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Protein

Serine/threonine-protein kinase 24

Gene

STK24

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase that acts on both serine and threonine residues and promotes apoptosis in response to stress stimuli and caspase activation. Mediates oxidative-stress-induced cell death by modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during oxidative stress. Plays a role in a staurosporine-induced caspase-independent apoptotic pathway by regulating the nuclear translocation of AIFM1 and ENDOG and the DNase activity associated with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its kinase activity. Regulates cellular migration with alteration of PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and inhibits its activity and may regulate PXN phosphorylation through PTPN12. May act as a key regulator of axon regeneration in the optic nerve and radial nerve.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+1 Publication, Mn2+1 Publication, Co2+1 Publication, Zn2+1 Publication

Kineticsi

  1. KM=12.8 µM for manganese ions1 Publication
  2. KM=34.9 µM for cobalt ions1 Publication
  3. KM=22.7 µM for magnesium ions1 Publication
  4. KM=4.1 µM for zinc ions1 Publication
  1. Vmax=2623.1 pmol/min/mg enzyme for manganese ions1 Publication
  2. Vmax=1746.1 pmol/min/mg enzyme for cobalt ions1 Publication
  3. Vmax=129.1 pmol/min/mg enzyme for magnesium ions1 Publication
  4. Vmax=22.3 pmol/min/mg enzyme for zinc ions1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei65ATP1
Active sitei156Proton acceptorPROSITE-ProRule annotation1
Metal bindingi161Magnesium1
Metal bindingi174Magnesium1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi42 – 50ATP9
Nucleotide bindingi112 – 114ATP3

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • protein kinase activity Source: ProtInc
  • protein serine/threonine kinase activity Source: UniProtKB
  • receptor signaling protein serine/threonine kinase activity Source: GO_Central

GO - Biological processi

  • cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  • execution phase of apoptosis Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to oxidative stress Source: UniProtKB
  • mitotic cell cycle Source: GO_Central
  • negative regulation of cell migration Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of axon regeneration Source: UniProtKB
  • response to hydrogen peroxide Source: UniProtKB
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS02397-MONOMER.
ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
R-HSA-75153. Apoptotic execution phase.
SignaLinkiQ9Y6E0.
SIGNORiQ9Y6E0.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase 24 (EC:2.7.11.1)
Alternative name(s):
Mammalian STE20-like protein kinase 3
Short name:
MST-3
STE20-like kinase MST3
Cleaved into the following 2 chains:
Alternative name(s):
Mammalian STE20-like protein kinase 3 N-terminal
Short name:
MST3/N
Alternative name(s):
Mammalian STE20-like protein kinase 3 C-terminal
Short name:
MST3/C
Gene namesi
Name:STK24
Synonyms:MST3, STK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:11403. STK24.

Subcellular locationi

  • Cytoplasm
  • Nucleus
  • Membrane

  • Note: The truncated form (MST3/N) translocates to the nucleus. Colocalizes with STK38L in the membrane.

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB-SubCell
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi18T → A: Loss of phosphorylation by PKA. 1 Publication1
Mutagenesisi65K → A: Loss of activity and autophosphorylation. 1 Publication1
Mutagenesisi190T → A: Loss of activity and autophosphorylation. 1 Publication1
Mutagenesisi321D → N: Loss of proteolytic cleavage by caspases. 1 Publication1

Organism-specific databases

DisGeNETi8428.
OpenTargetsiENSG00000102572.
PharmGKBiPA36210.

Chemistry databases

ChEMBLiCHEMBL5082.
GuidetoPHARMACOLOGYi2217.

Polymorphism and mutation databases

DMDMi13626607.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000867111 – 443Serine/threonine-protein kinase 24Add BLAST443
ChainiPRO_00004136181 – 325Serine/threonine-protein kinase 24 36 kDa subunitAdd BLAST325
ChainiPRO_0000413619326 – 443Serine/threonine-protein kinase 24 12 kDa subunitAdd BLAST118
Isoform A (identifier: Q9Y6E0-2)
Initiator methionineiRemovedCombined sources

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei18Phosphothreonine; by PKA1 Publication1
Modified residuei190Phosphothreonine; by autocatalysisCombined sources3 Publications1
Modified residuei320PhosphoserineCombined sources1
Isoform A (identifier: Q9Y6E0-2)
Modified residuei2N-acetylalanineCombined sources1
Modified residuei4PhosphoserineCombined sources1

