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

Serine/threonine-protein kinase PAK 2

Gene

PAK2

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 plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Full-length PAK2 stimulates cell survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Phosphorylates JUN and plays an important role in EGF-induced cell proliferation. Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP. Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis. On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway. Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by binding small G proteins. Binding of GTP-bound CDC42 or RAC1 to the autoregulatory region releases monomers from the autoinhibited dimer, enables phosphorylation of Thr-402 and allows the kinase domain to adopt an active structure (By similarity). Following caspase cleavage, autophosphorylated PAK-2p34 is constitutively active.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei278 – 2781ATPPROSITE-ProRule annotation
Active sitei367 – 3671Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi255 – 2639ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cellular response to organic cyclic compound Source: Ensembl
  • dendritic spine development Source: Ensembl
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • mitotic cell cycle Source: GO_Central
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis Source: UniProtKB
  • negative regulation of protein kinase activity Source: ProtInc
  • peptidyl-serine phosphorylation Source: BHF-UCL
  • phosphorylation Source: UniProtKB
  • positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • protein autophosphorylation Source: MGI
  • protein phosphorylation Source: MGI
  • regulation of defense response to virus by virus Source: Reactome
  • regulation of growth Source: UniProtKB-KW
  • signal transduction Source: ProtInc
  • stimulatory C-type lectin receptor signaling pathway Source: Reactome
  • T cell costimulation Source: Reactome
  • T cell receptor signaling pathway Source: Reactome
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Growth regulation, Host-virus interaction

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-164944. Nef and signal transduction.
R-HSA-202433. Generation of second messenger molecules.
R-HSA-211728. Regulation of PAK-2p34 activity by PS-GAP/RHG10.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-211736. Stimulation of the cell death response by PAK-2p34.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-389359. CD28 dependent Vav1 pathway.
R-HSA-3928664. Ephrin signaling.
R-HSA-399954. Sema3A PAK dependent Axon repulsion.
R-HSA-428540. Activation of Rac.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5218920. VEGFR2 mediated vascular permeability.
R-HSA-5621575. CD209 (DC-SIGN) signaling.
R-HSA-5627123. RHO GTPases activate PAKs.
R-HSA-5687128. MAPK6/MAPK4 signaling.
SignaLinkiQ13177.
SIGNORiQ13177.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PAK 2 (EC:2.7.11.1)
Alternative name(s):
Gamma-PAK
PAK65
S6/H4 kinase
p21-activated kinase 2
Short name:
PAK-2
p58
Cleaved into the following 2 chains:
PAK-2p27
Short name:
p27
PAK-2p34
Short name:
p34
Alternative name(s):
C-t-PAK2
Gene namesi
Name:PAK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:8591. PAK2.

Subcellular locationi

Serine/threonine-protein kinase PAK 2 :
  • Cytoplasm

  • Note: MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane.
PAK-2p34 :

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: BHF-UCL
  • cytosol Source: Reactome
  • nucleoplasm Source: HPA
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi212 – 2121D → N: Inhibits caspase-mediated cleavage. 1 Publication
Mutagenesisi213 – 2131G → A: Abolishes myristoylation of PAK-2p34 and membrane location.
Mutagenesisi239 – 2435IVSIG → REGRS: Abolishes nuclear export. 1 Publication
Mutagenesisi246 – 2483KKK → MHE: Greatly inhibits nuclear localization. 1 Publication
Mutagenesisi278 – 2781K → R: Abolishes kinase activity and autophosphorylation. 1 Publication
Mutagenesisi402 – 4021T → A: Abolishes kinase activity and greatly inhibits autophosphorylation of PAK-2p27 and PAK-2p34. 1 Publication

Organism-specific databases

PharmGKBiPA32918.

Chemistry

ChEMBLiCHEMBL4487.
GuidetoPHARMACOLOGYi2134.

