ARFG2_HUMAN
ID ARFG2_HUMAN Reviewed; 521 AA.
AC Q8N6H7; B4DX29; B7Z9M7; D3DQQ9; Q3LIF2; Q8N3I1; Q96SX7;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 2;
DE Short=ARF GAP 2;
DE AltName: Full=GTPase-activating protein ZNF289;
DE AltName: Full=Zinc finger protein 289;
GN Name=ARFGAP2; Synonyms=ZNF289; ORFNames=Nbla10535;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Teratocarcinoma, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-521 (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-521 (ISOFORM 1), AND VARIANT
RP ASN-411.
RC TISSUE=Neuroblastoma;
RX PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of the
RT genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
RN [7]
RP INTERACTION WITH COPG1.
RX PubMed=14690497; DOI=10.1111/j.1600-0854.2004.00158.x;
RA Watson P.J., Frigerio G., Collins B.M., Duden R., Owen D.J.;
RT "Gamma-COP appendage domain -- structure and function.";
RL Traffic 5:79-88(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH COATOMER.
RX PubMed=17760859; DOI=10.1111/j.1600-0854.2007.00631.x;
RA Frigerio G., Grimsey N., Dale M., Majoul I., Duden R.;
RT "Two human ARFGAPs associated with COP-I-coated vesicles.";
RL Traffic 8:1644-1655(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-368 AND SER-432, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 AND SER-368, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-368 AND SER-432, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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., Buerckstuemmer 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-432 AND SER-433, AND
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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-237; SER-240;
RP SER-312; SER-340; SER-364; SER-368; SER-432 AND SER-513, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-146; SER-201;
RP SER-334 AND SER-368, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-130.
RG Structural genomics consortium (SGC);
RT "Gap domain of ZNF289, an ID1-regulated zinc finger protein.";
RL Submitted (MAR-2007) to the PDB data bank.
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 1
CC (ARF1). Implicated in coatomer-mediated protein transport between the
CC Golgi complex and the endoplasmic reticulum. Hydrolysis of ARF1-bound
CC GTP may lead to dissociation of coatomer from Golgi-derived membranes
CC to allow fusion with target membranes. {ECO:0000269|PubMed:17760859}.
CC -!- SUBUNIT: Interacts with the coatomer complex. Interacts with the C-
CC terminal appendage domain of COPG1. {ECO:0000269|PubMed:14690497,
CC ECO:0000269|PubMed:17760859}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17760859}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:17760859}; Peripheral membrane
CC protein {ECO:0000269|PubMed:17760859}; Cytoplasmic side
CC {ECO:0000269|PubMed:17760859}. Note=Also found on peripheral punctate
CC structures likely to be endoplasmic reticulum-Golgi intermediate
CC compartment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N6H7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N6H7-2; Sequence=VSP_056055, VSP_056056;
CC Name=3;
CC IsoId=Q8N6H7-3; Sequence=VSP_056054;
CC -!- MISCELLANEOUS: Vero cells overexpressing truncated ARFGAP2 show
CC accumulation of cholera toxin A subunit in the Golgi complex rather
CC than the endoplasmic reticulum.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK027482; BAB55144.1; -; mRNA.
DR EMBL; AK301785; BAG63241.1; -; mRNA.
DR EMBL; AK315992; BAH14363.1; -; mRNA.
DR EMBL; AC090589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW67963.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW67968.1; -; Genomic_DNA.
DR EMBL; BC030148; AAH30148.1; -; mRNA.
DR EMBL; AL834337; CAD39004.1; -; mRNA.
DR EMBL; AB073358; BAE45716.1; -; mRNA.
DR CCDS; CCDS7926.1; -. [Q8N6H7-1]
DR RefSeq; NP_001229761.1; NM_001242832.1.
DR RefSeq; NP_115765.2; NM_032389.4. [Q8N6H7-1]
DR PDB; 2P57; X-ray; 1.80 A; A=3-130.
DR PDBsum; 2P57; -.
DR AlphaFoldDB; Q8N6H7; -.
DR SMR; Q8N6H7; -.
DR BioGRID; 124065; 157.
DR IntAct; Q8N6H7; 16.
DR MINT; Q8N6H7; -.
DR STRING; 9606.ENSP00000434442; -.
DR iPTMnet; Q8N6H7; -.
DR MetOSite; Q8N6H7; -.
DR PhosphoSitePlus; Q8N6H7; -.
DR BioMuta; ARFGAP2; -.
DR DMDM; 74729129; -.
DR EPD; Q8N6H7; -.
DR jPOST; Q8N6H7; -.
DR MassIVE; Q8N6H7; -.
DR MaxQB; Q8N6H7; -.
DR PaxDb; Q8N6H7; -.
DR PeptideAtlas; Q8N6H7; -.
DR PRIDE; Q8N6H7; -.
DR ProteomicsDB; 5401; -.
