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Protein

LIM domain kinase 1

Gene

LIMK1

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

Functioni

Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop. LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin-2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and stabilizing the actin cytoskeleton. In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation. Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly. Stimulates axonal outgrowth and may be involved in brain development. Isoform 3 has a dominant negative effect on actin cytoskeletal changes. Required for atypical chemokine receptor ACKR2-induced phosphorylation of cofilin (CFL1).8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei368ATPPROSITE-ProRule annotation1
Active sitei460By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi345 – 353ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • heat shock protein binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: Ensembl
  • protein kinase activity Source: ProtInc
  • protein serine/threonine kinase activity Source: GO_Central

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-399954 Sema3A PAK dependent Axon repulsion
R-HSA-416572 Sema4D induced cell migration and growth-cone collapse
R-HSA-5627117 RHO GTPases Activate ROCKs
R-HSA-5627123 RHO GTPases activate PAKs
SignaLinkiP53667
SIGNORiP53667

Names & Taxonomyi

Protein namesi
Recommended name:
LIM domain kinase 1 (EC:2.7.11.1)
Short name:
LIMK-1
Gene namesi
Name:LIMK1
Synonyms:LIMK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000106683.14
HGNCiHGNC:6613 LIMK1
MIMi601329 gene
neXtProtiNX_P53667

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

Cell projection, Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

LIMK1 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi84C → S: Enhances actin aggregation. 1 Publication1
Mutagenesisi177 – 178GL → EA: Enhances actin aggregation. 1 Publication2
Mutagenesisi460D → N: Abrogates kinase activity. 1 Publication1
Mutagenesisi496 – 506Missing : Reduces actin aggregation. 1 PublicationAdd BLAST11
Mutagenesisi503 – 505RKK → GAA: Abolishes kinase activity. 1 Publication3
Mutagenesisi508T → A: Abolishes activation by ROCK1. 2 Publications1
Mutagenesisi508T → EE: Enhances kinase activity. 2 Publications1
Mutagenesisi508T → V or E: Reduces kinase activity. 2 Publications1

Keywords - Diseasei

Williams-Beuren syndrome

Organism-specific databases

DisGeNETi3984
MalaCardsiLIMK1
OpenTargetsiENSG00000106683
Orphaneti904 Williams syndrome
PharmGKBiPA30386

Chemistry databases

ChEMBLiCHEMBL3836
DrugBankiDB08912 Dabrafenib
GuidetoPHARMACOLOGYi2054

Polymorphism and mutation databases

BioMutaiLIMK1
DMDMi90185240

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000758031 – 647LIM domain kinase 1Add BLAST647

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei210PhosphoserineCombined sources1
Modified residuei229PhosphothreonineCombined sources1
Modified residuei298PhosphoserineCombined sources1
Modified residuei302PhosphoserineCombined sources1
Modified residuei307PhosphoserineCombined sources1
Modified residuei310PhosphoserineCombined sources1
Modified residuei323Phosphoserine; by MAPKAPK21 Publication1
Modified residuei337PhosphoserineCombined sources1
Modified residuei508Phosphothreonine; by ROCK1 and PAK14 Publications1

Post-translational modificationi

Autophosphorylated (By similarity). Phosphorylated on Thr-508 by ROCK1 and PAK1, resulting in activation. Phosphorylated by PAK4 which increases the ability of LIMK1 to phosphorylate cofilin. Phosphorylated at Ser-323 by MAPKAPK2 during activation of VEGFA-induced signaling, which results in activation of LIMK1 and promotion of actin reorganization, cell migration, and tubule formation of endothelial cells. Dephosphorylated and inactivated by SSH1. Phosphorylated by CDC42BP.By similarity7 Publications
Ubiquitinated. 'Lys-48'-linked polyubiquitination by RNF6 leads to proteasomal degradation through the 26S proteasome, modulating LIMK1 levels in the growth cone and its effect on axonal outgrowth. Also polyubiquitinated by RLIM (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP53667
MaxQBiP53667
PaxDbiP53667
PeptideAtlasiP53667
PRIDEiP53667
ProteomicsDBi56598
56599 [P53667-2]
56600 [P53667-3]
56601 [P53667-4]

PTM databases

iPTMnetiP53667
PhosphoSitePlusiP53667
SwissPalmiP53667

Expressioni

Tissue specificityi

Highest expression in both adult and fetal nervous system. Detected ubiquitously throughout the different regions of adult brain, with highest levels in the cerebral cortex. Expressed to a lesser extent in heart and skeletal muscle.

