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Protein

Receptor-interacting serine/threonine-protein kinase 2

Gene

RIPK2

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

Functioni

Serine/threonine/tyrosine kinase that plays an essential role in modulation of innate and adaptive immune responses. Upon stimulation by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize and recruit RIPK2 through CARD-CARD domains. Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3. The polyubiquitinated protein mediates the recruitment of MAP3K7/TAK1 to IKBKG/NEMO and induces 'Lys-63'-linked polyubiquitination of IKBKG/NEMO and subsequent activation of IKBKB/IKKB. In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Plays also a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation.5 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471ATP
Active sitei146 – 1461Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 329ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • CARD domain binding Source: UniProtKB
  • LIM domain binding Source: UniProtKB
  • non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  • protein homodimerization activity Source: BHF-UCL
  • protein serine/threonine kinase activity Source: Reactome
  • receptor binding Source: UniProtKB
  • signal transducer activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Adaptive immunity, Apoptosis, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiR-HSA-168638. NOD1/2 Signaling Pathway.
R-HSA-202424. Downstream TCR signaling.
R-HSA-209543. p75NTR recruits signalling complexes.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-446652. Interleukin-1 signaling.
R-HSA-450302. activated TAK1 mediates p38 MAPK activation.
R-HSA-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
SignaLinkiO43353.
SIGNORiO43353.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-interacting serine/threonine-protein kinase 2 (EC:2.7.11.1)
Alternative name(s):
CARD-containing interleukin-1 beta-converting enzyme-associated kinase
Short name:
CARD-containing IL-1 beta ICE-kinase
RIP-like-interacting CLARP kinase
Receptor-interacting protein 2
Short name:
RIP-2
Tyrosine-protein kinase RIPK2 (EC:2.7.10.2)
Gene namesi
Name:RIPK2
Synonyms:CARDIAK, RICK, RIP2
ORF Names:UNQ277/PRO314/PRO34092
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:10020. RIPK2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB
  • cytosol Source: Reactome
  • protein complex Source: UniProtKB
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471K → A: Abolishes kinase activity. 2 Publications
Mutagenesisi47 – 471K → M: Reduces FAS-mediated apoptosis. 2 Publications
Mutagenesisi146 – 1461D → N: Abolishes kinase activity. 1 Publication
Mutagenesisi209 – 2091K → R: Complete loss of polyubiquitination. 1 Publication
Mutagenesisi381 – 3811Y → A: Prevents phosphorylation. Reduces serine and threonine phosphorylation of ARHGEF2.
Mutagenesisi444 – 4441R → E: Abolishes interaction with NOD1. 1 Publication
Mutagenesisi474 – 4741Y → F: Decreases interaction with NOD2. 1 Publication
Mutagenesisi483 – 4831R → E: Abolishes interaction with NOD1. 1 Publication
Mutagenesisi488 – 4881R → E: Abolishes interaction with NOD1. 1 Publication

Organism-specific databases

PharmGKBiPA34395.

Chemistry

ChEMBLiCHEMBL5014.
GuidetoPHARMACOLOGYi2190.

Polymorphism and mutation databases

BioMutaiRIPK2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 540540Receptor-interacting serine/threonine-protein kinase 2PRO_0000086608Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei168 – 1681PhosphoserineCombined sources
Modified residuei176 – 1761Phosphoserine; by autocatalysis1 Publication
Cross-linki209 – 209Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei363 – 3631PhosphoserineCombined sources
Modified residuei381 – 3811Phosphotyrosine; by CSK1 Publication
Modified residuei393 – 3931PhosphoserineCombined sources
Modified residuei474 – 4741Phosphotyrosine; by autocatalysis1 Publication
Modified residuei527 – 5271PhosphoserineCombined sources
Modified residuei529 – 5291PhosphoserineCombined sources
Modified residuei531 – 5311PhosphoserineCombined sources
Modified residuei539 – 5391PhosphoserineCombined sources

Post-translational modificationi

Autophosphorylated. Autophosphorylation at Tyr-474 is necessary for effective NOD2 signaling. Phosphorylated. Phosphorylation at Tyr-381 by Src kinase CSK occurs in a ARHGEF2-dependent manner and is required for NOD2-dependent innate immune activation.3 Publications
Ubiquitinated on Lys-209; undergoes 'Lys-63'-linked polyubiquitination catalyzed by ITCH. Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B. Also undergoes 'Met-1'-linked polyubiquitination; the head-to-tail linear polyubiquitination is mediated by the LUBAC complex in response to NOD2 stimulation. Linear polyubiquitination is restricted by FAM105B/otulin, probably to limit NOD2-dependent proinflammatory signaling activation of NF-kappa-B.5 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO43353.
MaxQBiO43353.
PaxDbiO43353.
PeptideAtlasiO43353.
PRIDEiO43353.

