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Ras-related protein Rab-4A

 RAB4A_HUMAN             Reviewed;         218 AA.
P20338; Q5T7P7; Q9BQ44;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
06-MAR-2013, sequence version 3.
25-OCT-2017, entry version 192.
RecName: Full=Ras-related protein Rab-4A;
Name=RAB4A; Synonyms=RAB4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2501306;
Zahraoui A., Touchot N., Chardin P., Tavitian A.;
"The human Rab genes encode a family of GTP-binding proteins related
to yeast YPT1 and SEC4 products involved in secretion.";
J. Biol. Chem. 264:12394-12401(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=16935861; DOI=10.1074/jbc.M606301200;
Nagy G., Ward J., Mosser D.D., Koncz A., Gergely P. Jr., Stancato C.,
Qian Y., Fernandez D., Niland B., Grossman C.E., Telarico T.,
Banki K., Perl A.;
"Regulation of CD4 expression via recycling by HRES-1/RAB4 controls
susceptibility to HIV infection.";
J. Biol. Chem. 281:34574-34591(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Caudate nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PHOSPHORYLATION BY CDK1.
PubMed=1902553; DOI=10.1038/350715a0;
Bailly E., McCaffrey M., Touchot N., Zahraoui A., Goud B., Bornens M.;
"Phosphorylation of two small GTP-binding proteins of the Rab family
by p34cdc2.";
Nature 350:715-718(1991).
[9]
PHOSPHORYLATION AT SER-204 BY CDK1, AND SUBCELLULAR LOCATION.
PubMed=1425574;
van der Sluijs P., Hull M., Huber L.A., Male P., Goud B., Mellman I.;
"Reversible phosphorylation-dephosphorylation determines the
localization of rab4 during the cell cycle.";
EMBO J. 11:4379-4389(1992).
[10]
INTERACTION WITH RABEP1.
PubMed=10698684; DOI=10.1042/bj3460593;
Nagelkerken B., van Anken E., van Raak M., Gerez L., Mohrmann K.,
van Uden N., Holthuizen J., Pelkmans L., van der Sluijs P.;
"Rabaptin4, a novel effector of the small GTPase rab4a, is recruited
to perinuclear recycling vesicles.";
Biochem. J. 346:593-601(2000).
[11]
INTERACTION WITH RAB11FIP1.
TISSUE=Cervix carcinoma;
PubMed=11786538; DOI=10.1074/jbc.M108665200;
Lindsay A.J., Hendrick A.G., Cantalupo G., Senic-Matuglia F., Goud B.,
Bucci C., McCaffrey M.W.;
"Rab coupling protein (RCP), a novel Rab4 and Rab11 effector
protein.";
J. Biol. Chem. 277:12190-12199(2002).
[12]
INTERACTION WITH ZFYVE20.
PubMed=11788822; DOI=10.1038/ncb744;
de Renzis S., Soennichsen B., Zerial M.;
"Divalent Rab effectors regulate the sub-compartmental organization
and sorting of early endosomes.";
Nat. Cell Biol. 4:124-133(2002).
[13]
INTERACTION WITH RAB11FIP1.
PubMed=15280022; DOI=10.1016/j.febslet.2004.06.068;
Lindsay A.J., McCaffrey M.W.;
"Characterisation of the Rab binding properties of Rab coupling
protein (RCP) by site-directed mutagenesis.";
FEBS Lett. 571:86-92(2004).
[14]
INTERACTION WITH RUFY1.
PubMed=14617813; DOI=10.1091/mbc.E03-05-0343;
Fouraux M.A., Deneka M., Ivan V., van der Heijden A., Raymackers J.,
van Suylekom D., van Venrooij W.J., van der Sluijs P., Pruijn G.J.M.;
"Rabip4' is an effector of rab5 and rab4 and regulates transport
through early endosomes.";
Mol. Biol. Cell 15:611-624(2004).
[15]
INTERACTION WITH NDRG1.