Gene expression databases

BgeeiENSG00000106683 Expressed in 125 organ(s), highest expression level in anterior cingulate cortex
CleanExiHS_LIMK1
ExpressionAtlasiP53667 baseline and differential
GenevisibleiP53667 HS

Organism-specific databases

HPAiHPA028064
HPA028516

Interactioni

Subunit structurei

Interacts (via LIM domain) with the cytoplasmic domain of NRG1. Interacts with NISCH. Interacts with RLIM and RNF6 (By similarity). Self-associates to form homodimers (PubMed:10196227). Interacts with HSP90AA1; this interaction promotes LIMK1 dimerization and subsequent transphosphorylation (PubMed:16641196). Interacts with CDKN1C (PubMed:14530263). Interacts with SSH1 (PubMed:15660133). Interacts with ROCK1 (PubMed:10436159, PubMed:10652353). Interacts (via LIM zinc-binding domains) with FAM89B/LRAP25 (via LRR repeat). Forms a tripartite complex with CDC42BPA, CDC42BPB and FAM89B/LRAP25 (By similarity).By similarity6 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi110172, 40 interactors
DIPiDIP-31605N
IntActiP53667, 41 interactors
MINTiP53667
STRINGi9606.ENSP00000336740

Chemistry databases

BindingDBiP53667

Structurei

Secondary structure

1647
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP53667
SMRiP53667
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53667

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 75LIM zinc-binding 1PROSITE-ProRule annotationAdd BLAST51
Domaini84 – 137LIM zinc-binding 2PROSITE-ProRule annotationAdd BLAST54
Domaini165 – 258PDZPROSITE-ProRule annotationAdd BLAST94
Domaini339 – 604Protein kinasePROSITE-ProRule annotationAdd BLAST266

Sequence similaritiesi

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiENOG410IEZ9 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00530000063025
HOGENOMiHOG000013121
HOVERGENiHBG052328
InParanoidiP53667
KOiK05743
PhylomeDBiP53667
TreeFamiTF318014

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR001478 PDZ
IPR036034 PDZ_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR001781 Znf_LIM
PfamiView protein in Pfam
PF00412 LIM, 2 hits
PF00595 PDZ, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00132 LIM, 2 hits
SM00228 PDZ, 1 hit
SUPFAMiSSF50156 SSF50156, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00478 LIM_DOMAIN_1, 2 hits
PS50023 LIM_DOMAIN_2, 2 hits
PS50106 PDZ, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit

Sequences (4+)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P53667-1) [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
MRLTLLCCTW REERMGEEGS ELPVCASCGQ RIYDGQYLQA LNADWHADCF
60 70 80 90 100
RCCDCSASLS HQYYEKDGQL FCKKDYWARY GESCHGCSEQ ITKGLVMVAG
110 120 130 140 150
ELKYHPECFI CLTCGTFIGD GDTYTLVEHS KLYCGHCYYQ TVVTPVIEQI
160 170 180 190 200
LPDSPGSHLP HTVTLVSIPA SSHGKRGLSV SIDPPHGPPG CGTEHSHTVR
210 220 230 240 250
VQGVDPGCMS PDVKNSIHVG DRILEINGTP IRNVPLDEID LLIQETSRLL
260 270 280 290 300
QLTLEHDPHD TLGHGLGPET SPLSSPAYTP SGEAGSSARQ KPVLRSCSID
310 320 330 340 350
RSPGAGSLGS PASQRKDLGR SESLRVVCRP HRIFRPSDLI HGEVLGKGCF
360 370 380 390 400
GQAIKVTHRE TGEVMVMKEL IRFDEETQRT FLKEVKVMRC LEHPNVLKFI
410 420 430 440 450
GVLYKDKRLN FITEYIKGGT LRGIIKSMDS QYPWSQRVSF AKDIASGMAY
460 470 480 490 500
LHSMNIIHRD LNSHNCLVRE NKNVVVADFG LARLMVDEKT QPEGLRSLKK
510 520 530 540 550
PDRKKRYTVV GNPYWMAPEM INGRSYDEKV DVFSFGIVLC EIIGRVNADP
560 570 580 590 600
DYLPRTMDFG LNVRGFLDRY CPPNCPPSFF PITVRCCDLD PEKRPSFVKL
610 620 630 640
EHWLETLRMH LAGHLPLGPQ LEQLDRGFWE TYRRGESGLP AHPEVPD
Length:647
Mass (Da):72,585
Last modified:March 7, 2006 - v3
Checksum:i9838BEFBE7006447
GO
Isoform 2 (identifier: P53667-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: Missing.

