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Protein

Serine/threonine-protein kinase 3

Gene

STK3

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

Functioni

Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates NKX2-1 (By similarity). Phosphorylates NEK2 and plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosome, and its ability to phosphorylate CROCC and CEP250. In conjunction with SAV1, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation. Positively regulates RAF1 activation via suppression of the inhibitory phosphorylation of RAF1 on 'Ser-259'. Phosphorylates MOBKL1A and RASSF2. Phosphorylates MOBKL1B on 'Thr-74'. Acts cooperatively with MOBKL1B to activate STK38.By similarity10 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Inhibited by the C-terminal non-catalytic region. Activated by caspase-cleavage. Full activation also requires homodimerization and autophosphorylation of Thr-180, which are inhibited by the proto-oncogene product RAF1. Activated by RASSF1 which acts by preventing its dephosphorylation.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei56ATP1
Active sitei146Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi33 – 41ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • protein kinase activity Source: ProtInc
  • protein serine/threonine kinase activator activity Source: BHF-UCL
  • protein serine/threonine kinase activity Source: UniProtKB
  • receptor signaling protein serine/threonine kinase activity Source: GO_Central

GO - Biological processi

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:HS02575-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-2028269. Signaling by Hippo.
SignaLinkiQ13188.
SIGNORiQ13188.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase 3 (EC:2.7.11.1)
Alternative name(s):
Mammalian STE20-like protein kinase 2
Short name:
MST-2
STE20-like kinase MST2
Serine/threonine-protein kinase Krs-1
Cleaved into the following 2 chains:
Gene namesi
Name:STK3
Synonyms:KRS1, MST2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:11406. STK3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • nucleus Source: UniProtKB-SubCell
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi56K → R: Loss of activity. 1 Publication1
Mutagenesisi322D → N: Resistant to proteolytic cleavage. 1 Publication1

Organism-specific databases

DisGeNETi6788.
OpenTargetsiENSG00000104375.
PharmGKBiPA36213.

Chemistry databases

ChEMBLiCHEMBL4708.
GuidetoPHARMACOLOGYi2219.

Polymorphism and mutation databases

BioMutaiSTK3.
DMDMi46577700.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000866891 – 491Serine/threonine-protein kinase 3Add BLAST491
ChainiPRO_00004137131 – 322Serine/threonine-protein kinase 3 36kDa subunitAdd BLAST322
ChainiPRO_0000413714323 – 491Serine/threonine-protein kinase 3 20kDa subunitAdd BLAST169

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei15PhosphoserineCombined sources1
Modified residuei117Phosphothreonine; by PKB/AKT12 Publications1
Modified residuei180Phosphothreonine; by autocatalysisCurated1
Modified residuei316PhosphoserineCombined sources1
Modified residuei336PhosphothreonineCombined sources1
Modified residuei384Phosphothreonine; by PKB/AKT11 Publication1
Modified residuei385PhosphoserineCombined sources1
Modified residuei444PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation at Thr-117 and Thr-384 by PKB/AKT1, leads to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation, and increase in its binding to RAF1.3 Publications
Proteolytically cleaved by caspase-3 during apoptosis. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei322 – 323Cleavage; by caspase-32

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13188.
MaxQBiQ13188.
PaxDbiQ13188.
PeptideAtlasiQ13188.
PRIDEiQ13188.

2D gel databases

OGPiQ13188.

PTM databases

iPTMnetiQ13188.
PhosphoSitePlusiQ13188.

Miscellaneous databases

PMAP-CutDBQ13188.

Expressioni

Tissue specificityi

Expressed at high levels in adult kidney, skeletal and placenta tissues and at very low levels in adult heart, lung and brain tissues.1 Publication

Inductioni

Activity increases during mitosis.1 Publication

Gene expression databases

BgeeiENSG00000104375.
CleanExiHS_STK3.
ExpressionAtlasiQ13188. baseline and differential.
GenevisibleiQ13188. HS.

Organism-specific databases

HPAiCAB025316.
HPA007120.

