteinModelPortaliQ5D1E8
SMRiQ5D1E8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123141, 23 interactors
CORUMiQ5D1E8
IntActiQ5D1E8, 16 interactors
MINTiQ5D1E8
STRINGi9606.ENSP00000362174

PTM databases

iPTMnetiQ5D1E8
PhosphoSitePlusiQ5D1E8

Polymorphism and mutation databases

BioMutaiZC3H12A
DMDMi190479827

Proteomic databases

EPDiQ5D1E8
MaxQBiQ5D1E8
PaxDbiQ5D1E8
PeptideAtlasiQ5D1E8
PRIDEiQ5D1E8
ProteomicsDBi62741

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373087; ENSP00000362179; ENSG00000163874
GeneIDi80149
KEGGihsa:80149
UCSCiuc001cbb.5 human

Organism-specific databases

CTDi80149
DisGeNETi80149
EuPathDBiHostDB:ENSG00000163874.8
GeneCardsiZC3H12A
HGNCiHGNC:26259 ZC3H12A
HPAiHPA032052
HPA032053
MIMi610562 gene
neXtProtiNX_Q5D1E8
OpenTargetsiENSG00000163874
PharmGKBiPA142670537
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3777 Eukaryota
ENOG410ZNK1 LUCA
GeneTreeiENSGT00750000117218
HOGENOMiHOG000060218
HOVERGENiHBG108758
InParanoidiQ5D1E8
KOiK18668
OMAiFPPREYW
OrthoDBiEOG091G03B2
PhylomeDBiQ5D1E8
TreeFamiTF315783

Miscellaneous databases

ChiTaRSiZC3H12A human
GenomeRNAii80149
PROiPR:Q5D1E8
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163874 Expressed in 131 organ(s), highest expression level in right adrenal gland
CleanExiHS_ZC3H12A
ExpressionAtlasiQ5D1E8 baseline and differential
GenevisibleiQ5D1E8 HS

Family and domain databases

InterProiView protein in InterPro
IPR021869 RNase_Zc3h12_NYN
PfamiView protein in Pfam
PF11977 RNase_Zc3h12a, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiZC12A_HUMAN
AccessioniPrimary (citable) accession number: Q5D1E8
Secondary accession number(s): D3DPT0, Q6I9Z1, Q9H5P1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: February 5, 2008
Last modified: October 10, 2018
This is version 92 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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