Polymorphism and mutation databases

BioMutaiPAK2.
DMDMi143811432.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 524523Serine/threonine-protein kinase PAK 2PRO_0000086465Add
BLAST
Chaini2 – 212211PAK-2p27PRO_0000304922Add
BLAST
Chaini213 – 524312PAK-2p34PRO_0000304923Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei20 – 201PhosphoserineCombined sources
Modified residuei55 – 551PhosphoserineCombined sources
Modified residuei58 – 581PhosphoserineCombined sources
Modified residuei60 – 601PhosphothreonineCombined sources
Modified residuei62 – 621N6-acetyllysineBy similarity
Modified residuei64 – 641PhosphoserineCombined sources
Modified residuei128 – 1281N6-acetyllysineCombined sources
Modified residuei134 – 1341PhosphothreonineCombined sources
Modified residuei139 – 1391PhosphotyrosineCombined sources
Modified residuei141 – 1411PhosphoserineCombined sources
Modified residuei143 – 1431PhosphothreonineCombined sources
Modified residuei152 – 1521PhosphoserineBy similarity
Modified residuei154 – 1541PhosphothreonineCombined sources
Modified residuei169 – 1691PhosphothreonineCombined sources
Modified residuei197 – 1971PhosphoserineCombined sources
Lipidationi213 – 2131N-myristoyl glycine; in form PAK-2p341 Publication
Modified residuei402 – 4021Phosphothreonine; by autocatalysisCurated

Post-translational modificationi

Full length PAK2 is autophosphorylated when activated by CDC42/p21. Following cleavage, both peptides, PAK-2p27 and PAK-2p34, become highly autophosphorylated, with PAK-2p27 being phosphorylated on serine and PAK-2p34 on threonine residues, respectively. Autophosphorylation of PAK-2p27 can occur in the absence of any effectors and is dependent on phosphorylation of Thr-402, because PAK-2p27 is acting as an exogenous substrate.
During apoptosis proteolytically cleaved by caspase-3 or caspase-3-like proteases to yield active PAK-2p34.
Ubiquitinated, leading to its proteasomal degradation.1 Publication
PAK-2p34 is myristoylated.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei212 – 2132Cleavage; by caspase-3 or caspase-3-like proteases

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13177.
MaxQBiQ13177.
PaxDbiQ13177.
PeptideAtlasiQ13177.
PRIDEiQ13177.

2D gel databases

OGPiQ13177.

PTM databases

iPTMnetiQ13177.
PhosphoSiteiQ13177.
SwissPalmiQ13177.

Miscellaneous databases

PMAP-CutDBQ13177.

Expressioni

Tissue specificityi

Ubiquitously expressed. Higher levels seen in skeletal muscle, ovary, thymus and spleen.

Gene expression databases

BgeeiENSG00000180370.
CleanExiHS_PAK2.
ExpressionAtlasiQ13177. baseline and differential.
GenevisibleiQ13177. HS.

Organism-specific databases

HPAiCAB007794.
HPA036205.

Interactioni

Subunit structurei

Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1. Interacts with SH3MD4. Interacts with and activated by HIV-1 Nef. Interacts with SCRIB. Interacts with ARHGEF7 and GIT1. PAK-2p34 interacts with ARHGAP10.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1045887,EBI-1045887
ARHGEF6Q150522EBI-1045887,EBI-1642523
ARHGEF7Q141554EBI-1045887,EBI-717515
Arhgef7O550438EBI-1045887,EBI-3649585From a different organism.
CASP7P552106EBI-1045887,EBI-523958
CDC42P609534EBI-1045887,EBI-81752
GRB2P629932EBI-1045887,EBI-401755
HCKP086312EBI-1045887,EBI-346340
HTTP428582EBI-1045887,EBI-466029
LIMK1P536672EBI-1045887,EBI-444403
NCK1P163332EBI-1045887,EBI-389883
RAC1P630004EBI-1045887,EBI-413628
RAF1P040492EBI-1045887,EBI-365996
RHOJQ9H4E53EBI-1045887,EBI-6285694
SH3RF3Q8TEJ32EBI-1045887,EBI-7975674
SORBS1Q9BX662EBI-1045887,EBI-433642
SORBS2O948752EBI-1045887,EBI-311323
SORBS3O605046EBI-1045887,EBI-741237
SRCP129312EBI-1045887,EBI-621482

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • identical protein binding Source: IntAct
  • protein kinase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi111098. 84 interactions.
DIPiDIP-38249N.
IntActiQ13177. 45 interactions.
MINTiMINT-235655.
STRINGi9606.ENSP00000314067.