Interactioni

Subunit structurei

Homodimer; mediated via the coiled-coil region. Interacts with NORE1, which inhibits autoactivation (By similarity). Interacts with and stabilizes SAV1. Interacts with RAF1, which prevents dimerization and phosphorylation. Interacts with RASSF1. Interacts (via SARAH domain) with isoform 1 of NEK2. Interacts with ESR1 only in the presence of SAV1. Interacts with PKB/AKT1. Forms a tripartite complex with MOBKL1B and STK38. Interacts with RASSF2 (via SARAH domain).By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FAM9BQ8IZU03EBI-992580,EBI-10175124
FLJ13057Q53SE73EBI-992580,EBI-10172181
GABARAPO951662EBI-992580,EBI-712001
GABARAPL1Q9H0R82EBI-992580,EBI-746969
GABARAPL2P605202EBI-992580,EBI-720116
GAD1Q992593EBI-992580,EBI-743184
MAP1LC3BQ9GZQ85EBI-992580,EBI-373144
MAP1LC3CQ9BXW42EBI-992580,EBI-2603996
MOB1BQ7L9L44EBI-992580,EBI-2558745
RASSF1Q9NS23-23EBI-992580,EBI-438698
RASSF2P5074913EBI-992580,EBI-960081
RASSF3Q86WH26EBI-992580,EBI-2845202
RASSF4Q9H2L58EBI-992580,EBI-2933362
RASSF5Q8WWW07EBI-992580,EBI-367390
SAV1Q9H4B617EBI-992580,EBI-1017775
SLMAPQ14BN46EBI-992580,EBI-1043216
STK4Q1304317EBI-992580,EBI-367376
TFPTG5E9B53EBI-992580,EBI-10178002
TRAF1Q130773EBI-992580,EBI-359224

GO - Molecular functioni

Protein-protein interaction databases

BioGridi112664. 89 interactors.
DIPiDIP-36128N.
IntActiQ13188. 74 interactors.
MINTiMINT-3027356.
STRINGi9606.ENSP00000390500.

Chemistry databases

BindingDBiQ13188.

Structurei

Secondary structure

1491
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 20Combined sources4
Helixi23 – 26Combined sources4
Beta strandi27 – 34Combined sources8
Beta strandi40 – 46Combined sources7
Turni47 – 49Combined sources3
Beta strandi52 – 58Combined sources7
Helixi64 – 76Combined sources13
Beta strandi85 – 91Combined sources7
Beta strandi94 – 100Combined sources7
Beta strandi103 – 106Combined sources4
Helixi107 – 114Combined sources8
Helixi120 – 139Combined sources20
Helixi149 – 151Combined sources3
Beta strandi152 – 154Combined sources3
Beta strandi160 – 162Combined sources3
Helixi170 – 172Combined sources3
Helixi175 – 182Combined sources8
Helixi185 – 187Combined sources3
Helixi190 – 195Combined sources6
Helixi201 – 216Combined sources16
Turni220 – 223Combined sources4
Helixi226 – 235Combined sources10
Helixi244 – 246Combined sources3
Helixi249 – 258Combined sources10
Helixi263 – 265Combined sources3
Helixi269 – 272Combined sources4
Helixi276 – 279Combined sources4
Helixi284 – 287Combined sources4
Helixi288 – 306Combined sources19
Beta strandi379 – 381Combined sources3
Helixi392 – 394Combined sources3
Turni395 – 397Combined sources3
Helixi436 – 440Combined sources5
Helixi445 – 483Combined sources39

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WWSX-ray2.01A/B/C/D436-484[»]
4HKDX-ray1.50A/B/C/D436-484[»]
4L0NX-ray1.40A/B/C/D/E/F/G/H/I/J436-484[»]
4LG4X-ray2.42A/B/C/D/E/F16-313[»]
4LGDX-ray3.05A/B/C/D9-491[»]
4OH9X-ray1.70A/B436-484[»]
5BRMX-ray2.65G/H/I/J/K/L/M/N/O371-401[»]
5DH3X-ray2.47A/B15-313[»]
ProteinModelPortaliQ13188.
SMRiQ13188.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 278Protein kinasePROSITE-ProRule annotationAdd BLAST252
Domaini437 – 484SARAHPROSITE-ProRule annotationAdd BLAST48

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili287 – 328Sequence analysisAdd BLAST42
Coiled coili442 – 475Sequence analysisAdd BLAST34

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi308 – 314Poly-Glu7
Compositional biasi370 – 375Poly-Glu6

