ID DAB2P_RAT Reviewed; 996 AA.
AC Q6P730; Q924M9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 148.
DE RecName: Full=Disabled homolog 2-interacting protein;
DE Short=DAB2-interacting protein;
DE AltName: Full=ASK-interacting protein 1;
DE Short=AIP-1;
DE AltName: Full=DIP1/2;
DE AltName: Full=DOC-2/DAB2 interactive protein;
GN Name=Dab2ip;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 977-996, FUNCTION, TISSUE
RP SPECIFICITY, INTERACTION WITH DAB1 AND DAB2, AND MUTAGENESIS OF ARG-220.
RC TISSUE=Brain;
RX PubMed=11812785; DOI=10.1074/jbc.m110568200;
RA Wang Z., Tseng C.-P., Pong R.-C., Chen H., McConnell J.D., Navone N.,
RA Hsieh J.-T.;
RT "The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate
RT cancer. Characterization of a novel GTPase-activating protein associated
RT with N-terminal domain of DOC-2/DAB2.";
RL J. Biol. Chem. 277:12622-12631(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Functions as a scaffold protein implicated in the regulation
CC of a large spectrum of both general and specialized signaling pathways.
CC Involved in several processes such as innate immune response,
CC inflammation and cell growth inhibition, apoptosis, cell survival,
CC angiogenesis, cell migration and maturation. Also plays a role in cell
CC cycle checkpoint control; reduces G1 phase cyclin levels resulting in
CC G0/G1 cell cycle arrest. Mediates signal transduction by receptor-
CC mediated inflammatory signals, such as the tumor necrosis factor (TNF),
CC interferon (IFN) or lipopolysaccharide (LPS). Modulates the balance
CC between phosphatidylinositol 3-kinase (PI3K)-AKT-mediated cell survival
CC and apoptosis stimulated kinase (MAP3K5)-JNK signaling pathways;
CC sequesters both AKT1 and MAP3K5 and counterbalances the activity of
CC each kinase by modulating their phosphorylation status in response to
CC pro-inflammatory stimuli. Acts as a regulator of the endoplasmic
CC reticulum (ER) unfolded protein response (UPR) pathway; specifically
CC involved in transduction of the ER stress-response to the JNK cascade
CC through ERN1. Mediates TNF-alpha-induced apoptosis activation by
CC facilitating dissociation of inhibitor 14-3-3 from MAP3K5; recruits the
CC PP2A phosphatase complex which dephosphorylates MAP3K5 on 'Ser-966',
CC leading to the dissociation of 13-3-3 proteins and activation of the
CC MAP3K5-JNK signaling pathway in endothelial cells. Acts a negative
CC regulator in the IFN-gamma-mediated JAK-STAT signaling cascade by
CC inhibiting smooth muscle cell (VSMCs) proliferation and intimal
CC expansion, and thus, prevents graft arteriosclerosis (GA). Acts as a
CC GTPase-activating protein (GAP) for the ADP ribosylation factor 6
CC (ARF6). Promotes hydrolysis of the ARF6-bound GTP and thus, negatively
CC regulates phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent TLR4-
CC TIRAP-MyD88 and NF-kappa-B signaling pathways in endothelial cells in
CC response to lipopolysaccharides (LPS). Binds specifically to
CC phosphatidylinositol 4-phosphate (PtdIns4P) and phosphatidylinositol 3-
CC phosphate (PtdIns3P). In response to vascular endothelial growth factor
CC (VEGFA), acts as a negative regulator of the VEGFR2-PI3K-mediated
CC angiogenic signaling pathway by inhibiting endothelial cell migration
CC and tube formation. In the developing brain, promotes both the
CC transition from the multipolar to the bipolar stage and the radial
CC migration of cortical neurons from the ventricular zone toward the
CC superficial layer of the neocortex in a glial-dependent locomotion
CC process. Probable downstream effector of the Reelin signaling pathway;
CC promotes Purkinje cell (PC) dendrites development and formation of
CC cerebellar synapses. Functions also as a tumor suppressor protein in
CC prostate cancer progression; prevents cell proliferation and
CC epithelial-to-mesenchymal transition (EMT) through activation of the
CC glycogen synthase kinase-3 beta (GSK3B)-induced beta-catenin and
CC inhibition of PI3K-AKT and Ras-MAPK survival downstream signaling
CC cascades, respectively (By similarity). Mediates TNF/TRAF2-induced
CC MAP3K5-JNK activation, while it inhibits CHUK-NF-kappa-B signaling.