PubMed=17786215; DOI=10.1371/journal.pone.0000844;
Kachhap S.K., Faith D., Qian D.Z., Shabbeer S., Galloway N.L.,
Pili R., Denmeade S.R., DeMarzo A.M., Carducci M.A.;
"The N-Myc down regulated Gene1 (NDRG1) is a Rab4a effector involved
in vesicular recycling of E-cadherin.";
PLoS ONE 2:E844-E844(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
INTERACTION WITH GRIPAP1; RABEP1 AND RBSN.
PubMed=20098723; DOI=10.1371/journal.pbio.1000283;
Hoogenraad C.C., Popa I., Futai K., Martinez-Sanchez E.,
Sanchez-Martinez E., Wulf P.S., van Vlijmen T., Dortland B.R.,
Oorschot V., Govers R., Monti M., Heck A.J., Sheng M., Klumperman J.,
Rehmann H., Jaarsma D., Kapitein L.C., van der Sluijs P.;
"Neuron specific Rab4 effector GRASP-1 coordinates membrane
specialization and maturation of recycling endosomes.";
PLoS Biol. 8:E1000283-E1000283(2010).
[19]
X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 6-189 IN COMPLEX WITH GTP
ANALOG AND GDP.
PubMed=15907487; DOI=10.1016/j.febslet.2005.04.020;
Huber S.K., Scheidig A.J.;
"High resolution crystal structures of human Rab4a in its active and
inactive conformations.";
FEBS Lett. 579:2821-2829(2005).
[20]
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 7-177 IN COMPLEX WITH GTP,
INTERACTION WITH ZFYVE20, AND MUTAGENESIS OF GLY-51.
PubMed=16034420; DOI=10.1038/nature03798;
Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
"Structural basis of family-wide Rab GTPase recognition by rabenosyn-
5.";
Nature 436:415-419(2005).
-!- FUNCTION: Protein transport. Probably involved in vesicular
traffic (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with SGSM1, SGSM2 and SGSM3 (By similarity).
Interacts with RAB11FIP1, RABEP1, ZFYVE20 and RUFY1
(PubMed:10698684, PubMed:11786538, PubMed:11788822,
PubMed:14617813, PubMed:15280022, PubMed:16034420). Interacts
(membrane-bound form) with NDRG1; the interaction involves NDRG1
in vesicular recycling of E-cadherin (PubMed:17786215). Interacts
(in GTP-bound form) with GRIPAP1 (via N-terminus)
(PubMed:20098723). Interacts with RABEP1 and RBSN
(PubMed:20098723). Does not interact with HPS4 (By similarity).
{ECO:0000250|UniProtKB:P56371, ECO:0000269|PubMed:10698684,
ECO:0000269|PubMed:11786538, ECO:0000269|PubMed:11788822,
ECO:0000269|PubMed:14617813, ECO:0000269|PubMed:15280022,
ECO:0000269|PubMed:15907487, ECO:0000269|PubMed:16034420,
ECO:0000269|PubMed:17786215, ECO:0000269|PubMed:20098723}.
-!- INTERACTION:
O00471:EXOC5; NbExp=5; IntAct=EBI-722284, EBI-949824;
P31150:GDI1; NbExp=3; IntAct=EBI-722284, EBI-946999;
P50395:GDI2; NbExp=2; IntAct=EBI-722284, EBI-1049143;
Q4V328:GRIPAP1; NbExp=3; IntAct=EBI-722284, EBI-717919;
Q8N1B4:VPS52; NbExp=3; IntAct=EBI-722284, EBI-2799833;
-!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein
{ECO:0000269|PubMed:1425574}. Cytoplasm
{ECO:0000269|PubMed:1425574}. Early endosome membrane
{ECO:0000250|UniProtKB:P05714}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P05714}. Recycling endosome membrane
{ECO:0000250|UniProtKB:P05714}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P05714}. Note=Generally associated with
membranes. Cytoplasmic when phosphorylated by CDK1.
