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UniProtKB - P51812 (KS6A3_HUMAN)

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Protein

Ribosomal protein S6 kinase alpha-3

Gene

RPS6KA3

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 downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3. Negatively regulates EGF-induced MAPK1/3 phosphorylation via phosphorylation of SOS1. Phosphorylates SOS1 at 'Ser-1134' and 'Ser-1161' that create YWHAB and YWHAE binding sites and which contribute to the negative regulation of MAPK1/3 phosphorylation (By similarity). Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration (PubMed:26158630).By similarity8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Upon extracellular signal or mitogen stimulation, phosphorylated at Thr-577 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-386, allowing binding of PDPK1, which in turn phosphorylates Ser-227 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei100ATPPROSITE-ProRule annotation1
Active sitei193Proton acceptorBy similarity1
Binding sitei451ATPPROSITE-ProRule annotation1
Active sitei539Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi74 – 82ATPPROSITE-ProRule annotation9
Nucleotide bindingi428 – 436ATPPROSITE-ProRule annotation9

GO - Molecular functioni

Complete GO annotation...

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • central nervous system development Source: ProtInc
  • intracellular signal transduction Source: GO_Central
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • peptidyl-serine phosphorylation Source: ARUK-UCL
  • positive regulation of cell differentiation Source: UniProtKB
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • regulation of DNA-templated transcription in response to stress Source: UniProtKB
  • regulation of translation in response to stress Source: UniProtKB
  • response to lipopolysaccharide Source: UniProtKB
  • signal transduction Source: ProtInc
  • skeletal system development Source: ProtInc
  • toll-like receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Stress response
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-198753. ERK/MAPK targets.
R-HSA-199920. CREB phosphorylation.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-437239. Recycling pathway of L1.
R-HSA-442742. CREB phosphorylation through the activation of Ras.
R-HSA-444257. RSK activation.
R-HSA-881907. Gastrin-CREB signalling pathway via PKC and MAPK.
SignaLinkiP51812.
SIGNORiP51812.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal protein S6 kinase alpha-3 (EC:2.7.11.1)
Short name:
S6K-alpha-3
Alternative name(s):
90 kDa ribosomal protein S6 kinase 3
Short name:
p90-RSK 3
Short name:
p90RSK3
Insulin-stimulated protein kinase 1
Short name:
ISPK-1
MAP kinase-activated protein kinase 1b
Short name:
MAPK-activated protein kinase 1b
Short name:
MAPKAP kinase 1b
Short name:
MAPKAPK-1b
Ribosomal S6 kinase 2
Short name:
RSK-2
pp90RSK2
Gene namesi
Name:RPS6KA3
Synonyms:ISPK1, MAPKAPK1B, RSK2
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 X

Organism-specific databases

HGNCiHGNC:10432. RPS6KA3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Coffin-Lowry syndrome (CLS)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA X-linked mental retardation associated with facial and digital dysmorphisms, progressive skeletal malformations, growth retardation, hearing deficit and paroxysmal movement disorders.
See also OMIM:303600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00618975G → V in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454124Ensembl.1
Natural variantiVAR_00619082V → F in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454126Ensembl.1
Natural variantiVAR_006191114R → W in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454127Ensembl.1
Natural variantiVAR_006192127H → Q in CLS. 1 Publication1
Natural variantiVAR_006193154D → Y in CLS. 1 Publication1
Natural variantiVAR_065894189I → K in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454130Ensembl.1
Natural variantiVAR_006194225A → V in CLS. 1 PublicationCorresponds to variant dbSNP:rs879027948Ensembl.1
Natural variantiVAR_006195227S → A in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454125Ensembl.1
Natural variantiVAR_065896268F → S in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454131Ensembl.1
Natural variantiVAR_006196431G → D in CLS. 1 Publication1
Natural variantiVAR_065898477Missing in CLS. 1 Publication1
Natural variantiVAR_006197729R → Q in CLS. 1 PublicationCorresponds to variant dbSNP:rs28935171Ensembl.1
Mental retardation, X-linked 19 (MRX19)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA non-syndromic form of mild to moderate mental retardation. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. In contrast to syndromic or specific X-linked mental retardation which also present with associated physical, neurological and/or psychiatric manifestations, intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation.
See also OMIM:300844
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_065892115T → S in MRX19. 1 PublicationCorresponds to variant dbSNP:rs387906703Ensembl.1
Natural variantiVAR_065893152Missing in MRX19. 1 Publication1
Natural variantiVAR_065895202Missing in MRX19. 1 Publication1
Natural variantiVAR_065897383R → W in MRX19; kinase activity is decreased but not abolished. 1 PublicationCorresponds to variant dbSNP:rs122454129Ensembl.1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi6197.
MalaCardsiRPS6KA3.
MIMi300844. phenotype.
303600. phenotype.
OpenTargetsiENSG00000177189.
Orphaneti192. Coffin-Lowry syndrome.
777. X-linked non-syndromic intellectual disability.
PharmGKBiPA34847.