Show »
Length:633
Mass (Da):70,793
Checksum:iEAF0A3B93916D9FA
GO
Isoform 3 (identifier: P53667-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     294-305: LRSCSIDRSPGA → FARTWVALSPSA
     306-647: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:305
Mass (Da):33,373
Checksum:i65FEF49849CCA142
GO
Isoform 4 (identifier: P53667-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: MRLTLLCCTWREERMGEEGSELPVCASCGQRIYDGQYLQALNADWHADCFR → MLLASAPRRRRFLQRAK

Note: No experimental confirmation available.
Show »
Length:613
Mass (Da):68,729
Checksum:iA78F41C1313E9CEE
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PC47E9PC47_HUMAN
LIM domain kinase 1
LIMK1
677Annotation score:

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042246190G → A1 PublicationCorresponds to variant dbSNP:rs35827364Ensembl.1
Natural variantiVAR_042247247S → N1 PublicationCorresponds to variant dbSNP:rs55661242Ensembl.1
Natural variantiVAR_042248422R → Q1 PublicationCorresponds to variant dbSNP:rs55679316Ensembl.1
Natural variantiVAR_050148580F → Y2 PublicationsCorresponds to variant dbSNP:rs178412Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0433311 – 51MRLTL…ADCFR → MLLASAPRRRRFLQRAK in isoform 4. 1 PublicationAdd BLAST51
Alternative sequenceiVSP_0031251 – 14Missing in isoform 2. CuratedAdd BLAST14
Alternative sequenceiVSP_003126294 – 305LRSCS…RSPGA → FARTWVALSPSA in isoform 3. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_003127306 – 647Missing in isoform 3. 1 PublicationAdd BLAST342

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26309 mRNA Translation: BAA05371.1
U62293 Genomic DNA Translation: AAB17545.1
U62293 Genomic DNA Translation: AAB17546.1
U63721 Genomic DNA Translation: AAC13885.1
U63721 Genomic DNA Translation: AAC13886.1
AF134379 mRNA Translation: AAD25742.1
AK300382 mRNA Translation: BAH13274.1
AC005056 Genomic DNA No translation available.
AC005057 Genomic DNA Translation: AAS07438.1
CH471200 Genomic DNA Translation: EAW69620.1
CH471200 Genomic DNA Translation: EAW69621.1
CH471200 Genomic DNA Translation: EAW69622.1
CH471200 Genomic DNA Translation: EAW69623.1
CCDSiCCDS5563.1 [P53667-1]
CCDS56491.1 [P53667-4]
PIRiJP0078
RefSeqiNP_001191355.1, NM_001204426.1 [P53667-4]
NP_002305.1, NM_002314.3 [P53667-1]
UniGeneiHs.647035

Genome annotation databases

EnsembliENST00000336180; ENSP00000336740; ENSG00000106683 [P53667-1]
ENST00000435201; ENSP00000414606; ENSG00000106683 [P53667-3]
ENST00000538333; ENSP00000444452; ENSG00000106683 [P53667-4]
GeneIDi3984
KEGGihsa:3984
UCSCiuc003uaa.3 human [P53667-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26309 mRNA Translation: BAA05371.1
U62293 Genomic DNA Translation: AAB17545.1
U62293 Genomic DNA Translation: AAB17546.1
U63721 Genomic DNA Translation: AAC13885.1
U63721 Genomic DNA Translation: AAC13886.1
AF134379 mRNA Translation: AAD25742.1
AK300382 mRNA Translation: BAH13274.1
AC005056 Genomic DNA No translation available.
AC005057 Genomic DNA Translation: AAS07438.1
CH471200 Genomic DNA Translation: EAW69620.1
CH471200 Genomic DNA Translation: EAW69621.1
CH471200 Genomic DNA Translation: EAW69622.1
CH471200 Genomic DNA Translation: EAW69623.1
CCDSiCCDS5563.1 [P53667-1]
CCDS56491.1 [P53667-4]
PIRiJP0078
RefSeqiNP_001191355.1, NM_001204426.1 [P53667-4]
NP_002305.1, NM_002314.3 [P53667-1]
UniGeneiHs.647035