Post-translational modificationi

Proteolytically processed by caspases during apoptosis. Proteolytic cleavage results in kinase activation, nuclear translocation of the truncated form (MST3/N) and the induction of apoptosis.1 Publication
Isoform B is activated by phosphorylation by PKA. Oxidative stress induces phosphorylation. Activated by autophosphorylation at Thr-190 and phosphorylation at this site is essential for its function. Manganese, magnesium and cobalt-dependent autophosphorylation is mainly on threonine residues while zinc-dependent autophosphorylation is on both serine and threonine residues.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei325 – 326Cleavage; by caspase-3, caspase-7 and caspase-82

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9Y6E0.
PaxDbiQ9Y6E0.
PeptideAtlasiQ9Y6E0.
PRIDEiQ9Y6E0.

PTM databases

iPTMnetiQ9Y6E0.
PhosphoSitePlusiQ9Y6E0.
SwissPalmiQ9Y6E0.

Expressioni

Tissue specificityi

Isoform A is ubiquitous. Isoform B is expressed in brain with high expression in hippocampus and cerebral cortex.

Gene expression databases

BgeeiENSG00000102572.
CleanExiHS_STK24.
HS_STK3.
ExpressionAtlasiQ9Y6E0. baseline and differential.
GenevisibleiQ9Y6E0. HS.

Organism-specific databases

HPAiHPA026435.
HPA026502.

Interactioni

Subunit structurei

Monomer. Interacts with CTTNBP2NL.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTTNBP2NLQ9P2B44EBI-740175,EBI-1774273
PDCD10Q9BUL87EBI-740175,EBI-740195
STRNO438153EBI-740175,EBI-1046642
TRAF3IP3Q9Y2282EBI-740175,EBI-765817

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi114011. 77 interactors.
DIPiDIP-40608N.
IntActiQ9Y6E0. 36 interactors.
MINTiMINT-3088034.
STRINGi9606.ENSP00000365730.

Chemistry databases

BindingDBiQ9Y6E0.

Structurei

Secondary structure

1443
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni24 – 27Combined sources4
Helixi32 – 34Combined sources3
Beta strandi36 – 44Combined sources9
Beta strandi46 – 55Combined sources10
Turni56 – 58Combined sources3
Beta strandi61 – 68Combined sources8
Turni69 – 71Combined sources3
Turni73 – 75Combined sources3
Helixi76 – 88Combined sources13
Beta strandi97 – 103Combined sources7
Beta strandi106 – 112Combined sources7
Beta strandi116 – 118Combined sources3
Helixi119 – 123Combined sources5
Beta strandi124 – 126Combined sources3
Helixi130 – 149Combined sources20
Helixi159 – 161Combined sources3
Beta strandi162 – 164Combined sources3
Beta strandi166 – 168Combined sources3
Beta strandi170 – 172Combined sources3
Beta strandi183 – 185Combined sources3
Beta strandi186 – 188Combined sources3
Helixi195 – 197Combined sources3
Helixi200 – 203Combined sources4
Helixi211 – 226Combined sources16
Turni230 – 233Combined sources4
Helixi236 – 245Combined sources10
Beta strandi253 – 255Combined sources3
Helixi257 – 266Combined sources10
Helixi271 – 273Combined sources3
Helixi277 – 280Combined sources4
Helixi284 – 289Combined sources6
Helixi293 – 296Combined sources4
Helixi297 – 309Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A7FX-ray1.55A27-315[»]
3A7GX-ray2.00A/B27-315[»]
3A7HX-ray1.96A/B27-315[»]
3A7IX-ray1.45A27-315[»]
3A7JX-ray1.50A27-315[»]
3CKWX-ray1.96A31-323[»]
3CKXX-ray2.70A31-323[»]
3ZHPX-ray2.90C/D31-301[»]
4O27X-ray3.19B30-309[»]
4QMLX-ray1.88A24-315[»]
4QMMX-ray1.85A24-315[»]
4QMNX-ray2.09A27-315[»]
4QMOX-ray1.90A24-315[»]
4QMPX-ray2.00A24-315[»]
4QMQX-ray1.77A24-315[»]
4QMSX-ray1.88A24-315[»]
4QMTX-ray1.50A24-315[»]
4QMUX-ray1.55A24-315[»]
4QMVX-ray2.40A24-315[»]
4QMWX-ray1.60A24-315[»]
4QMXX-ray1.88A24-315[»]
4QMYX-ray1.88A24-315[»]
4QMZX-ray1.88A24-315[»]
4QNAX-ray1.85A27-315[»]
4QO9X-ray2.20A/B24-315[»]
4U8ZX-ray1.63A24-310[»]
4W8DX-ray1.77A24-310[»]
4W8EX-ray1.79A24-311[»]
ProteinModelPortaliQ9Y6E0.
SMRiQ9Y6E0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y6E0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 286Protein kinasePROSITE-ProRule annotationAdd BLAST251