PTM databases

iPTMnetiO43353.
PhosphoSiteiO43353.

Expressioni

Tissue specificityi

Detected in heart, brain, placenta, lung, peripheral blood leukocytes, spleen, kidney, testis, prostate, pancreas and lymph node.

Gene expression databases

BgeeiENSG00000104312.
CleanExiHS_RIPK2.
ExpressionAtlasiO43353. baseline and differential.
GenevisibleiO43353. HS.

Organism-specific databases

HPAiHPA015273.
HPA016499.

Interactioni

Subunit structurei

Found in a signaling complex consisting of at least ARHGEF2, NOD2 and RIPK2. Interacts with ARHGEF2; the interaction mediates tyrosine phosphorylation of RIPK2 by Src kinase CSK. Binds to CFLAR/CLARP and CASP1 via their CARD domains. Binds to BIRC3/c-IAP1 and BIRC2/c-IAP2, TRAF1, TRAF2, TRAF5 and TRAF6. May be a component of both the TNFRSF1A and TNRFSF5/CD40 receptor complex. Interacts with NOD1. Interacts (via CARD domain) with NOD2 (via CARD domain). Interacts with MAP3K4; this interaction sequesters RIPK2 from the NOD2 signaling pathway. Interacts with IKBKG/NEMO. The polyubiquitinated protein interacts with MAP3K7/TAK1. Interacts with XIAP/BIRC4. Interacts with NLRP10. Interacts with CARD9.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BIRC2Q134903EBI-358522,EBI-514538
BIRC3Q134893EBI-358522,EBI-517709
MAVSQ7Z4343EBI-358522,EBI-995373
NOD2Q9HC292EBI-358522,EBI-7445625
TRAF3Q131145EBI-358522,EBI-357631
XIAPP981704EBI-358522,EBI-517127

GO - Molecular functioni

  • CARD domain binding Source: UniProtKB
  • LIM domain binding Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114300. 44 interactions.
DIPiDIP-27518N.
IntActiO43353. 13 interactions.
MINTiMINT-90752.
STRINGi9606.ENSP00000220751.

Chemistry

BindingDBiO43353.

Structurei

Secondary structure

1
540
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Helixi15 – 173Combined sources
Beta strandi18 – 258Combined sources
Beta strandi31 – 377Combined sources
Turni38 – 403Combined sources
Beta strandi43 – 486Combined sources
Helixi59 – 7214Combined sources
Beta strandi81 – 866Combined sources
Beta strandi91 – 966Combined sources
Helixi103 – 1086Combined sources
Turni110 – 1123Combined sources
Helixi118 – 13619Combined sources
Beta strandi138 – 1403Combined sources
Helixi149 – 1513Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi160 – 1623Combined sources
Helixi190 – 1923Combined sources
Helixi195 – 1973Combined sources
Turni202 – 2043Combined sources
Helixi210 – 22415Combined sources
Beta strandi228 – 2314Combined sources
Helixi235 – 2439Combined sources
Turni252 – 2543Combined sources
Helixi262 – 27211Combined sources
Helixi277 – 2793Combined sources
Helixi283 – 29412Combined sources
Helixi299 – 3079Combined sources
Helixi436 – 45015Combined sources
Helixi453 – 46513Combined sources
Helixi471 – 4766Combined sources
Helixi483 – 49715Combined sources
Helixi501 – 51111Combined sources
Beta strandi526 – 5283Combined sources
Turni530 – 5323Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2N7ZNMR-A434-539[»]
2N83NMR-B434-539[»]
4C8BX-ray2.75A/B8-317[»]
5AR2X-ray2.44A/B1-310[»]
5AR3X-ray3.23A/B1-310[»]
5AR4X-ray2.70A/B1-310[»]
5AR5X-ray2.66A/B1-310[»]
5AR7X-ray2.71A/B1-310[»]
5AR8X-ray2.79A/B1-310[»]
5J79X-ray2.69A/B1-310[»]
5J7BX-ray2.53A/B1-310[»]
ProteinModelPortaliO43353.
SMRiO43353. Positions 9-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 294277Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini432 – 52493CARDPROSITE-ProRule annotationAdd
BLAST