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3S95X-ray1.65A/B330-637[»]
5HVJX-ray2.20A/B329-638[»]
5HVKX-ray3.50A/C329-638[»]
5L6WX-ray2.53L330-637[»]
5NXCX-ray2.25L330-637[»]
ProteinModelPortaliP53667
SMRiP53667
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110172, 40 interactors
DIPiDIP-31605N
IntActiP53667, 41 interactors
MINTiP53667
STRINGi9606.ENSP00000336740

Chemistry databases

BindingDBiP53667
ChEMBLiCHEMBL3836
DrugBankiDB08912 Dabrafenib
GuidetoPHARMACOLOGYi2054

PTM databases

iPTMnetiP53667
PhosphoSitePlusiP53667
SwissPalmiP53667

Polymorphism and mutation databases

BioMutaiLIMK1
DMDMi90185240

Proteomic databases

EPDiP53667
MaxQBiP53667
PaxDbiP53667
PeptideAtlasiP53667
PRIDEiP53667
ProteomicsDBi56598
56599 [P53667-2]
56600 [P53667-3]
56601 [P53667-4]

Protocols and materials databases

DNASUi3984
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336180; ENSP00000336740; ENSG00000106683 [P53667-1]
ENST00000435201; ENSP00000414606; ENSG00000106683 [P53667-3]
ENST00000538333; ENSP00000444452; ENSG00000106683 [P53667-4]
GeneIDi3984
KEGGihsa:3984
UCSCiuc003uaa.3 human [P53667-1]

Organism-specific databases

CTDi3984
DisGeNETi3984
EuPathDBiHostDB:ENSG00000106683.14
GeneCardsiLIMK1
HGNCiHGNC:6613 LIMK1
HPAiHPA028064
HPA028516
MalaCardsiLIMK1
MIMi601329 gene
neXtProtiNX_P53667
OpenTargetsiENSG00000106683
Orphaneti904 Williams syndrome
PharmGKBiPA30386
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEZ9 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00530000063025
HOGENOMiHOG000013121
HOVERGENiHBG052328
InParanoidiP53667
KOiK05743
PhylomeDBiP53667
TreeFamiTF318014

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-399954 Sema3A PAK dependent Axon repulsion
R-HSA-416572 Sema4D induced cell migration and growth-cone collapse
R-HSA-5627117 RHO GTPases Activate ROCKs
R-HSA-5627123 RHO GTPases activate PAKs
SignaLinkiP53667
SIGNORiP53667

Miscellaneous databases

ChiTaRSiLIMK1 human
EvolutionaryTraceiP53667
GeneWikiiLIMK1
GenomeRNAii3984
PROiPR:P53667
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106683 Expressed in 125 organ(s), highest expression level in anterior cingulate cortex
CleanExiHS_LIMK1
ExpressionAtlasiP53667 baseline and differential
GenevisibleiP53667 HS

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR001478 PDZ
IPR036034 PDZ_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR001781 Znf_LIM
PfamiView protein in Pfam
PF00412 LIM, 2 hits
PF00595 PDZ, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00132 LIM, 2 hits
SM00228 PDZ, 1 hit
SUPFAMiSSF50156 SSF50156, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00478 LIM_DOMAIN_1, 2 hits
PS50023 LIM_DOMAIN_2, 2 hits
PS50106 PDZ, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiLIMK1_HUMAN
AccessioniPrimary (citable) accession number: P53667
Secondary accession number(s): B7Z6I8
, D3DXF4, D3DXF5, O15283, Q15820, Q15821, Q75MU3, Q9Y5Q1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 7, 2006
Last modified: September 12, 2018
This is version 198 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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