CC Functions as a Ras GTPase-activating protein. May act as a tumor
CC suppressor gene. {ECO:0000250, ECO:0000269|PubMed:11812785}.
CC -!- SUBUNIT: On plasma membrane, exists in an inactive form complexed with
CC TNFR1; in response to TNF-alpha, dissociates from TNFR1 complex,
CC translocates to cytoplasm and forms part of an intracellular signaling
CC complex comprising TRADD, RIPK1, TRAF2 and MAP3K5. Interacts (via NPXY
CC motif) with DAB2 (via PID domain). Interacts (via PH domain) with ERN1.
CC Part of a cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in
CC response to TNF-alpha; this complex formation promotes MAP3K5-JNK
CC activation and subsequent apoptosis. Interacts (via N-terminal domain)
CC with JAK2; the interaction occurs in a IFNG/IFN-gamma-dependent manner
CC and inhibits JAK2 autophosphorylation activity. Interacts (via C2
CC domain) with GSK3B; the interaction stimulates GSK3B kinase activation.
CC Interacts (via C2 domain) with PPP2CA. Interacts (via proline-rich
CC motif) with a regulatory p85 subunit (via SH3 domain) of the PI3K
CC complex; the interaction inhibits the PI3K-AKT complex activity in a
CC TNF-alpha-dependent manner in prostate cancer (PCa) cells. Interacts
CC with AKT1; the interaction is increased in a TNF-alpha-induced manner.
CC Interacts (via C2 domain and active form preferentially) with
CC KDR/VEGFR2 (tyrosine-phosphorylated active form preferentially); the
CC interaction occurs at the late phase of VEGFA response and inhibits
CC KDR/VEGFR2 activity. Interacts (via N-terminus C2 domain) with MAP3K5
CC ('Ser-966' dephosphorylated form preferentially); the interaction
CC occurs in a TNF-alpha-induced manner. Interacts (via Ras-GAP domain)
CC with the catalytic subunit of protein phosphatase PP2A; the interaction
CC occurs in resting endothelial cells, is further enhanced by TNF-alpha
CC stimulation and is required to bridge PP2A to MAP3K5. Interacts (via C-
CC terminus PER domain) with TRAF2 (via zinc fingers); the interaction
CC occurs in a TNF-alpha-dependent manner. Interacts with 14-3-3 proteins;
CC the interaction occurs in a TNF-alpha-dependent manner. Interacts (via
CC Ras-GAP domain) with RIPK1 (via kinase domain); the interaction occurs
CC in a TNF-alpha-dependent manner (By similarity). Interacts with DAB1
CC and DAB2. {ECO:0000250, ECO:0000269|PubMed:11812785}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane
CC {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Localized
CC in soma and dendrites of Purkinje cells as well as in scattered cell
CC bodies in the molecular layer of the cerebellum. Colocalizes with TIRAP
CC at the plasma membrane. Colocalizes with ARF6 at the plasma membrane
CC and endocytic vesicles. Translocates from the plasma membrane to the
CC cytoplasm in response to TNF-alpha. Phosphatidylinositol 4-phosphate
CC (PtdIns4P) binding is essential for plasma membrane localization (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, lung, thymus, bladder and
CC skeletal muscle. Up-regulatedd during prostate degeneration.
