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UniProtKB - P52333 (JAK3_HUMAN)

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Protein

Tyrosine-protein kinase JAK3

Gene

JAK3

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

Functioni

Non-receptor tyrosine kinase involved in various processes such as cell growth, development, or differentiation. Mediates essential signaling events in both innate and adaptive immunity and plays a crucial role in hematopoiesis during T-cells development. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors sharing the common subunit gamma such as IL2R, IL4R, IL7R, IL9R, IL15R and IL21R. Following ligand binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, upon IL2R activation by IL2, JAK1 and JAK3 molecules bind to IL2R beta (IL2RB) and gamma chain (IL2RG) subunits inducing the tyrosine phosphorylation of both receptor subunits on their cytoplasmic domain. Then, STAT5A AND STAT5B are recruited, phosphorylated and activated by JAK1 and JAK3. Once activated, dimerized STAT5 translocates to the nucleus and promotes the transcription of specific target genes in a cytokine-specific fashion.4 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei855ATPPROSITE-ProRule annotation1
Active sitei949Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi828 – 836ATPPROSITE-ProRule annotation9

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionKinase, Transferase, Tyrosine-protein kinase
Biological processAdaptive immunity, Immunity, Innate immunity
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-1266695 Interleukin-7 signaling
R-HSA-392451 G beta:gamma signalling through PI3Kgamma
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6785807 Interleukin-4 and 13 signaling
R-HSA-8854691 Interleukin-20 family signaling
R-HSA-8983432 Interleukin-15 signaling
R-HSA-8985947 Interleukin-9 signaling
R-HSA-9020558 Interleukin-2 signaling
R-HSA-9020958 Interleukin-21 signaling
R-HSA-912526 Interleukin receptor SHC signaling
SignaLinkiP52333
SIGNORiP52333

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase JAK3 (EC:2.7.10.2)
Alternative name(s):
Janus kinase 3
Short name:
JAK-3
Leukocyte janus kinase
Short name:
L-JAK
Gene namesi
Name:JAK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000105639.18
HGNCiHGNC:6193 JAK3
MIMi600173 gene
neXtProtiNX_P52333

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, Membrane

Pathology & Biotechi

Involvement in diseasei

Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-positive/NK-cell-negative (T(-)B(+)NK(-) SCID)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development.
See also OMIM:600802
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01933758Missing in T(-)B(+)NK(-) SCID. 1 Publication1
Natural variantiVAR_006284100Y → C in T(-)B(+)NK(-) SCID. 1 PublicationCorresponds to variant dbSNP:rs137852624EnsemblClinVar.1
Natural variantiVAR_010492151P → R in T(-)B(+)NK(-) SCID. 2 PublicationsCorresponds to variant dbSNP:rs55778349EnsemblClinVar.1
Natural variantiVAR_019338169D → E in T(-)B(+)NK(-) SCID. 1 PublicationCorresponds to variant dbSNP:rs147181709Ensembl.1
Natural variantiVAR_010493481E → G in T(-)B(+)NK(-) SCID. 1 Publication1
Natural variantiVAR_010494582R → W in T(-)B(+)NK(-) SCID. 1 PublicationCorresponds to variant dbSNP:rs193922361EnsemblClinVar.1
Natural variantiVAR_010495586 – 592Missing in T(-)B(+)NK(-) SCID; lack of phosphorylation in response to cytokine stimulation. 1 Publication7
Natural variantiVAR_019339589G → S in T(-)B(+)NK(-) SCID. 1 PublicationCorresponds to variant dbSNP:rs886039394EnsemblClinVar.1
Natural variantiVAR_010497759C → R in T(-)B(+)NK(-) SCID; constitutive phosphorylation. 1 Publication1
Natural variantiVAR_010498910L → S in T(-)B(+)NK(-) SCID. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi785Y → F: Strong decrease of JAK3 phosphorylation. 1 Publication1
Mutagenesisi855K → A: More than 90% loss of STAT5a activation. 1 Publication1
Mutagenesisi904Y → F: About 40% loss of STAT5a activation. 1 Publication1
Mutagenesisi939Y → F: About 80% loss of STAT5a activation. 1 Publication1

