ID   PHLB1_HUMAN             Reviewed;        1377 AA.
AC   Q86UU1; B0YJ63; B0YJ64; O75133; Q4KMF8; Q8TEQ2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Pleckstrin homology-like domain family B member 1;
DE   AltName: Full=Protein LL5-alpha;
GN   Name=PHLDB1; Synonyms=KIAA0638, LL5A; ORFNames=DLNB07;
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] (ISOFORM 1).
RA   Kubo T., Arai Y., Ohira M., Gamou T., Maeno G., Sakiyama T., Toyoda A.,
RA   Hattori M., Sakaki Y., Nakagawara A., Ohki M.;
RT   "Identification of a 500-kb region of common allelic loss in chromosome
RT   11q23 in non-MYCN amplified type of neuroblastoma.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA   Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA   Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. X. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:169-176(1998).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Spleen;
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Placenta;
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   [9]
RP   BINDING TO PHOSPHOINOSITIDES.
RX   PubMed=11001876; DOI=10.1042/0264-6021:3510019;
RA   Dowler S.J., Currie R.A., Campbell D.G., Deak M., Kular G., Downes C.P.,
RA   Alessi D.R.;
RT   "Identification of pleckstrin-homology-domain-containing proteins with
RT   novel phosphoinositide-binding specificities.";
RL   Biochem. J. 351:19-31(2000).
RN   [10]
RP   ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
RX   PubMed=14532993;
RA   Katoh M., Katoh M.;
RT   "Identification and characterization of human LL5A gene and mouse Ll5a gene
RT   in silico.";
RL   Int. J. Oncol. 23:1477-1483(2003).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, 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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-223; SER-430;
RP   SER-443; SER-501; SER-520; SER-551; SER-555 AND SER-583, AND IDENTIFICATION
RP   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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND IDENTIFICATION BY
RP   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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520 AND THR-522, 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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-220; SER-324;
RP   SER-334; SER-404; SER-430; SER-443; SER-461; SER-489; SER-501; SER-518;
RP   SER-520; SER-563; SER-578; SER-583; SER-678 AND SER-971, 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-324, AND IDENTIFICATION BY
RP   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   -!- INTERACTION:
CC       Q86UU1; P51114: FXR1; NbExp=2; IntAct=EBI-4289858, EBI-713291;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q86UU1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86UU1-2; Sequence=VSP_016737, VSP_016740;
CC       Name=3;
CC         IsoId=Q86UU1-3; Sequence=VSP_016737, VSP_016738, VSP_016739;
CC   -!- DOMAIN: The PH domain mediates the binding to phosphoinositides.
CC   -!- MISCELLANEOUS: [Isoform 1]: Minor.
CC   -!- MISCELLANEOUS: [Isoform 2]: Major. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA31613.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB84896.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB094090; BAC76044.1; -; mRNA.
DR   EMBL; AB014538; BAA31613.2; ALT_INIT; mRNA.
DR   EMBL; AK074070; BAB84896.2; ALT_INIT; mRNA.
DR   EMBL; EF445008; ACA06043.1; -; Genomic_DNA.
DR   EMBL; EF445008; ACA06041.1; -; Genomic_DNA.
DR   EMBL; AP000941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP002954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471065; EAW67401.1; -; Genomic_DNA.
DR   EMBL; BC098586; AAH98586.1; -; mRNA.
DR   CCDS; CCDS44750.1; -. [Q86UU1-2]
DR   CCDS; CCDS8401.1; -. [Q86UU1-1]
DR   RefSeq; NP_001138230.1; NM_001144758.2. [Q86UU1-1]
DR   RefSeq; NP_001138231.1; NM_001144759.2. [Q86UU1-2]
DR   RefSeq; NP_055972.1; NM_015157.3. [Q86UU1-1]
DR   AlphaFoldDB; Q86UU1; -.
DR   SMR; Q86UU1; -.
DR   BioGRID; 116797; 40.
DR   IntAct; Q86UU1; 25.
DR   MINT; Q86UU1; -.
DR   STRING; 9606.ENSP00000354498; -.
DR   GlyGen; Q86UU1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q86UU1; -.
DR   PhosphoSitePlus; Q86UU1; -.
DR   BioMuta; PHLDB1; -.
DR   DMDM; 74723506; -.
DR   EPD; Q86UU1; -.
DR   jPOST; Q86UU1; -.
DR   MassIVE; Q86UU1; -.
DR   MaxQB; Q86UU1; -.
DR   PaxDb; 9606-ENSP00000354498; -.
DR   PeptideAtlas; Q86UU1; -.
DR   ProteomicsDB; 69894; -. [Q86UU1-1]
DR   ProteomicsDB; 69895; -. [Q86UU1-2]
DR   ProteomicsDB; 69896; -. [Q86UU1-3]
DR   Pumba; Q86UU1; -.
DR   Antibodypedia; 45815; 76 antibodies from 15 providers.
