ID A0A3B3ITG3_HUMAN Unreviewed; 1128 AA.
AC A0A3B3ITG3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=DAB2 interacting protein {ECO:0000313|Ensembl:ENSP00000497706.1};
GN Name=DAB2IP {ECO:0000313|Ensembl:ENSP00000497706.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000497706.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000497706.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2] {ECO:0007829|PubMed:18669648}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [3] {ECO:0007829|PubMed:21269460}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [4] {ECO:0007829|PubMed:21406692}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [5] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [6] {ECO:0000313|Ensembl:ENSP00000497706.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AL357936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005251781.1; XM_005251724.4.
DR AlphaFoldDB; A0A3B3ITG3; -.
DR SMR; A0A3B3ITG3; -.
DR MassIVE; A0A3B3ITG3; -.
DR PeptideAtlas; A0A3B3ITG3; -.
DR Antibodypedia; 48362; 146 antibodies from 20 providers.
DR Ensembl; ENST00000648444.1; ENSP00000497706.1; ENSG00000136848.19.
DR HGNC; HGNC:17294; DAB2IP.
DR VEuPathDB; HostDB:ENSG00000136848; -.
DR GeneTree; ENSGT00940000155853; -.
DR ChiTaRS; DAB2IP; human.
DR Proteomes; UP000005640; Chromosome 9.
DR Bgee; ENSG00000136848; Expressed in right hemisphere of cerebellum and 179 other cell types or tissues.
DR ExpressionAtlas; A0A3B3ITG3; baseline and differential.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR CDD; cd04013; C2_SynGAP_like; 1.
DR CDD; cd05136; RasGAP_DAB2IP; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR021887; DAB2P_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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 SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Proteomics identification {ECO:0007829|EPD:A0A3B3ITG3,
KW ECO:0007829|MaxQB:A0A3B3ITG3};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT DOMAIN 107..141
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 132..250
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 310..502
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 28..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1070..1097
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 654..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..874
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..974
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1128 AA; 124418 MW; 6D44969824F5E93D CRC64;
MGLCGLGLLS DNFGKILGRA GGAAHWRPGH LRKPDLAPEP RGLQVPRTRS AERPALPPQR
SHLMPRLKES RSHESLLSPS SAVEALDLSM EEEVVIKPVH SSILGQDYCF EVTTSSGSKC
FSCRSAAERD KWMENLRRAV HPNKDNSRRV EHILKLWVIE AKDLPAKKKY LCELCLDDVL
YARTTGKLKT DNVFWGEHFE FHNLPPLRTV TVHLYRETDK KKKKERNSYL GLVSLPAASV
AGRQFVEKWY PVVTPNPKGG KGPGPMIRIK ARYQTITILP MEMYKEFAEH ITNHYLGLCA
ALEPILSAKT KEEMASALVH ILQSTGKVKD FLTDLMMSEV DRCGDNEHLI FRENTLATKA
IEEYLKLVGQ KYLQDALGEF IKALYESDEN CEVDPSKCSA ADLPEHQGNL KMCCELAFCK
IINSYCVFPR ELKEVFASWR QECSSRGRPD ISERLISASL FLRFLCPAIM SPSLFNLLQE
YPDDRTARTL TLIAKVTQNL ANFAKFGSKE EYMSFMNQFL EHEWTNMQRF LLEISNPETL
SNTAGFEGYI DLGRELSSLH SLLWEAVSQL EQSIVSKLGP LPRILRDVHT ALSTPGSGQL
PGTNDLASTP GSGSSSISAG LQKMVIENDL SGLIDFTRLP SPTPENKDLF FVTRSSGVQP
SPARSSSYSE ANEPDLQMAN GGKSLSMVDL QDARTLDGEA GSPAGPDVLP TDGQAAAAQL
VAGWPARATP VNLAGLATVR RAGQTPTTPG TSEGAPGRPQ LLAPLSFQNP VYQMAAGLPL
SPRGLGDSGS EGHSSLSSHS NSEELAAAAK LGSFSTAAEE LARRPGELAR RQMSLTEKGG
QPTVPRQNSA GPQRRIDQPP PPPPPPPPAP RGRTPPNLLS TLQYPRPSSG TLASASPDWV
GPSTRLRQQS SSSKGDSPEL KPRAVHKQGP SPVSPNALDR TAAWLLTMNA QLLEDEGLGP
DPPHRDRLRS KDELSQAEKD LAVLQDKLRI STKKLEEYET LFKCQEETTQ KLVLEYQARL
EEGEERLRRQ QEDKDIQMKG IISRLMSVEE ELKKDHAEMQ AAVDSKQKII DAQEKRIASL
DAANARLMSA LTQLKERYSM QARNGISPTN PTKLQITENG EFRNSSNC
//