Chemistry databases

ChEMBLiCHEMBL2345.
DrugBankiDB00945. Acetylsalicylic acid.
GuidetoPHARMACOLOGYi1528.

Polymorphism and mutation databases

BioMutaiRPS6KA3.
DMDMi1730070.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000862031 – 740Ribosomal protein S6 kinase alpha-3Add BLAST740

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei227Phosphoserine; by PDPK1Curated1
Modified residuei365PhosphothreonineCombined sources1
Modified residuei369PhosphoserineCombined sources1
Modified residuei375PhosphoserineCombined sources1
Modified residuei386Phosphoserine; by autocatalysis and MAPKAPK2Combined sources1
Modified residuei415PhosphoserineCombined sources1
Modified residuei529Phosphotyrosine; by FGFR3By similarity1
Modified residuei556PhosphoserineCombined sources1
Modified residuei715PhosphoserineCombined sources1

Post-translational modificationi

Activated by phosphorylation at Ser-227 by PDPK1. Autophosphorylated on Ser-386, as part of the activation process. May be phosphorylated at Thr-365 and Ser-369 by MAPK1/ERK2 and MAPK3/ERK1. Can also be activated via phosphorylation at Ser-386 by MAPKAPK2.
N-terminal myristoylation results in an activated kinase in the absence of added growth factors.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP51812.
MaxQBiP51812.
PaxDbiP51812.
PeptideAtlasiP51812.
PRIDEiP51812.

PTM databases

iPTMnetiP51812.
PhosphoSitePlusiP51812.

Expressioni

Tissue specificityi

Expressed in many tissues, highest levels in skeletal muscle.

Gene expression databases

BgeeiENSG00000177189.
CleanExiHS_RPS6KA3.
ExpressionAtlasiP51812. baseline and differential.
GenevisibleiP51812. HS.

Organism-specific databases

HPAiCAB003853.
CAB013520.
HPA003221.

Interactioni

Subunit structurei

Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation (By similarity). Interacts with NFATC4, ETV1/ER81 and FGFR1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPK1P284823EBI-1046616,EBI-959949

GO - Molecular functioni

Complete GO annotation...

Protein-protein interaction databases

BioGridi112111. 55 interactors.
DIPiDIP-38247N.
IntActiP51812. 18 interactors.
MINTiMINT-1542962.
STRINGi9606.ENSP00000368884.

Chemistry databases

BindingDBiP51812.