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SARAH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0201. Eukaryota.
ENOG410XP9G. LUCA.
GeneTreeiENSGT00810000125395.
HOGENOMiHOG000234203.
HOVERGENiHBG108518.
InParanoidiQ13188.
KOiK04412.
OMAiKQDSKLK.
OrthoDBiEOG091G065P.
PhylomeDBiQ13188.
TreeFamiTF354217.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR024205. Mst1_SARAH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR011524. SARAH_dom.
[Graphical view]
PfamiPF11629. Mst1_SARAH. 1 hit.
PF00069. 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.
PS50951. SARAH. 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 1 (identifier: Q13188-1) [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
MEQPPAPKSK LKKLSEDSLT KQPEEVFDVL EKLGEGSYGS VFKAIHKESG
60 70 80 90 100
QVVAIKQVPV ESDLQEIIKE ISIMQQCDSP YVVKYYGSYF KNTDLWIVME
110 120 130 140 150
YCGAGSVSDI IRLRNKTLIE DEIATILKST LKGLEYLHFM RKIHRDIKAG
160 170 180 190 200
NILLNTEGHA KLADFGVAGQ LTDTMAKRNT VIGTPFWMAP EVIQEIGYNC
210 220 230 240 250
VADIWSLGIT SIEMAEGKPP YADIHPMRAI FMIPTNPPPT FRKPELWSDD
260 270 280 290 300
FTDFVKKCLV KNPEQRATAT QLLQHPFIKN AKPVSILRDL ITEAMEIKAK
310 320 330 340 350
RHEEQQRELE EEEENSDEDE LDSHTMVKTS VESVGTMRAT STMSEGAQTM
360 370 380 390 400
IEHNSTMLES DLGTMVINSE DEEEEDGTMK RNATSPQVQR PSFMDYFDKQ
410 420 430 440 450
DFKNKSHENC NQNMHEPFPM SKNVFPDNWK VPQDGDFDFL KNLSLEELQM
460 470 480 490
RLKALDPMME REIEELRQRY TAKRQPILDA MDAKKRRQQN F
Length:491
Mass (Da):56,301
Last modified:April 26, 2004 - v2
Checksum:i84F598ED3617292C
GO
Isoform 2 (identifier: Q13188-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MEQPPAPK → MLQLMDSGITICLRNGAASVFKKKEWSTQGEENKQD

Note: No experimental confirmation available.
Show »
Length:519
Mass (Da):59,462
Checksum:i84CB5FEAA629AE68
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti96 – 98WIV → YLY in CAA80909 (PubMed:8274451).Curated3
Sequence conflicti121D → Y in CAA80909 (PubMed:8274451).Curated1
Sequence conflicti203D → G in CAA80909 (PubMed:8274451).Curated1
Sequence conflicti303E → D in AAC50386 (PubMed:8566796).Curated1
Sequence conflicti332 – 334ESV → GEC in AAC50386 (PubMed:8566796).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04112260V → L in an ovarian clear cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_051670418F → C.Corresponds to variant rs36047674dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0541671 – 8MEQPPAPK → MLQLMDSGITICLRNGAASV FKKKEWSTQGEENKQD in isoform 2. 1 Publication8

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26424 mRNA. Translation: AAC50386.1.
U60206 mRNA. Translation: AAB17261.1.
AK131363 mRNA. Translation: BAG54769.1.
AK291837 mRNA. Translation: BAF84526.1.
AC016877 Genomic DNA. No translation available.
AP002087 Genomic DNA. No translation available.
AP003355 Genomic DNA. No translation available.
AP003467 Genomic DNA. No translation available.
AP003551 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW91781.1.
BC010640 mRNA. Translation: AAH10640.1.
Z25422 mRNA. Translation: CAA80909.1.
CCDSiCCDS47900.1. [Q13188-1]
CCDS59108.1. [Q13188-2]
PIRiI38212.
RefSeqiNP_001243241.1. NM_001256312.1. [Q13188-2]
NP_006272.2. NM_006281.3. [Q13188-1]
UniGeneiHs.492333.
Hs.738869.