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi278 – 292Bipartite nuclear localization signalAdd BLAST15
Motifi335 – 386Nuclear export signal (NES)Add BLAST52

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0201. Eukaryota.
ENOG410XP9G. LUCA.
GeneTreeiENSGT00810000125395.
HOGENOMiHOG000234203.
HOVERGENiHBG108518.
InParanoidiQ9Y6E0.
KOiK08838.
OMAiRAQLWGL.
OrthoDBiEOG091G0F24.
PhylomeDBiQ9Y6E0.
TreeFamiTF354217.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

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

Isoform B (identifier: Q9Y6E0-1) [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
MDSRAQLWGL ALNKRRATLP HPGGSTNLKA DPEELFTKLE KIGKGSFGEV
60 70 80 90 100
FKGIDNRTQK VVAIKIIDLE EAEDEIEDIQ QEITVLSQCD SPYVTKYYGS
110 120 130 140 150
YLKDTKLWII MEYLGGGSAL DLLEPGPLDE TQIATILREI LKGLDYLHSE
160 170 180 190 200
KKIHRDIKAA NVLLSEHGEV KLADFGVAGQ LTDTQIKRNT FVGTPFWMAP
210 220 230 240 250
EVIKQSAYDS KADIWSLGIT AIELARGEPP HSELHPMKVL FLIPKNNPPT
260 270 280 290 300
LEGNYSKPLK EFVEACLNKE PSFRPTAKEL LKHKFILRNA KKTSYLTELI
310 320 330 340 350
DRYKRWKAEQ SHDDSSSEDS DAETDGQASG GSDSGDWIFT IREKDPKNLE
360 370 380 390 400
NGALQPSDLD RNKMKDIPKR PFSQCLSTII SPLFAELKEK SQACGGNLGS
410 420 430 440
IEELRGAIYL AEEACPGISD TMVAQLVQRL QRYSLSGGGT SSH
Length:443
Mass (Da):49,308
Last modified:November 1, 1999 - v1
Checksum:i4A9FF1F6B6A88A97
GO
Isoform A (identifier: Q9Y6E0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MDSRAQLWGLALNKRRATLPHPGGST → MAHSPVQSGLPGMQ

Show »
Length:431
Mass (Da):47,913
Checksum:i26D863FDFEDF90AD
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041148414A → V.2 PublicationsCorresponds to variant rs55953606dbSNPEnsembl.1
Natural variantiVAR_041149426L → I.1 PublicationCorresponds to variant rs55897869dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0048741 – 26MDSRA…PGGST → MAHSPVQSGLPGMQ in isoform A. 2 PublicationsAdd BLAST26

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF024636 mRNA. Translation: AAB82560.1.
AF083420 mRNA. Translation: AAD42039.1.
AL356423, AL137249 Genomic DNA. Translation: CAI13114.1.
AL137249, AL356423 Genomic DNA. Translation: CAI39453.1.
CH471085 Genomic DNA. Translation: EAX08986.1.
BC035578 mRNA. Translation: AAH35578.1.
CCDSiCCDS32001.1. [Q9Y6E0-2]
CCDS9488.1. [Q9Y6E0-1]
RefSeqiNP_001027467.2. NM_001032296.3. [Q9Y6E0-2]
NP_003567.2. NM_003576.4. [Q9Y6E0-1]
UniGeneiHs.508514.