CC {ECO:0000269|PubMed:11812785}.
CC -!- DOMAIN: Exists in a closed inactive form by an intramolecular
CC interaction between the N- and the C-terminal domains. The proline-rich
CC motif is critical both for PI3K-AKT activity inhibition and MAP3K5
CC activation. The PH and C2 domains are necessary for the binding to
CC phosphatidylinositol phosphate. The Ras-GAP domain is necessary for its
CC tumor-suppressive function. The C2 and Ras-GAP domains constitutively
CC bind to MAP3K5 and facilitate the release of 14-3-3 proteins from
CC MAP3K5. The PH and Ras-GAP domains, but not the NPXY motif, are crucial
CC for its cell membrane localization and neuronal migration function. The
CC PH domain is necessary but not sufficient to activate the JNK signaling
CC pathway through ERN1 (By similarity). {ECO:0000250}.
CC -!- PTM: In response to TNF-alpha-induction, phosphorylated at Ser-535;
CC phosphorylation leads to a conformational change, and thus, increases
CC its association with 14-3-3 proteins, MAP3K5, RIPK1 and TRAF2 in
CC endothelial cells; also stimulates regulatory p85 subunit sequestring
CC and PI3K-p85 complex activity inhibition. {ECO:0000250}.
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DR EMBL; BC061865; AAH61865.1; -; mRNA.
DR EMBL; AF236130; AAK93947.1; -; mRNA.
DR RefSeq; NP_619724.3; NM_138710.3.
DR AlphaFoldDB; Q6P730; -.
DR SMR; Q6P730; -.
DR BioGRID; 251329; 1.
DR STRING; 10116.ENSRNOP00000068688; -.
DR iPTMnet; Q6P730; -.
DR PhosphoSitePlus; Q6P730; -.
DR jPOST; Q6P730; -.
DR PaxDb; 10116-ENSRNOP00000056740; -.
DR GeneID; 192126; -.
DR KEGG; rno:192126; -.
DR UCSC; RGD:621686; rat.
DR AGR; RGD:621686; -.
DR CTD; 153090; -.
DR RGD; 621686; Dab2ip.
DR VEuPathDB; HostDB:ENSRNOG00000055226; -.
DR eggNOG; KOG3508; Eukaryota.
DR InParanoid; Q6P730; -.
DR OrthoDB; 22721at2759; -.
DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR PRO; PR:Q6P730; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000055226; Expressed in skeletal muscle tissue and 19 other cell types or tissues.
DR ExpressionAtlas; Q6P730; baseline and differential.
DR Genevisible; Q6P730; RN.
DR GO; GO:1990597; C:AIP1-IRE1 complex; ISO:RGD.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0044300; C:cerebellar mossy fiber; ISS:UniProtKB.
DR GO; GO:0044301; C:climbing fiber; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
DR GO; GO:1990032; C:parallel fiber; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISO:RGD.
DR GO; GO:0005123; F:death receptor binding; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:RGD.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:RGD.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISS:UniProtKB.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:RGD.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
DR GO; GO:0035591; F:signaling adaptor activity; ISO:RGD.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0021814; P:cell motility involved in cerebral cortex radial glia guided migration; ISS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:BHF-UCL.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0021819; P:layer formation in cerebral cortex; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0070317; P:negative regulation of G0 to G1 transition; ISS:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IDA:RGD.
DR GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISS:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:2001224; P:positive regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:1900744; P:regulation of p38MAPK cascade; ISS:UniProtKB.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0035148; P:tube formation; ISS:UniProtKB.
DR GO; GO:0036324; P:vascular endothelial growth factor receptor-2 signaling pathway; ISS:UniProtKB.
DR CDD; cd04013; C2_SynGAP_like; 1.
DR CDD; cd05136; RasGAP_DAB2IP; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR021887; DAB2P_C.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR10194:SF26; DISABLED HOMOLOG 2-INTERACTING PROTEIN; 1.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12004; DAB2P_C; 1.
