PACN3_HUMAN
ID PACN3_HUMAN Reviewed; 424 AA.
AC Q9UKS6; A6NH84; Q9H331; Q9NWV9;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Protein kinase C and casein kinase substrate in neurons protein 3;
DE AltName: Full=SH3 domain-containing protein 6511;
GN Name=PACSIN3;
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 [MRNA], AND VARIANT VAL-61.
RC TISSUE=Mammary carcinoma;
RX PubMed=10531379; DOI=10.1074/jbc.274.44.31693;
RA Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.;
RT "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two
RT SH3 domain-containing proteins, endophilin I and SH3PX1.";
RL J. Biol. Chem. 274:31693-31699(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11082044; DOI=10.1242/jcs.113.24.4511;
RA Modregger J., Ritter B., Witter B., Paulsson M., Plomann M.;
RT "All three PACSIN isoforms bind to endocytic proteins and inhibit
RT endocytosis.";
RL J. Cell Sci. 113:4511-4521(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11179684; DOI=10.1016/s0378-1119(00)00531-x;
RA Sumoy L., Pluvinet R., Andreu N., Estivill X., Escarceller M.;
RT "PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the pacsin-
RT syndapin-FAP52 gene family.";
RL Gene 262:199-205(2001).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-405.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; THR-324; SER-327;
RP SER-354 AND SER-383, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-319; SER-354 AND
RP SER-383, AND 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP 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 [14]
RP DOMAIN.
RX PubMed=23236520; DOI=10.1371/journal.pone.0051628;
RA Goh S.L., Wang Q., Byrnes L.J., Sondermann H.;
RT "Versatile membrane deformation potential of activated pacsin.";
RL PLoS ONE 7:E51628-E51628(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-319; SER-354 AND
RP SER-383, AND IDENTIFICATION 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-319 AND SER-354, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Plays a role in endocytosis and regulates internalization of
CC plasma membrane proteins. Overexpression impairs internalization of
CC SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and
CC TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel activity
CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:11082044}.
CC -!- SUBUNIT: Homodimer. May form heterooligomers with other PACSINs.
CC Interacts (via SH3 domain) with DNM1, SYNJ1 and WASL. Interacts with
CC TRPV4 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UKS6; O14672: ADAM10; NbExp=3; IntAct=EBI-77926, EBI-1536151;
CC Q9UKS6; Q13444: ADAM15; NbExp=3; IntAct=EBI-77926, EBI-77818;
CC Q9UKS6; Q13443: ADAM9; NbExp=2; IntAct=EBI-77926, EBI-77903;
CC Q9UKS6; P48023: FASLG; NbExp=4; IntAct=EBI-77926, EBI-495538;
CC Q9UKS6; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-77926, EBI-10176379;
CC Q9UKS6; Q9UHV8: LGALS13; NbExp=3; IntAct=EBI-77926, EBI-3957707;
CC Q9UKS6; Q9BY11: PACSIN1; NbExp=8; IntAct=EBI-77926, EBI-721769;
CC Q9UKS6; Q9UNF0: PACSIN2; NbExp=3; IntAct=EBI-77926, EBI-742503;
CC Q9UKS6; Q9UKS6: PACSIN3; NbExp=3; IntAct=EBI-77926, EBI-77926;
CC Q9UKS6; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-77926, EBI-358489;
CC Q9UKS6; Q07889: SOS1; NbExp=2; IntAct=EBI-77926, EBI-297487;
CC Q9UKS6; Q07890: SOS2; NbExp=2; IntAct=EBI-77926, EBI-298181;
CC Q9UKS6; O43597: SPRY2; NbExp=3; IntAct=EBI-77926, EBI-742487;
CC Q9UKS6; O14787-2: TNPO2; NbExp=3; IntAct=EBI-77926, EBI-12076664;
CC Q9UKS6; O00401: WASL; NbExp=3; IntAct=EBI-77926, EBI-957615;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11179684}. Cell
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Note=Detected at the inner aspect of
CC the plasma membrane in myotubes. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in heart and
CC skeletal muscle, intermediate levels in placenta, liver and pancreas,
CC and very low levels in brain, lung and kidney.
CC {ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:11179684}.
CC -!- DOMAIN: The F-BAR domain forms a coiled coil and mediates membrane-
CC binding and membrane tubulation. {ECO:0000269|PubMed:23236520}.
CC -!- PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C
CC (PKC).
CC -!- SIMILARITY: Belongs to the PACSIN family. {ECO:0000305}.
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DR EMBL; AF130979; AAF04472.1; -; mRNA.
DR EMBL; AF149825; AAG31023.1; -; mRNA.
DR EMBL; AF242530; AAK29207.1; -; mRNA.
DR EMBL; AC090589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007914; AAH07914.1; -; mRNA.
DR EMBL; BC011889; AAH11889.1; -; mRNA.
DR EMBL; AK000577; BAA91267.1; -; mRNA.
DR CCDS; CCDS31481.1; -.
DR RefSeq; NP_001171903.1; NM_001184974.1.
DR RefSeq; NP_001171904.1; NM_001184975.1.