Keywords - Diseasei

Disease mutation, SCID

Organism-specific databases

DisGeNETi3718
MalaCardsiJAK3
MIMi600802 phenotype
OpenTargetsiENSG00000105639
Orphaneti35078 T-B+ severe combined immunodeficiency due to JAK3 deficiency
PharmGKBiPA29990

Chemistry databases

ChEMBLiCHEMBL2148
DrugBankiDB08895 Tofacitinib
GuidetoPHARMACOLOGYi2049

Polymorphism and mutation databases

BioMutaiJAK3
DMDMi50403745

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000881151 – 1124Tyrosine-protein kinase JAK3Add BLAST1124

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17PhosphoserineBy similarity1
Modified residuei785Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei904Phosphotyrosine1 Publication1
Modified residuei939Phosphotyrosine1 Publication1
Modified residuei980Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei981Phosphotyrosine; by autocatalysis1 Publication1

Post-translational modificationi

Tyrosine phosphorylated in response to IL-2 and IL-4. Dephosphorylation of Tyr-980 and Tyr-981 by PTPN2 negatively regulates cytokine-mediated signaling (Probable).4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP52333
PaxDbiP52333
PeptideAtlasiP52333
PRIDEiP52333
ProteomicsDBi56482
56483 [P52333-2]

PTM databases

iPTMnetiP52333
PhosphoSitePlusiP52333

Expressioni

Tissue specificityi

In NK cells and an NK-like cell line but not in resting T-cells or in other tissues. The S-form is more commonly seen in hematopoietic lines, whereas the B-form is detected in cells both of hematopoietic and epithelial origins.1 Publication

Gene expression databases

BgeeiENSG00000105639
CleanExiHS_JAK3
ExpressionAtlasiP52333 baseline and differential
GenevisibleiP52333 HS

Organism-specific databases

HPAiHPA070314

Interactioni

Subunit structurei

Interacts with STAM2 and MYO18A (By similarity). Interacts with SHB.By similarity3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi109921, 73 interactors
DIPiDIP-274N
IntActiP52333, 50 interactors
MINTiP52333
STRINGi9606.ENSP00000391676

Chemistry databases

BindingDBiP52333

Structurei

Secondary structure

11124
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi816 – 818Combined sources3
Helixi819 – 821Combined sources3
Beta strandi822 – 830Combined sources9
Beta strandi832 – 841Combined sources10
Beta strandi845 – 847Combined sources3
Beta strandi849 – 859Combined sources11
Helixi862 – 877Combined sources16
Beta strandi886 – 891Combined sources6
Beta strandi893 – 896Combined sources4
Beta strandi898 – 903Combined sources6
Helixi910 – 917Combined sources8
Helixi918 – 920Combined sources3
Helixi923 – 942Combined sources20
Helixi952 – 954Combined sources3
Beta strandi955 – 959Combined sources5
Beta strandi962 – 965Combined sources4
Helixi968 – 970Combined sources3
Beta strandi979 – 982Combined sources4
Helixi991 – 993Combined sources3
Helixi996 – 1001Combined sources6
Beta strandi1003 – 1005Combined sources3
Helixi1006 – 1021Combined sources16
Turni1022 – 1024Combined sources3
Helixi1026 – 1028Combined sources3
Helixi1030 – 1037Combined sources8
Beta strandi1042 – 1044Combined sources3
Helixi1046 – 1055Combined sources10
Helixi1068 – 1077Combined sources10
Helixi1082 – 1084Combined sources3
Helixi1088 – 1102Combined sources15

3D structure databases

ProteinModelPortaliP52333
SMRiP52333
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52333