{ECO:0000269|PubMed:1425574}.
-!- PTM: Phosphorylated by CDK1 kinase during mitosis.
{ECO:0000269|PubMed:1425574, ECO:0000269|PubMed:1902553}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA60244.1; Type=Frameshift; Positions=6; Evidence={ECO:0000305};
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EMBL; M28211; AAA60244.1; ALT_FRAME; mRNA.
EMBL; AY585832; AAT91347.1; -; mRNA.
EMBL; AF498934; AAM21082.1; -; mRNA.
EMBL; AK313807; BAG36543.1; -; mRNA.
EMBL; AL162595; CAI19037.1; -; Genomic_DNA.
EMBL; AL117350; CAI19037.1; JOINED; Genomic_DNA.
EMBL; AL117350; CAI22870.1; -; Genomic_DNA.
EMBL; AL162595; CAI22870.1; JOINED; Genomic_DNA.
EMBL; CH471098; EAW69890.1; -; Genomic_DNA.
EMBL; BC002438; AAH02438.1; -; mRNA.
EMBL; BC004309; AAH04309.1; -; mRNA.
CCDS; CCDS31050.1; -.
PIR; E34323; E34323.
RefSeq; NP_001258927.1; NM_001271998.1.
RefSeq; NP_004569.2; NM_004578.3.
UniGene; Hs.296169; -.
PDB; 1YU9; X-ray; 2.07 A; A=7-177.
PDB; 1Z0K; X-ray; 1.92 A; A/C=7-177.
PDB; 2BMD; X-ray; 1.80 A; A=6-189.
PDB; 2BME; X-ray; 1.57 A; A/B/C/D=6-189.
PDBsum; 1YU9; -.
PDBsum; 1Z0K; -.
PDBsum; 2BMD; -.
PDBsum; 2BME; -.
ProteinModelPortal; P20338; -.
SMR; P20338; -.
BioGrid; 111805; 43.
DIP; DIP-372N; -.
IntAct; P20338; 21.
MINT; MINT-1376149; -.
STRING; 9606.ENSP00000355651; -.
iPTMnet; P20338; -.
PhosphoSitePlus; P20338; -.
DMDM; 460018296; -.
EPD; P20338; -.
MaxQB; P20338; -.
PaxDb; P20338; -.
PeptideAtlas; P20338; -.
PRIDE; P20338; -.
DNASU; 5867; -.
Ensembl; ENST00000366690; ENSP00000355651; ENSG00000168118.
GeneID; 5867; -.
KEGG; hsa:5867; -.
UCSC; uc001hth.5; human.
CTD; 5867; -.
DisGeNET; 5867; -.
EuPathDB; HostDB:ENSG00000168118.11; -.
GeneCards; RAB4A; -.
HGNC; HGNC:9781; RAB4A.
MIM; 179511; gene.
neXtProt; NX_P20338; -.
OpenTargets; ENSG00000168118; -.
PharmGKB; PA34141; -.
eggNOG; KOG0086; Eukaryota.
eggNOG; ENOG410XQ9X; LUCA.
GeneTree; ENSGT00760000118841; -.
HOVERGEN; HBG009351; -.
InParanoid; P20338; -.
KO; K07879; -.
OMA; QNICILL; -.
OrthoDB; EOG091G0QOB; -.
PhylomeDB; P20338; -.
TreeFam; TF300032; -.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-HSA-8854214; TBC/RABGAPs.
Reactome; R-HSA-8873719; RAB geranylgeranylation.
Reactome; R-HSA-8875656; MET receptor recycling.
SignaLink; P20338; -.
SIGNOR; P20338; -.
ChiTaRS; RAB4A; human.
EvolutionaryTrace; P20338; -.
GeneWiki; RAB4A; -.
GenomeRNAi; 5867; -.
PRO; PR:P20338; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000168118; -.