Chemistry

BindingDBiQ13177.

Structurei

Secondary structure

1
524
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi123 – 1264Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PCSX-ray2.86E/F/G/H121-136[»]
ProteinModelPortaliQ13177.
SMRiQ13177. Positions 69-143, 228-519.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13177.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 8714CRIBPROSITE-ProRule annotationAdd
BLAST
Domaini249 – 499251Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni69 – 13769Autoregulatory regionBy similarityAdd
BLAST
Regioni69 – 11244GTPase-bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi245 – 2517Nuclear localization signal

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0578. Eukaryota.
ENOG410XP4K. LUCA.
GeneTreeiENSGT00840000129718.
HOGENOMiHOG000234202.
HOVERGENiHBG108518.
InParanoidiQ13177.
KOiK04410.
OMAiMTSASHK.
OrthoDBiEOG091G04H8.
PhylomeDBiQ13177.
TreeFamiTF105351.

Family and domain databases

Gene3Di3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q13177-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDNGELEDK PPAPPVRMSS TIFSTGGKDP LSANHSLKPL PSVPEEKKPR
60 70 80 90 100
HKIISIFSGT EKGSKKKEKE RPEISPPSDF EHTIHVGFDA VTGEFTGMPE
110 120 130 140 150
QWARLLQTSN ITKLEQKKNP QAVLDVLKFY DSNTVKQKYL SFTPPEKDGF
160 170 180 190 200
PSGTPALNAK GTEAPAVVTE EEDDDEETAP PVIAPRPDHT KSIYTRSVID
210 220 230 240 250
PVPAPVGDSH VDGAAKSLDK QKKKTKMTDE EIMEKLRTIV SIGDPKKKYT
260 270 280 290 300
RYEKIGQGAS GTVFTATDVA LGQEVAIKQI NLQKQPKKEL IINEILVMKE
310 320 330 340 350
LKNPNIVNFL DSYLVGDELF VVMEYLAGGS LTDVVTETCM DEAQIAAVCR
360 370 380 390 400
ECLQALEFLH ANQVIHRDIK SDNVLLGMEG SVKLTDFGFC AQITPEQSKR
410 420 430 440 450
STMVGTPYWM APEVVTRKAY GPKVDIWSLG IMAIEMVEGE PPYLNENPLR
460 470 480 490 500
ALYLIATNGT PELQNPEKLS PIFRDFLNRC LEMDVEKRGS AKELLQHPFL
510 520
KLAKPLSSLT PLIMAAKEAM KSNR
Length:524
Mass (Da):58,043
Last modified:April 3, 2007 - v3
Checksum:i00A7CD15F93D4180
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901A → T in AAA75468 (PubMed:7744004).Curated
Sequence conflicti150 – 1501F → L in AAA65442 (Ref. 1) Curated
Sequence conflicti225 – 2251T → P in AAA65442 (Ref. 1) Curated
Sequence conflicti258 – 2581G → R in AAH69613 (PubMed:15489334).Curated
Sequence conflicti329 – 3291G → R in AAA75468 (PubMed:7744004).Curated
Sequence conflicti338 – 3381T → TA in AAA65442 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24153 mRNA. Translation: AAA65442.1.
BC069613 mRNA. Translation: AAH69613.1.
U25975 mRNA. Translation: AAA75468.1.
CCDSiCCDS3321.1.
PIRiS58682.
RefSeqiNP_002568.2. NM_002577.4.
XP_011511172.1. XM_011512870.2.
UniGeneiHs.518530.