DR RefSeq; NP_057307.2; NM_016223.4.
DR AlphaFoldDB; Q9UKS6; -.
DR SMR; Q9UKS6; -.
DR BioGRID; 118896; 129.
DR IntAct; Q9UKS6; 56.
DR MINT; Q9UKS6; -.
DR STRING; 9606.ENSP00000440945; -.
DR GlyGen; Q9UKS6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UKS6; -.
DR PhosphoSitePlus; Q9UKS6; -.
DR SwissPalm; Q9UKS6; -.
DR BioMuta; PACSIN3; -.
DR DMDM; 22256967; -.
DR EPD; Q9UKS6; -.
DR jPOST; Q9UKS6; -.
DR MassIVE; Q9UKS6; -.
DR MaxQB; Q9UKS6; -.
DR PaxDb; Q9UKS6; -.
DR PeptideAtlas; Q9UKS6; -.
DR PRIDE; Q9UKS6; -.
DR ProteomicsDB; 84843; -.
DR Antibodypedia; 26590; 500 antibodies from 33 providers.
DR DNASU; 29763; -.
DR Ensembl; ENST00000298838.11; ENSP00000298838.6; ENSG00000165912.16.
DR Ensembl; ENST00000539589.5; ENSP00000440945.1; ENSG00000165912.16.
DR GeneID; 29763; -.
DR KEGG; hsa:29763; -.
DR MANE-Select; ENST00000298838.11; ENSP00000298838.6; NM_016223.5; NP_057307.2.
DR UCSC; uc001ndw.4; human.
DR CTD; 29763; -.
DR DisGeNET; 29763; -.
DR GeneCards; PACSIN3; -.
DR HGNC; HGNC:8572; PACSIN3.
DR HPA; ENSG00000165912; Group enriched (heart muscle, skeletal muscle, tongue).
DR MIM; 606513; gene.
DR neXtProt; NX_Q9UKS6; -.
DR OpenTargets; ENSG00000165912; -.
DR PharmGKB; PA32898; -.
DR VEuPathDB; HostDB:ENSG00000165912; -.
DR eggNOG; KOG2856; Eukaryota.
DR GeneTree; ENSGT00950000182973; -.
DR HOGENOM; CLU_030752_2_0_1; -.
DR InParanoid; Q9UKS6; -.
DR OMA; HAKADST; -.
DR OrthoDB; 727724at2759; -.
DR PhylomeDB; Q9UKS6; -.
DR TreeFam; TF313677; -.
DR PathwayCommons; Q9UKS6; -.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q9UKS6; -.
DR BioGRID-ORCS; 29763; 11 hits in 1074 CRISPR screens.
DR ChiTaRS; PACSIN3; human.
DR GeneWiki; PACSIN3; -.
DR GenomeRNAi; 29763; -.
DR Pharos; Q9UKS6; Tbio.
DR PRO; PR:Q9UKS6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9UKS6; protein.
DR Bgee; ENSG00000165912; Expressed in apex of heart and 144 other tissues.
DR ExpressionAtlas; Q9UKS6; baseline and differential.
DR Genevisible; Q9UKS6; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0019855; F:calcium channel inhibitor activity; ISS:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; ISS:UniProtKB.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISS:UniProtKB.
DR GO; GO:0097320; P:plasma membrane tubulation; IDA:UniProtKB.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IMP:BHF-UCL.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR028523; PACSIN3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065:SF18; PTHR23065:SF18; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasm; Endocytosis; Lipid-binding;
KW Membrane; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..424
FT /note="Protein kinase C and casein kinase substrate in
FT neurons protein 3"
FT /id="PRO_0000161800"
FT DOMAIN 10..280
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 363..424
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 155..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..272
FT /evidence="ECO:0000250"
FT COMPBIAS 155..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JB8"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 61
FT /note="A -> V (in dbSNP:rs7106654)"
FT /evidence="ECO:0000269|PubMed:10531379"
FT /id="VAR_053556"
SQ SEQUENCE 424 AA; 48487 MW; 6DBD940AE6D1F352 CRC64;
MAPEEDAGGE ALGGSFWEAG NYRRTVQRVE DGHRLCGDLV SCFQERARIE KAYAQQLADW
ARKWRGTVEK GPQYGTLEKA WHAFFTAAER LSALHLEVRE KLQGQDSERV RAWQRGAFHR
PVLGGFRESR AAEDGFRKAQ KPWLKRLKEV EASKKSYHAA RKDEKTAQTR ESHAKADSAV
SQEQLRKLQE RVERCAKEAE KTKAQYEQTL AELHRYTPRY MEDMEQAFET CQAAERQRLL
FFKDMLLTLH QHLDLSSSEK FHELHRDLHQ GIEAASDEED LRWWRSTHGP GMAMNWPQFE
EWSLDTQRTI SRKEKGGRSP DEVTLTSIVP TRDGTAPPPQ SPGSPGTGQD EEWSDEESPR
KAATGVRVRA LYDYAGQEAD ELSFRAGEEL LKMSEEDEQG WCQGQLQSGR IGLYPANYVE
CVGA