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 356FERMPROSITE-ProRule annotationAdd BLAST333
Domaini375 – 475SH2; atypicalAdd BLAST101
Domaini521 – 781Protein kinase 1PROSITE-ProRule annotationAdd BLAST261
Domaini822 – 1111Protein kinase 2PROSITE-ProRule annotationAdd BLAST290

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 223Interaction with cytokine/interferon/growth hormone receptorsBy similarityAdd BLAST223

Domaini

Possesses two phosphotransferase domains. The second one probably contains the catalytic domain (By similarity), while the presence of slight differences suggest a different role for domain 1.By similarity1 Publication

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. JAK subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain

Phylogenomic databases

eggNOGiKOG0197 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00900000140909
HOGENOMiHOG000049158
HOVERGENiHBG006195
InParanoidiP52333
KOiK11218
OMAiNCMESFL
OrthoDBiEOG091G01IS
PhylomeDBiP52333
TreeFamiTF327041

Family and domain databases

Gene3Di3.30.505.10, 1 hit
InterProiView protein in InterPro
IPR019749 Band_41_domain
IPR000299 FERM_domain
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR016251 Tyr_kinase_non-rcpt_Jak/Tyk2
IPR020775 Tyr_kinase_non-rcpt_Jak3
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 2 hits
PIRSFiPIRSF000636 TyrPK_Jak, 1 hit
PRINTSiPR01823 JANUSKINASE
PR01826 JANUSKINASE3
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00295 B41, 1 hit
SM00252 SH2, 1 hit
SM00219 TyrKc, 2 hits
SUPFAMiSSF55550 SSF55550, 2 hits
SSF56112 SSF56112, 2 hits
PROSITEiView protein in PROSITE
PS50057 FERM_3, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 2 hits
PS00109 PROTEIN_KINASE_TYR, 1 hit

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: P52333-1) [UniParc]FASTAAdd to basket
Also known as: JAK3S, Spleen-JAK3

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
MAPPSEETPL IPQRSCSLLS TEAGALHVLL PARGPGPPQR LSFSFGDHLA 
        60         70         80         90        100
EDLCVQAAKA SGILPVYHSL FALATEDLSC WFPPSHIFSV EDASTQVLLY 
       110        120        130        140        150
RIRFYFPNWF GLEKCHRFGL RKDLASAILD LPVLEHLFAQ HRSDLVSGRL 
       160        170        180        190        200
PVGLSLKEQG ECLSLAVLDL ARMAREQAQR PGELLKTVSY KACLPPSLRD 
       210        220        230        240        250
LIQGLSFVTR RRIRRTVRRA LRRVAACQAD RHSLMAKYIM DLERLDPAGA 
       260        270        280        290        300
AETFHVGLPG ALGGHDGLGL LRVAGDGGIA WTQGEQEVLQ PFCDFPEIVD 
       310        320        330        340        350
ISIKQAPRVG PAGEHRLVTV TRTDNQILEA EFPGLPEALS FVALVDGYFR 
       360        370        380        390        400
LTTDSQHFFC KEVAPPRLLE EVAEQCHGPI TLDFAINKLK TGGSRPGSYV 
       410        420        430        440        450
LRRSPQDFDS FLLTVCVQNP LGPDYKGCLI RRSPTGTFLL VGLSRPHSSL 
       460        470        480        490        500
RELLATCWDG GLHVDGVAVT LTSCCIPRPK EKSNLIVVQR GHSPPTSSLV 
       510        520        530        540        550
QPQSQYQLSQ MTFHKIPADS LEWHENLGHG SFTKIYRGCR HEVVDGEARK 
       560        570        580        590        600
TEVLLKVMDA KHKNCMESFL EAASLMSQVS YRHLVLLHGV CMAGDSTMVQ 
       610        620        630        640        650
EFVHLGAIDM YLRKRGHLVP ASWKLQVVKQ LAYALNYLED KGLPHGNVSA 
       660        670        680        690        700
RKVLLAREGA DGSPPFIKLS DPGVSPAVLS LEMLTDRIPW VAPECLREAQ 
       710        720        730        740        750
TLSLEADKWG FGATVWEVFS GVTMPISALD PAKKLQFYED RQQLPAPKWT 
       760        770        780        790        800
ELALLIQQCM AYEPVQRPSF RAVIRDLNSL ISSDYELLSD PTPGALAPRD 
       810        820        830        840        850
GLWNGAQLYA CQDPTIFEER HLKYISQLGK GNFGSVELCR YDPLGDNTGA 
       860        870        880        890        900
LVAVKQLQHS GPDQQRDFQR EIQILKALHS DFIVKYRGVS YGPGRQSLRL 
       910        920        930        940        950
VMEYLPSGCL RDFLQRHRAR LDASRLLLYS SQICKGMEYL GSRRCVHRDL 
       960        970        980        990       1000
AARNILVESE AHVKIADFGL AKLLPLDKDY YVVREPGQSP IFWYAPESLS 
      1010       1020       1030       1040       1050
DNIFSRQSDV WSFGVVLYEL FTYCDKSCSP SAEFLRMMGC ERDVPALCRL 
      1060       1070       1080       1090       1100
LELLEEGQRL PAPPACPAEV HELMKLCWAP SPQDRPSFSA LGPQLDMLWS 
      1110       1120 
GSRGCETHAF TAHPEGKHHS LSFS
Length:1,124
Mass (Da):125,099
Last modified:July 19, 2004 - v2
Checksum:i895D8563439B2B7C
GO
Isoform 1 (identifier: P52333-2) [UniParc]FASTAAdd to basket
Also known as: JAK3B, Breast-JAK3