Genome annotation databases

EnsembliENST00000327134; ENSP00000314067; ENSG00000180370.
GeneIDi5062.
KEGGihsa:5062.
UCSCiuc003fwy.4. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24153 mRNA. Translation: AAA65442.1.
BC069613 mRNA. Translation: AAH69613.1.
U25975 mRNA. Translation: AAA75468.1.
CCDSiCCDS3321.1.
PIRiS58682.
RefSeqiNP_002568.2. NM_002577.4.
XP_011511172.1. XM_011512870.2.
UniGeneiHs.518530.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PCSX-ray2.86E/F/G/H121-136[»]
ProteinModelPortaliQ13177.
SMRiQ13177. Positions 69-143, 228-519.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111098. 84 interactions.
DIPiDIP-38249N.
IntActiQ13177. 45 interactions.
MINTiMINT-235655.
STRINGi9606.ENSP00000314067.

Chemistry

BindingDBiQ13177.
ChEMBLiCHEMBL4487.
GuidetoPHARMACOLOGYi2134.

PTM databases

iPTMnetiQ13177.
PhosphoSiteiQ13177.
SwissPalmiQ13177.

Polymorphism and mutation databases

BioMutaiPAK2.
DMDMi143811432.

2D gel databases

OGPiQ13177.

Proteomic databases

EPDiQ13177.
MaxQBiQ13177.
PaxDbiQ13177.
PeptideAtlasiQ13177.
PRIDEiQ13177.

Protocols and materials databases

DNASUi5062.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327134; ENSP00000314067; ENSG00000180370.
GeneIDi5062.
KEGGihsa:5062.
UCSCiuc003fwy.4. human.

Organism-specific databases

CTDi5062.
GeneCardsiPAK2.
H-InvDBHIX0030815.
HGNCiHGNC:8591. PAK2.
HPAiCAB007794.
HPA036205.
MIMi605022. gene.
neXtProtiNX_Q13177.
PharmGKBiPA32918.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0578. Eukaryota.
ENOG410XP4K. LUCA.
GeneTreeiENSGT00840000129718.
HOGENOMiHOG000234202.
HOVERGENiHBG108518.
InParanoidiQ13177.
KOiK04410.
OMAiMTSASHK.
OrthoDBiEOG091G04H8.
PhylomeDBiQ13177.
TreeFamiTF105351.

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-164944. Nef and signal transduction.
R-HSA-202433. Generation of second messenger molecules.
R-HSA-211728. Regulation of PAK-2p34 activity by PS-GAP/RHG10.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-211736. Stimulation of the cell death response by PAK-2p34.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-389359. CD28 dependent Vav1 pathway.
R-HSA-3928664. Ephrin signaling.
R-HSA-399954. Sema3A PAK dependent Axon repulsion.
R-HSA-428540. Activation of Rac.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5218920. VEGFR2 mediated vascular permeability.
R-HSA-5621575. CD209 (DC-SIGN) signaling.
R-HSA-5627123. RHO GTPases activate PAKs.
R-HSA-5687128. MAPK6/MAPK4 signaling.
SignaLinkiQ13177.
SIGNORiQ13177.

Miscellaneous databases

ChiTaRSiPAK2. human.
EvolutionaryTraceiQ13177.
GeneWikiiPAK2.
GenomeRNAii5062.
PMAP-CutDBQ13177.
PROiQ13177.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000180370.
CleanExiHS_PAK2.
ExpressionAtlasiQ13177. baseline and differential.
GenevisibleiQ13177. HS.

Family and domain databases

Gene3Di3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPAK2_HUMAN
AccessioniPrimary (citable) accession number: Q13177
Secondary accession number(s): Q13154, Q6ISC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 3, 2007
Last modified: September 7, 2016
This is version 179 of the entry and version 3 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, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. 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.