Domaini

Contains an N-terminal kinase domain and a C-terminal caspase activation and recruitment domain (CARD) that mediates the recruitment of CARD-containing proteins.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0192. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00550000074536.
HOGENOMiHOG000136856.
HOVERGENiHBG054242.
InParanoidiO43353.
KOiK08846.
OMAiPFEEVIN.
OrthoDBiEOG091G0505.
PhylomeDBiO43353.
TreeFamiTF106506.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017322. Rcpt-int_Ser/Thr_kinase-2.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF037921. STPK_RIP2. 1 hit.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43353-1) [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
MNGEAICSAL PTIPYHKLAD LRYLSRGASG TVSSARHADW RVQVAVKHLH
60 70 80 90 100
IHTPLLDSER KDVLREAEIL HKARFSYILP ILGICNEPEF LGIVTEYMPN
110 120 130 140 150
GSLNELLHRK TEYPDVAWPL RFRILHEIAL GVNYLHNMTP PLLHHDLKTQ
160 170 180 190 200
NILLDNEFHV KIADFGLSKW RMMSLSQSRS SKSAPEGGTI IYMPPENYEP
210 220 230 240 250
GQKSRASIKH DIYSYAVITW EVLSRKQPFE DVTNPLQIMY SVSQGHRPVI
260 270 280 290 300
NEESLPYDIP HRARMISLIE SGWAQNPDER PSFLKCLIEL EPVLRTFEEI
310 320 330 340 350
TFLEAVIQLK KTKLQSVSSA IHLCDKKKME LSLNIPVNHG PQEESCGSSQ
360 370 380 390 400
LHENSGSPET SRSLPAPQDN DFLSRKAQDC YFMKLHHCPG NHSWDSTISG
410 420 430 440 450
SQRAAFCDHK TTPCSSAIIN PLSTAGNSER LQPGIAQQWI QSKREDIVNQ
460 470 480 490 500
MTEACLNQSL DALLSRDLIM KEDYELVSTK PTRTSKVRQL LDTTDIQGEE
510 520 530 540
FAKVIVQKLK DNKQMGLQPY PEILVVSRSP SLNLLQNKSM
Length:540
Mass (Da):61,195
Last modified:November 1, 1998 - v2
Checksum:i575A692239505792
GO
Isoform 2 (identifier: O43353-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: Missing.

Show »
Length:403
Mass (Da):45,582
Checksum:i9F0DE53A01B25EF5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2711S → G in BAH13484 (PubMed:14702039).Curated
Sequence conflicti514 – 5141Q → R in BAH13484 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti259 – 2591I → T.1 Publication
Corresponds to variant rs2230801 [ dbSNP | Ensembl ].
VAR_041045
Natural varianti268 – 2681L → V.1 Publication
Corresponds to variant rs35004667 [ dbSNP | Ensembl ].
VAR_041046
Natural varianti313 – 3131K → N.1 Publication
Corresponds to variant rs35395048 [ dbSNP | Ensembl ].
VAR_041047

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 137137Missing in isoform 2. 2 PublicationsVSP_013266Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027706 mRNA. Translation: AAC34970.1.
AF078530 mRNA. Translation: AAC27722.1.
AF064824 mRNA. Translation: AAC25668.1.
AY358813 mRNA. Translation: AAQ89172.1.
AY358814 mRNA. Translation: AAQ89173.1.
AK301448 mRNA. Translation: BAH13484.1.
AC004003 Genomic DNA. Translation: AAC24561.1.
AF117829 Genomic DNA. No translation available.
BC004553 mRNA. Translation: AAH04553.1.
CCDSiCCDS6247.1. [O43353-1]
RefSeqiNP_003812.1. NM_003821.5. [O43353-1]
XP_005251149.1. XM_005251092.3. [O43353-2]
UniGeneiHs.103755.