CleanEx; HS_RAB4A; -.
ExpressionAtlas; P20338; baseline and differential.
Genevisible; P20338; HS.
GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
GO; GO:0005768; C:endosome; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0032593; C:insulin-responsive compartment; IBA:GO_Central.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0098837; C:postsynaptic recycling endosome; IEA:Ensembl.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0001671; F:ATPase activator activity; IEA:Ensembl.
GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IEA:Ensembl.
GO; GO:0008565; F:protein transporter activity; IEA:Ensembl.
GO; GO:0019905; F:syntaxin binding; IEA:Ensembl.
GO; GO:0019882; P:antigen processing and presentation; IMP:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0032482; P:Rab protein signal transduction; IEA:Ensembl.
GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51419; RAB; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Endosome; GTP-binding;
Lipoprotein; Membrane; Methylation; Nucleotide-binding;
Phosphoprotein; Prenylation; Protein transport; Reference proteome;
Transport.
CHAIN 1 218 Ras-related protein Rab-4A.
/FTId=PRO_0000121093.
NP_BIND 20 28 GTP. {ECO:0000269|PubMed:16034420}.
NP_BIND 68 72 GTP. {ECO:0000269|PubMed:16034420}.
NP_BIND 126 129 GTP. {ECO:0000269|PubMed:16034420}.
NP_BIND 156 158 GTP. {ECO:0000269|PubMed:16034420}.
MOTIF 42 50 Effector region. {ECO:0000250}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 204 204 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:1425574}.
MOD_RES 218 218 Cysteine methyl ester. {ECO:0000250}.
LIPID 216 216 S-geranylgeranyl cysteine. {ECO:0000250}.
LIPID 218 218 S-geranylgeranyl cysteine. {ECO:0000250}.
MUTAGEN 51 51 G->A: 10-fold decrease in ZFYVE20 binding
affinity. {ECO:0000269|PubMed:16034420}.
MUTAGEN 51 51 G->L: 10-fold decrease in ZFYVE20 binding
affinity. {ECO:0000269|PubMed:16034420}.
CONFLICT 162 162 N -> D (in Ref. 1; AAA60244).
{ECO:0000305}.
CONFLICT 208 208 A -> T (in Ref. 1; AAA60244).
{ECO:0000305}.
STRAND 11 21 {ECO:0000244|PDB:2BME}.
HELIX 26 35 {ECO:0000244|PDB:2BME}.
STRAND 46 57 {ECO:0000244|PDB:2BME}.
STRAND 60 69 {ECO:0000244|PDB:2BME}.
HELIX 73 75 {ECO:0000244|PDB:2BME}.
HELIX 76 80 {ECO:0000244|PDB:2BME}.
STRAND 87 94 {ECO:0000244|PDB:2BME}.
HELIX 98 102 {ECO:0000244|PDB:2BME}.
HELIX 104 114 {ECO:0000244|PDB:2BME}.
STRAND 120 126 {ECO:0000244|PDB:2BME}.
HELIX 128 133 {ECO:0000244|PDB:2BME}.
HELIX 138 147 {ECO:0000244|PDB:2BME}.
STRAND 151 154 {ECO:0000244|PDB:2BME}.
TURN 157 159 {ECO:0000244|PDB:2BME}.
HELIX 163 179 {ECO:0000244|PDB:2BME}.
SEQUENCE 218 AA; 24390 MW; 983D65E1162741B0 CRC64;
MSQTAMSETY DFLFKFLVIG NAGTGKSCLL HQFIEKKFKD DSNHTIGVEF GSKIINVGGK
YVKLQIWDTA GQERFRSVTR SYYRGAAGAL LVYDITSRET YNALTNWLTD ARMLASQNIV
IILCGNKKDL DADREVTFLE ASRFAQENEL MFLETSALTG ENVEEAFVQC ARKILNKIES
GELDPERMGS GIQYGDAALR QLRSPRRAQA PNAQECGC


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