The sequence of this isoform differs from the canonical sequence as follows:
     1071-1124: HELMKLCWAP...EGKHHSLSFS → SAAGLASVSQSVDWAGVSGKPAGA

Note: May be inactive as it lacks some part of the kinase domain.
Show »
Length:1,094
Mass (Da):121,268
Checksum:iD491FADB3D772693
GO
Isoform 3 (identifier: P52333-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     597-619: TMVQEFVHLGAIDMYLRKRGHLV → ESPPPTHPTPASPKSRLFFPPLF
     620-1124: Missing.

Note: No experimental confirmation available.
Show »
Length:619
Mass (Da):68,279
Checksum:i2DA342038998636C
GO

Sequence cautioni

The sequence AAC50227 differs from that shown. Wrong choice of CDS. Was erroneously described as an isoform JAK3M while it is a fragmentary mRNA of INSL3.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti34G → A in AAA19626 (PubMed:8022790).Curated1
Sequence conflicti45F → S in AAC50950 (PubMed:8921370).Curated1
Sequence conflicti103R → RS in AAC50950 (PubMed:8921370).Curated1
Sequence conflicti147Missing in AAC50542 (PubMed:8662778).Curated1
Sequence conflicti187T → A in AAC50542 (PubMed:8662778).Curated1
Sequence conflicti212R → A in AAA19626 (PubMed:8022790).Curated1
Sequence conflicti212R → A in AAC50950 (PubMed:8921370).Curated1
Sequence conflicti222R → P in AAA19626 (PubMed:8022790).Curated1
Sequence conflicti222R → P in AAC50950 (PubMed:8921370).Curated1
Sequence conflicti271L → F in AAC50950 (PubMed:8921370).Curated1
Sequence conflicti287Missing in AAC50950 (PubMed:8921370).Curated1
Sequence conflicti610M → I in AAC50226 (PubMed:7559633).Curated1
Sequence conflicti845 – 846GD → AH in AAA19626 (PubMed:8022790).Curated2
Sequence conflicti895 – 897RQS → EPE in AAC50950 (PubMed:8921370).Curated3
Sequence conflicti896 – 897QS → PE in AAA19626 (PubMed:8022790).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04172212P → L1 PublicationCorresponds to variant dbSNP:rs56061056EnsemblClinVar.1
Natural variantiVAR_04172340R → H1 PublicationCorresponds to variant dbSNP:rs56384680EnsemblClinVar.1
Natural variantiVAR_01933758Missing in T(-)B(+)NK(-) SCID. 1 Publication1
Natural variantiVAR_006284100Y → C in T(-)B(+)NK(-) SCID. 1 PublicationCorresponds to variant dbSNP:rs137852624EnsemblClinVar.1
Natural variantiVAR_019336132P → T2 PublicationsCorresponds to variant dbSNP:rs3212723EnsemblClinVar.1
Natural variantiVAR_010492151P → R in T(-)B(+)NK(-) SCID. 2 PublicationsCorresponds to variant dbSNP:rs55778349EnsemblClinVar.1
Natural variantiVAR_019338169D → E in T(-)B(+)NK(-) SCID. 1 PublicationCorresponds to variant dbSNP:rs147181709Ensembl.1
Natural variantiVAR_010493481E → G in T(-)B(+)NK(-) SCID. 1 Publication1