Structurei

Secondary structure

1740
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi50 – 54Combined sources5
Helixi65 – 67Combined sources3
Beta strandi68 – 76Combined sources9
Beta strandi78 – 87Combined sources10
Turni91 – 94Combined sources4
Beta strandi96 – 104Combined sources9
Turni105 – 107Combined sources3
Helixi109 – 124Combined sources16
Beta strandi133 – 139Combined sources7
Beta strandi142 – 148Combined sources7
Beta strandi152 – 154Combined sources3
Helixi155 – 162Combined sources8
Helixi167 – 186Combined sources20
Beta strandi189 – 192Combined sources4
Helixi196 – 198Combined sources3
Beta strandi199 – 201Combined sources3
Beta strandi203 – 205Combined sources3
Beta strandi207 – 209Combined sources3
Beta strandi214 – 216Combined sources3
Helixi217 – 223Combined sources7
Turni224 – 226Combined sources3
Helixi232 – 234Combined sources3
Helixi237 – 240Combined sources4
Helixi249 – 263Combined sources15
Helixi273 – 282Combined sources10
Helixi293 – 302Combined sources10
Helixi307 – 309Combined sources3
Turni315 – 318Combined sources4
Helixi319 – 322Combined sources4
Helixi325 – 327Combined sources3
Helixi332 – 336Combined sources5
Helixi351 – 353Combined sources3
Beta strandi409 – 411Combined sources3
Helixi412 – 414Combined sources3
Turni419 – 421Combined sources3
Beta strandi422 – 430Combined sources9
Beta strandi432 – 441Combined sources10
Turni442 – 445Combined sources4
Beta strandi446 – 454Combined sources9
Turni455 – 457Combined sources3
Helixi461 – 470Combined sources10
Beta strandi479 – 484Combined sources6
Beta strandi486 – 494Combined sources9
Helixi501 – 506Combined sources6
Helixi513 – 532Combined sources20
Helixi542 – 544Combined sources3
Beta strandi545 – 551Combined sources7
Helixi554 – 556Combined sources3
Beta strandi557 – 559Combined sources3
Beta strandi571 – 573Combined sources3
Helixi587 – 613Combined sources27
Helixi626 – 635Combined sources10
Helixi643 – 645Combined sources3
Beta strandi646 – 648Combined sources3
Helixi650 – 659Combined sources10
Turni664 – 666Combined sources3
Helixi670 – 673Combined sources4
Helixi677 – 680Combined sources4
Helixi682 – 684Combined sources3
Helixi696 – 710Combined sources15
Helixi711 – 713Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4D9TX-ray2.40A399-740[»]
4D9UX-ray2.40A399-740[»]
4JG6X-ray2.60A399-740[»]
4JG7X-ray3.00A399-740[»]
4JG8X-ray3.10A399-740[»]
4NUSX-ray2.39A39-359[»]
4NW5X-ray1.94A39-359[»]
4NW6X-ray1.74A39-359[»]
5D9KX-ray2.55A/B39-366[»]
5D9LX-ray2.15A39-359[»]
ProteinModelPortaliP51812.
SMRiP51812.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini68 – 327Protein kinase 1PROSITE-ProRule annotationAdd BLAST260
Domaini328 – 397AGC-kinase C-terminalAdd BLAST70
Domaini422 – 679Protein kinase 2PROSITE-ProRule annotationAdd BLAST258

Sequence similaritiesi

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0598. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00880000137853.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP51812.
KOiK04373.
OMAiYTLNRQD.
OrthoDBiEOG091G05Z7.
PhylomeDBiP51812.
TreeFamiTF313438.

Family and domain databases

InterProiView protein in InterPro
IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016239. Ribosomal_S6_kinase_II.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF00069. Pkinase. 2 hits.
PF00433. Pkinase_C. 1 hit.
PIRSFiPIRSF000606. Ribsml_S6_kin_2. 1 hit.
SMARTiView protein in SMART
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 2 hits.
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiView protein in PROSITE
PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 2 hits.

Sequencei

Sequence statusi: Complete.

P51812-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLAQLADPW QKMAVESPSD SAENGQQIMD EPMGEEEINP QTEEVSIKEI 
        60         70         80         90        100
AITHHVKEGH EKADPSQFEL LKVLGQGSFG KVFLVKKISG SDARQLYAMK 
       110        120        130        140        150
VLKKATLKVR DRVRTKMERD ILVEVNHPFI VKLHYAFQTE GKLYLILDFL 
       160        170        180        190        200
RGGDLFTRLS KEVMFTEEDV KFYLAELALA LDHLHSLGII YRDLKPENIL 
       210        220        230        240        250
LDEEGHIKLT DFGLSKESID HEKKAYSFCG TVEYMAPEVV NRRGHTQSAD 
       260        270        280        290        300
WWSFGVLMFE MLTGTLPFQG KDRKETMTMI LKAKLGMPQF LSPEAQSLLR 
       310        320        330        340        350
MLFKRNPANR LGAGPDGVEE IKRHSFFSTI DWNKLYRREI HPPFKPATGR 
       360        370        380        390        400
PEDTFYFDPE FTAKTPKDSP GIPPSANAHQ LFRGFSFVAI TSDDESQAMQ 
       410        420        430        440        450
TVGVHSIVQQ LHRNSIQFTD GYEVKEDIGV GSYSVCKRCI HKATNMEFAV 
       460        470        480        490        500
KIIDKSKRDP TEEIEILLRY GQHPNIITLK DVYDDGKYVY VVTELMKGGE 
       510        520        530        540        550
LLDKILRQKF FSEREASAVL FTITKTVEYL HAQGVVHRDL KPSNILYVDE 
       560        570        580        590        600
SGNPESIRIC DFGFAKQLRA ENGLLMTPCY TANFVAPEVL KRQGYDAACD 
       610        620        630        640        650
IWSLGVLLYT MLTGYTPFAN GPDDTPEEIL ARIGSGKFSL SGGYWNSVSD 
       660        670        680        690        700
TAKDLVSKML HVDPHQRLTA ALVLRHPWIV HWDQLPQYQL NRQDAPHLVK 
       710        720        730        740
GAMAATYSAL NRNQSPVLEP VGRSTLAQRR GIKKITSTAL
Length:740
Mass (Da):83,736
Last modified:October 1, 1996 - v1
Checksum:i486AE8357CEAB6C8
GO