Genome annotation databases

EnsembliENST00000419617; ENSP00000390500; ENSG00000104375. [Q13188-1]
ENST00000523601; ENSP00000429744; ENSG00000104375. [Q13188-2]
GeneIDi6788.
KEGGihsa:6788.
UCSCiuc003yio.5. human. [Q13188-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26424 mRNA. Translation: AAC50386.1.
U60206 mRNA. Translation: AAB17261.1.
AK131363 mRNA. Translation: BAG54769.1.
AK291837 mRNA. Translation: BAF84526.1.
AC016877 Genomic DNA. No translation available.
AP002087 Genomic DNA. No translation available.
AP003355 Genomic DNA. No translation available.
AP003467 Genomic DNA. No translation available.
AP003551 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW91781.1.
BC010640 mRNA. Translation: AAH10640.1.
Z25422 mRNA. Translation: CAA80909.1.
CCDSiCCDS47900.1. [Q13188-1]
CCDS59108.1. [Q13188-2]
PIRiI38212.
RefSeqiNP_001243241.1. NM_001256312.1. [Q13188-2]
NP_006272.2. NM_006281.3. [Q13188-1]
UniGeneiHs.492333.
Hs.738869.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WWSX-ray2.01A/B/C/D436-484[»]
4HKDX-ray1.50A/B/C/D436-484[»]
4L0NX-ray1.40A/B/C/D/E/F/G/H/I/J436-484[»]
4LG4X-ray2.42A/B/C/D/E/F16-313[»]
4LGDX-ray3.05A/B/C/D9-491[»]
4OH9X-ray1.70A/B436-484[»]
5BRMX-ray2.65G/H/I/J/K/L/M/N/O371-401[»]
5DH3X-ray2.47A/B15-313[»]
ProteinModelPortaliQ13188.
SMRiQ13188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112664. 89 interactors.
DIPiDIP-36128N.
IntActiQ13188. 74 interactors.
MINTiMINT-3027356.
STRINGi9606.ENSP00000390500.

Chemistry databases

BindingDBiQ13188.
ChEMBLiCHEMBL4708.
GuidetoPHARMACOLOGYi2219.

PTM databases

iPTMnetiQ13188.
PhosphoSitePlusiQ13188.

Polymorphism and mutation databases

BioMutaiSTK3.
DMDMi46577700.

2D gel databases

OGPiQ13188.

Proteomic databases

EPDiQ13188.
MaxQBiQ13188.
PaxDbiQ13188.
PeptideAtlasiQ13188.
PRIDEiQ13188.

Protocols and materials databases

DNASUi6788.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000419617; ENSP00000390500; ENSG00000104375. [Q13188-1]
ENST00000523601; ENSP00000429744; ENSG00000104375. [Q13188-2]
GeneIDi6788.
KEGGihsa:6788.
UCSCiuc003yio.5. human. [Q13188-1]

Organism-specific databases

CTDi6788.
DisGeNETi6788.
GeneCardsiSTK3.
HGNCiHGNC:11406. STK3.
HPAiCAB025316.
HPA007120.
MIMi605030. gene.
neXtProtiNX_Q13188.
OpenTargetsiENSG00000104375.
PharmGKBiPA36213.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0201. Eukaryota.
ENOG410XP9G. LUCA.
GeneTreeiENSGT00810000125395.
HOGENOMiHOG000234203.
HOVERGENiHBG108518.
InParanoidiQ13188.
KOiK04412.
OMAiKQDSKLK.
OrthoDBiEOG091G065P.
PhylomeDBiQ13188.
TreeFamiTF354217.

Enzyme and pathway databases

BioCyciZFISH:HS02575-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-2028269. Signaling by Hippo.
SignaLinkiQ13188.
SIGNORiQ13188.

Miscellaneous databases

ChiTaRSiSTK3. human.
GeneWikiiSTK3.
GenomeRNAii6788.
PMAP-CutDBQ13188.
PROiQ13188.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000104375.
CleanExiHS_STK3.
ExpressionAtlasiQ13188. baseline and differential.
GenevisibleiQ13188. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR024205. Mst1_SARAH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR011524. SARAH_dom.
[Graphical view]
PfamiPF11629. Mst1_SARAH. 1 hit.
PF00069. 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.
PS50951. SARAH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSTK3_HUMAN
AccessioniPrimary (citable) accession number: Q13188
Secondary accession number(s): A8K722
, B3KYA7, Q15445, Q15801, Q96FM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: April 26, 2004
Last modified: November 30, 2016
This is version 175 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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.