Natural variantiVAR_041724521L → V1 PublicationCorresponds to variant dbSNP:rs55666418EnsemblClinVar.1
Natural variantiVAR_041725527L → P in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_010494582R → W in T(-)B(+)NK(-) SCID. 1 PublicationCorresponds to variant dbSNP:rs193922361EnsemblClinVar.1
Natural variantiVAR_010495586 – 592Missing in T(-)B(+)NK(-) SCID; lack of phosphorylation in response to cytokine stimulation. 1 Publication7
Natural variantiVAR_019339589G → S in T(-)B(+)NK(-) SCID. 1 PublicationCorresponds to variant dbSNP:rs886039394EnsemblClinVar.1
Natural variantiVAR_041726688I → F1 PublicationCorresponds to variant dbSNP:rs35785705EnsemblClinVar.1
Natural variantiVAR_010496722V → I4 PublicationsCorresponds to variant dbSNP:rs3213409EnsemblClinVar.1
Natural variantiVAR_010497759C → R in T(-)B(+)NK(-) SCID; constitutive phosphorylation. 1 Publication1
Natural variantiVAR_010498910L → S in T(-)B(+)NK(-) SCID. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_054165597 – 619TMVQE…RGHLV → ESPPPTHPTPASPKSRLFFP PLF in isoform 3. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_054166620 – 1124Missing in isoform 3. 1 PublicationAdd BLAST505
Alternative sequenceiVSP_0049891071 – 1124HELMK…SLSFS → SAAGLASVSQSVDWAGVSGK PAGA in isoform 1. 1 PublicationAdd BLAST54

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09607 mRNA Translation: AAA19626.1
U31601 mRNA Translation: AAC50226.1
U31602 mRNA Translation: AAC50227.1 Sequence problems.
U70065 Genomic DNA Translation: AAC50950.1
AF513860 Genomic DNA Translation: AAM44860.1
AC007201 Genomic DNA Translation: AAD22741.1
CH471106 Genomic DNA Translation: EAW84639.1
BC028068 mRNA Translation: AAH28068.1
U57096 mRNA Translation: AAC50542.1
CCDSiCCDS12366.1 [P52333-1]
PIRiA55747
RefSeqiNP_000206.2, NM_000215.3 [P52333-1]
UniGeneiHs.515247

Genome annotation databases

EnsembliENST00000458235; ENSP00000391676; ENSG00000105639 [P52333-1]
ENST00000527670; ENSP00000432511; ENSG00000105639 [P52333-1]
ENST00000534444; ENSP00000436421; ENSG00000105639 [P52333-2]
GeneIDi3718
KEGGihsa:3718
UCSCiuc002nhn.5 human [P52333-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiJAK3_HUMAN
AccessioniPrimary (citable) accession number: P52333
Secondary accession number(s): Q13259
, Q13260, Q13611, Q8N1E8, Q99699, Q9Y6S2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 19, 2004
Last modified: June 20, 2018
This is version 202 of the entry and version 2 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 19
    Human chromosome 19: 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

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