Sequence cautioni

The sequence BAD92170 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti89S → L in AAH96303 (PubMed:15489334).Curated1
Sequence conflicti410Missing in BAD92170 (Ref. 3) Curated1
Sequence conflicti424V → L in AAC82495 (PubMed:8141249).Curated1
Sequence conflicti480K → N in AAC82495 (PubMed:8141249).Curated1
Sequence conflicti494Missing in AAC82495 (PubMed:8141249).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00618838I → S2 PublicationsCorresponds to variant dbSNP:rs56218010Ensembl.1
Natural variantiVAR_00618975G → V in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454124Ensembl.1
Natural variantiVAR_00619082V → F in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454126Ensembl.1
Natural variantiVAR_006191114R → W in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454127Ensembl.1
Natural variantiVAR_065892115T → S in MRX19. 1 PublicationCorresponds to variant dbSNP:rs387906703Ensembl.1
Natural variantiVAR_006192127H → Q in CLS. 1 Publication1
Natural variantiVAR_065893152Missing in MRX19. 1 Publication1
Natural variantiVAR_006193154D → Y in CLS. 1 Publication1
Natural variantiVAR_065894189I → K in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454130Ensembl.1
Natural variantiVAR_065895202Missing in MRX19. 1 Publication1
Natural variantiVAR_006194225A → V in CLS. 1 PublicationCorresponds to variant dbSNP:rs879027948Ensembl.1
Natural variantiVAR_006195227S → A in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454125Ensembl.1
Natural variantiVAR_065896268F → S in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454131Ensembl.1
Natural variantiVAR_065897383R → W in MRX19; kinase activity is decreased but not abolished. 1 PublicationCorresponds to variant dbSNP:rs122454129Ensembl.1
Natural variantiVAR_035627416I → V in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs148050184Ensembl.1
Natural variantiVAR_006196431G → D in CLS. 1 Publication1
Natural variantiVAR_065898477Missing in CLS. 1 Publication1
Natural variantiVAR_040629483Y → C in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_040630608L → F in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_040631723R → C1 PublicationCorresponds to variant dbSNP:rs35026425Ensembl.1
Natural variantiVAR_006197729R → Q in CLS. 1 PublicationCorresponds to variant dbSNP:rs28935171Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08316 mRNA. Translation: AAA81952.1.
AK313932 mRNA. Translation: BAG36651.1.
AB208933 mRNA. Translation: BAD92170.1. Different initiation.
AL732366, AL807772 Genomic DNA. Translation: CAI40548.1.
AL807772, AL732366 Genomic DNA. Translation: CAI39687.1.
BC096301 mRNA. Translation: AAH96301.1.
BC096302 mRNA. Translation: AAH96302.1.
BC096303 mRNA. Translation: AAH96303.1.
L07599 mRNA. Translation: AAC82495.1.
AB102662 mRNA. Translation: BAC81131.1.
CCDSiCCDS14197.1.
PIRiI38556.
RefSeqiNP_004577.1. NM_004586.2.
UniGeneiHs.445387.

Genome annotation databases

EnsembliENST00000379565; ENSP00000368884; ENSG00000177189.
GeneIDi6197.
KEGGihsa:6197.
UCSCiuc004czu.4. human.

Keywords - Coding sequence diversityi

Polymorphism

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.

Entry informationi

Entry nameiKS6A3_HUMAN
AccessioniPrimary (citable) accession number: P51812
Secondary accession number(s): B2R9V4
, Q4VAP3, Q59H26, Q5JPK8, Q7Z3Z7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 7, 2017
This is version 183 of the entry and version 1 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 X
    Human chromosome X: 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