Genome annotation databases

EnsembliENST00000220751; ENSP00000220751; ENSG00000104312. [O43353-1]
GeneIDi8767.
KEGGihsa:8767.
UCSCiuc003yee.4. human. [O43353-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027706 mRNA. Translation: AAC34970.1.
AF078530 mRNA. Translation: AAC27722.1.
AF064824 mRNA. Translation: AAC25668.1.
AY358813 mRNA. Translation: AAQ89172.1.
AY358814 mRNA. Translation: AAQ89173.1.
AK301448 mRNA. Translation: BAH13484.1.
AC004003 Genomic DNA. Translation: AAC24561.1.
AF117829 Genomic DNA. No translation available.
BC004553 mRNA. Translation: AAH04553.1.
CCDSiCCDS6247.1. [O43353-1]
RefSeqiNP_003812.1. NM_003821.5. [O43353-1]
XP_005251149.1. XM_005251092.3. [O43353-2]
UniGeneiHs.103755.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2N7ZNMR-A434-539[»]
2N83NMR-B434-539[»]
4C8BX-ray2.75A/B8-317[»]
5AR2X-ray2.44A/B1-310[»]
5AR3X-ray3.23A/B1-310[»]
5AR4X-ray2.70A/B1-310[»]
5AR5X-ray2.66A/B1-310[»]
5AR7X-ray2.71A/B1-310[»]
5AR8X-ray2.79A/B1-310[»]
5J79X-ray2.69A/B1-310[»]
5J7BX-ray2.53A/B1-310[»]
ProteinModelPortaliO43353.
SMRiO43353. Positions 9-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114300. 44 interactions.
DIPiDIP-27518N.
IntActiO43353. 13 interactions.
MINTiMINT-90752.
STRINGi9606.ENSP00000220751.

Chemistry

BindingDBiO43353.
ChEMBLiCHEMBL5014.
GuidetoPHARMACOLOGYi2190.

PTM databases

iPTMnetiO43353.
PhosphoSiteiO43353.

Polymorphism and mutation databases

BioMutaiRIPK2.

Proteomic databases

EPDiO43353.
MaxQBiO43353.
PaxDbiO43353.
PeptideAtlasiO43353.
PRIDEiO43353.

Protocols and materials databases

DNASUi8767.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000220751; ENSP00000220751; ENSG00000104312. [O43353-1]
GeneIDi8767.
KEGGihsa:8767.
UCSCiuc003yee.4. human. [O43353-1]

Organism-specific databases

CTDi8767.
GeneCardsiRIPK2.
HGNCiHGNC:10020. RIPK2.
HPAiHPA015273.
HPA016499.
MIMi603455. gene.
neXtProtiNX_O43353.
PharmGKBiPA34395.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0192. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00550000074536.
HOGENOMiHOG000136856.
HOVERGENiHBG054242.
InParanoidiO43353.
KOiK08846.
OMAiPFEEVIN.
OrthoDBiEOG091G0505.
PhylomeDBiO43353.
TreeFamiTF106506.

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiR-HSA-168638. NOD1/2 Signaling Pathway.
R-HSA-202424. Downstream TCR signaling.
R-HSA-209543. p75NTR recruits signalling complexes.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-446652. Interleukin-1 signaling.
R-HSA-450302. activated TAK1 mediates p38 MAPK activation.
R-HSA-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
SignaLinkiO43353.
SIGNORiO43353.

Miscellaneous databases

ChiTaRSiRIPK2. human.
GeneWikiiRIPK2.
GenomeRNAii8767.
PROiO43353.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000104312.
CleanExiHS_RIPK2.
ExpressionAtlasiO43353. baseline and differential.
GenevisibleiO43353. HS.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017322. Rcpt-int_Ser/Thr_kinase-2.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF037921. STPK_RIP2. 1 hit.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRIPK2_HUMAN
AccessioniPrimary (citable) accession number: O43353
Secondary accession number(s): B7Z748, Q6UWF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1998
Last modified: September 7, 2016
This is version 179 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, 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.