DR Pfam; PF00616; RasGAP; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Apoptosis; Cell cycle; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasm; Developmental protein; Direct protein sequencing;
KW Growth regulation; GTPase activation; Membrane; Phosphoprotein;
KW Reference proteome; Stress response; Tumor suppressor;
KW Unfolded protein response.
FT CHAIN 1..996
FT /note="Disabled homolog 2-interacting protein"
FT /id="PRO_0000252409"
FT DOMAIN 1..118
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 178..370
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT REGION 453..750
FT /note="Necessary for interaction with AKT1"
FT /evidence="ECO:0000250"
FT REGION 460..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 832..966
FT /evidence="ECO:0000255"
FT COMPBIAS 656..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..742
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 535
FT /note="Phosphoserine; by MAP3K5 and RIPK1"
FT /evidence="ECO:0000250|UniProtKB:Q5VWQ8"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWQ8"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWQ8"
FT MUTAGEN 220
FT /note="R->L: Loss of GAP activity."
FT /evidence="ECO:0000269|PubMed:11812785"
FT CONFLICT 228
FT /note="A -> G (in Ref. 1; AAK93947)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="Q -> H (in Ref. 1; AAK93947)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="G -> C (in Ref. 1; AAK93947)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="A -> T (in Ref. 1; AAK93947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 996 AA; 110005 MW; CA6B43D3129F4D6E CRC64;
MENLRRAVHP NKDNSRRVEH ILKLWVIEAK DLPAKKKYLC ELCLDDVLYA RTTGKLKTDN
VFWGEHFEFH NLPPLRTVTV HLYRETDKKK KKERNSYLGL VSLPAASVAG RQFVEKWYPV
VTPNPKGGKG PGPMIRIKAR YQTITILPME MYKEFAEHIT NHYLGLCAAL EPILSAKTKE
EMASALVHIL QSTGKVKDFL TDLMMSEVDR CGDNEHLIFR ENTLATKAIE EYLKLVGQKY
LQDALGEFIK ALYESDENCE VDPSKCSAAD LPEHQGNLKM CCELAFCKII NSYCVFPREL
KEVFASWRQE CSSRGRPDIS ERLISASLFL RFLCPAIMSP SLFNLLQEYP DDRTARTLTL
IAKVTQNLAN FAKFGSKEEY MSFMNQFLEH EWTNMQRFLL EISNPETLSN TAGFEGYIDL
GRELSSLHSL LWEAVSQLDQ SIVSKLGPLP RILRDVHTAL STPGSGQLPG TNDLASTPGS
GSSSVSAGLQ KMVIENDLSG LIDFTRLPSP TPENKDLFFV TRSSGVQPSP ARSSSYSEAN
EPDLQMANGS KSLSMVDLQD ARTLDGEAGS PVGPEALPAD GQVPATQLVA GWPARAAPVS
LAGLATVRRA VPTPTTPGTS EGAPGRPQLL APLSFQNPVY QMAAGLPLSP RGLGDSGSEG
HSSLSSHSNS EELAAAAKLG SFSTAAEELA RRPGELARRQ MSLTEKGGQP TVPRQNSAGP
QRRIDQPPPP PPPPPPAPRG RTPPTMLSTL QYPRPSSGTL ASASPDWAGP GTRLRQQSSS
SKGDSPELKP RALHKQGPSP VSPNALDRTA AWLLTMNAQL LEDEGLGPDP PHRDRLRSKE
ELSQAEKDLA VLQDKLRIST KKLEEYETLF KCQEETTQKL VLEYQARLEE GEERLRRQQE
DKDVQMKGII SRLMSVEEEL KKDHAEMQAA VDSKQKIIDA QEKRIASLDA ANARLMSALT
QLKERYSMRA RNGVSPTNPT KLQITENGEF RNSSNC
//