DR ProteomicsDB; 72177; -. [Q8N6H7-1]
DR Antibodypedia; 13559; 186 antibodies from 27 providers.
DR DNASU; 84364; -.
DR Ensembl; ENST00000524782.6; ENSP00000434442.1; ENSG00000149182.15. [Q8N6H7-1]
DR GeneID; 84364; -.
DR KEGG; hsa:84364; -.
DR MANE-Select; ENST00000524782.6; ENSP00000434442.1; NM_032389.6; NP_115765.2.
DR UCSC; uc001ndt.4; human. [Q8N6H7-1]
DR CTD; 84364; -.
DR DisGeNET; 84364; -.
DR GeneCards; ARFGAP2; -.
DR HGNC; HGNC:13504; ARFGAP2.
DR HPA; ENSG00000149182; Low tissue specificity.
DR MIM; 606908; gene.
DR neXtProt; NX_Q8N6H7; -.
DR OpenTargets; ENSG00000149182; -.
DR PharmGKB; PA162376868; -.
DR VEuPathDB; HostDB:ENSG00000149182; -.
DR eggNOG; KOG0706; Eukaryota.
DR GeneTree; ENSGT00940000155568; -.
DR InParanoid; Q8N6H7; -.
DR OMA; QNVGESI; -.
DR OrthoDB; 1155557at2759; -.
DR PhylomeDB; Q8N6H7; -.
DR TreeFam; TF313985; -.
DR PathwayCommons; Q8N6H7; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR SignaLink; Q8N6H7; -.
DR BioGRID-ORCS; 84364; 16 hits in 1086 CRISPR screens.
DR ChiTaRS; ARFGAP2; human.
DR EvolutionaryTrace; Q8N6H7; -.
DR GenomeRNAi; 84364; -.
DR Pharos; Q8N6H7; Tbio.
DR PRO; PR:Q8N6H7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8N6H7; protein.
DR Bgee; ENSG00000149182; Expressed in skin of leg and 197 other tissues.
DR ExpressionAtlas; Q8N6H7; baseline and differential.
DR Genevisible; Q8N6H7; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.220.150; -; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW ER-Golgi transport; Golgi apparatus; GTPase activation; Membrane;
KW Metal-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Transport; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..521
FT /note="ADP-ribosylation factor GTPase-activating protein 2"
FT /id="PRO_0000278468"
FT DOMAIN 11..127
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 26..49
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 97..521
FT /note="Required for interaction with coatomer"
FT REGION 143..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 242..308
FT /evidence="ECO:0000255"
FT COMPBIAS 169..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..269
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056054"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056055"
FT VAR_SEQ 133..160
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056056"
FT VARIANT 143
FT /note="P -> R (in dbSNP:rs11542793)"
FT /id="VAR_048321"
FT VARIANT 339
FT /note="R -> H (in dbSNP:rs34662994)"
FT /id="VAR_048322"
FT VARIANT 406
FT /note="R -> W (in dbSNP:rs35950498)"
FT /id="VAR_048323"
FT VARIANT 411
FT /note="S -> N (in dbSNP:rs3740691)"
FT /evidence="ECO:0000269|PubMed:12880961"
FT /id="VAR_030780"
FT CONFLICT 40
FT /note="T -> M (in Ref. 1; BAB55144)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="N -> S (in Ref. 1; BAB55144)"
FT /evidence="ECO:0000305"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:2P57"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:2P57"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2P57"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2P57"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:2P57"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2P57"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:2P57"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:2P57"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2P57"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:2P57"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:2P57"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:2P57"
FT HELIX 109..124
FT /evidence="ECO:0007829|PDB:2P57"
SQ SEQUENCE 521 AA; 56720 MW; 16655EBA94D29E81 CRC64;
MAAEPNKTEI QTLFKRLRAV PTNKACFDCG AKNPSWASIT YGVFLCIDCS GVHRSLGVHL
SFIRSTELDS NWNWFQLRCM QVGGNANATA FFRQHGCTAN DANTKYNSRA AQMYREKIRQ
LGSAALARHG TDLWIDNMSS AVPNHSPEKK DSDFFTEHTQ PPAWDAPATE PSGTQQPAPS
TESSGLAQPE HGPNTDLLGT SPKASLELKS SIIGKKKPAA AKKGLGAKKG LGAQKVSSQS
FSEIERQAQV AEKLREQQAA DAKKQAEESM VASMRLAYQE LQIDRKKEEK KLQNLEGKKR
EQAERLGMGL VSRSSVSHSV LSEMQVIEQE TPVSAKSSRS QLDLFDDVGT FASGPPKYKD
NPFSLGESFG SRWDTDAAWG MDRVEEKEPE VTISSIRPIS ERATNRREVE SRSSGLESSE
ARQKFAGAKA ISSDMFFGRE VDAEYEARSR LQQLSGSSAI SSSDLFGDMD GAHGAGSVSL
GNVLPTADIA QFKQGVKSVA GKMAVLANGV MNSLQDRYGS Y