Genome annotation databases

EnsembliENST00000376547; ENSP00000365730; ENSG00000102572. [Q9Y6E0-1]
ENST00000539966; ENSP00000442539; ENSG00000102572. [Q9Y6E0-2]
GeneIDi8428.
KEGGihsa:8428.
UCSCiuc001vnm.3. human. [Q9Y6E0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF024636 mRNA. Translation: AAB82560.1.
AF083420 mRNA. Translation: AAD42039.1.
AL356423, AL137249 Genomic DNA. Translation: CAI13114.1.
AL137249, AL356423 Genomic DNA. Translation: CAI39453.1.
CH471085 Genomic DNA. Translation: EAX08986.1.
BC035578 mRNA. Translation: AAH35578.1.
CCDSiCCDS32001.1. [Q9Y6E0-2]
CCDS9488.1. [Q9Y6E0-1]
RefSeqiNP_001027467.2. NM_001032296.3. [Q9Y6E0-2]
NP_003567.2. NM_003576.4. [Q9Y6E0-1]
UniGeneiHs.508514.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A7FX-ray1.55A27-315[»]
3A7GX-ray2.00A/B27-315[»]
3A7HX-ray1.96A/B27-315[»]
3A7IX-ray1.45A27-315[»]
3A7JX-ray1.50A27-315[»]
3CKWX-ray1.96A31-323[»]
3CKXX-ray2.70A31-323[»]
3ZHPX-ray2.90C/D31-301[»]
4O27X-ray3.19B30-309[»]
4QMLX-ray1.88A24-315[»]
4QMMX-ray1.85A24-315[»]
4QMNX-ray2.09A27-315[»]
4QMOX-ray1.90A24-315[»]
4QMPX-ray2.00A24-315[»]
4QMQX-ray1.77A24-315[»]
4QMSX-ray1.88A24-315[»]
4QMTX-ray1.50A24-315[»]
4QMUX-ray1.55A24-315[»]
4QMVX-ray2.40A24-315[»]
4QMWX-ray1.60A24-315[»]
4QMXX-ray1.88A24-315[»]
4QMYX-ray1.88A24-315[»]
4QMZX-ray1.88A24-315[»]
4QNAX-ray1.85A27-315[»]
4QO9X-ray2.20A/B24-315[»]
4U8ZX-ray1.63A24-310[»]
4W8DX-ray1.77A24-310[»]
4W8EX-ray1.79A24-311[»]
ProteinModelPortaliQ9Y6E0.
SMRiQ9Y6E0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114011. 77 interactors.
DIPiDIP-40608N.
IntActiQ9Y6E0. 36 interactors.
MINTiMINT-3088034.
STRINGi9606.ENSP00000365730.

Chemistry databases

BindingDBiQ9Y6E0.
ChEMBLiCHEMBL5082.
GuidetoPHARMACOLOGYi2217.

PTM databases

iPTMnetiQ9Y6E0.
PhosphoSitePlusiQ9Y6E0.
SwissPalmiQ9Y6E0.

Polymorphism and mutation databases

DMDMi13626607.

Proteomic databases

EPDiQ9Y6E0.
PaxDbiQ9Y6E0.
PeptideAtlasiQ9Y6E0.
PRIDEiQ9Y6E0.

Protocols and materials databases

DNASUi8428.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376547; ENSP00000365730; ENSG00000102572. [Q9Y6E0-1]
ENST00000539966; ENSP00000442539; ENSG00000102572. [Q9Y6E0-2]
GeneIDi8428.
KEGGihsa:8428.
UCSCiuc001vnm.3. human. [Q9Y6E0-1]

Organism-specific databases

CTDi8428.
DisGeNETi8428.
GeneCardsiSTK24.
HGNCiHGNC:11403. STK24.
HPAiHPA026435.
HPA026502.
MIMi604984. gene.
neXtProtiNX_Q9Y6E0.
OpenTargetsiENSG00000102572.
PharmGKBiPA36210.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0201. Eukaryota.
ENOG410XP9G. LUCA.
GeneTreeiENSGT00810000125395.
HOGENOMiHOG000234203.
HOVERGENiHBG108518.
InParanoidiQ9Y6E0.
KOiK08838.
OMAiRAQLWGL.
OrthoDBiEOG091G0F24.
PhylomeDBiQ9Y6E0.
TreeFamiTF354217.

Enzyme and pathway databases

BioCyciZFISH:HS02397-MONOMER.
ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
R-HSA-75153. Apoptotic execution phase.
SignaLinkiQ9Y6E0.
SIGNORiQ9Y6E0.

Miscellaneous databases

ChiTaRSiSTK24. human.
EvolutionaryTraceiQ9Y6E0.
GeneWikiiSTK24.
GenomeRNAii8428.
PROiQ9Y6E0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000102572.
CleanExiHS_STK24.
HS_STK3.
ExpressionAtlasiQ9Y6E0. baseline and differential.
GenevisibleiQ9Y6E0. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSTK24_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6E0
Secondary accession number(s): O14840, Q5JV92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 167 of the entry and version 1 of the sequence. [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 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.