DR   DNASU; 23187; -.
DR   Ensembl; ENST00000356063.9; ENSP00000348359.5; ENSG00000019144.20. [Q86UU1-2]
DR   Ensembl; ENST00000361417.6; ENSP00000354498.2; ENSG00000019144.20. [Q86UU1-1]
DR   Ensembl; ENST00000528594.5; ENSP00000435520.1; ENSG00000019144.20. [Q86UU1-3]
DR   Ensembl; ENST00000530994.5; ENSP00000431508.1; ENSG00000019144.20. [Q86UU1-3]
DR   Ensembl; ENST00000600882.6; ENSP00000469820.1; ENSG00000019144.20. [Q86UU1-1]
DR   GeneID; 23187; -.
DR   KEGG; hsa:23187; -.
DR   MANE-Select; ENST00000600882.6; ENSP00000469820.1; NM_001144758.3; NP_001138230.1.
DR   UCSC; uc001ptr.3; human. [Q86UU1-1]
DR   AGR; HGNC:23697; -.
DR   CTD; 23187; -.
DR   DisGeNET; 23187; -.
DR   GeneCards; PHLDB1; -.
DR   HGNC; HGNC:23697; PHLDB1.
DR   HPA; ENSG00000019144; Low tissue specificity.
DR   MIM; 612834; gene.
DR   neXtProt; NX_Q86UU1; -.
DR   OpenTargets; ENSG00000019144; -.
DR   PharmGKB; PA134917952; -.
DR   VEuPathDB; HostDB:ENSG00000019144; -.
DR   eggNOG; ENOG502QPZY; Eukaryota.
DR   GeneTree; ENSGT00940000155231; -.
DR   HOGENOM; CLU_003180_0_0_1; -.
DR   InParanoid; Q86UU1; -.
DR   OMA; DKKSPFQ; -.
DR   OrthoDB; 5477608at2759; -.
DR   PhylomeDB; Q86UU1; -.
DR   TreeFam; TF329165; -.
DR   PathwayCommons; Q86UU1; -.
DR   SignaLink; Q86UU1; -.
DR   BioGRID-ORCS; 23187; 16 hits in 1160 CRISPR screens.
DR   ChiTaRS; PHLDB1; human.
DR   GeneWiki; PHLDB1; -.
DR   GenomeRNAi; 23187; -.
DR   Pharos; Q86UU1; Tbio.
DR   PRO; PR:Q86UU1; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q86UU1; Protein.
DR   Bgee; ENSG00000019144; Expressed in sural nerve and 205 other cell types or tissues.
DR   ExpressionAtlas; Q86UU1; baseline and differential.
DR   GO; GO:0045180; C:basal cortex; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; IMP:UniProtKB.
DR   GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR   GO; GO:0010470; P:regulation of gastrulation; IMP:UniProtKB.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IGI:UniProtKB.
DR   CDD; cd22713; FHA_PHLB1; 1.
DR   CDD; cd14673; PH_PHLDB1_2; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR037810; PHLDB1/2/3_PH.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR12156:SF23; PLECKSTRIN HOMOLOGY-LIKE DOMAIN FAMILY B MEMBER 1; 1.
DR   PANTHER; PTHR12156; PLECKSTRIN HOMOLOGY-LIKE DOMAIN, FAMILY B, MEMBER 3; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   Genevisible; Q86UU1; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Methylation; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1377
FT                   /note="Pleckstrin homology-like domain family B member 1"
FT                   /id="PRO_0000053891"
FT   DOMAIN          64..125
FT                   /note="FHA"
FT   DOMAIN          1256..1370
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          150..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          936..1019
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1119..1138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          683..809
FT                   /evidence="ECO:0000255"
FT   COILED          1144..1208
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        163..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..707
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        976..1019
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PDH0"
FT   MOD_RES         131
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PDH0"
FT   MOD_RES         192
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         220
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         334
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         381
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PDH0"
FT   MOD_RES         404
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         430
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         461
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         470
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PDH0"
FT   MOD_RES         489
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         501
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         512
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PDH0"
FT   MOD_RES         518
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         520
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         522
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         533
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PDH0"
FT   MOD_RES         539
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PDH0"
FT   MOD_RES         551
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         555
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         563
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         578
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         583
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         678
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         971
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1017
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PDH0"
FT   VAR_SEQ         913..959
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016737"
FT   VAR_SEQ         1042
FT                   /note="Q -> E (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016738"
FT   VAR_SEQ         1043..1377
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016739"
FT   VAR_SEQ         1321..1331
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_016740"
SQ   SEQUENCE   1377 AA;  151162 MW;  DA2829CC9C2ECD3D CRC64;
     MDALNRNQIG PGCQTQTMVQ KGPLDLIETG KGLKVQTDKP HLVSLGSGRL STAITLLPLE
     EGRTVIGSAA RDISLQGPGL APEHCYIENL RGTLTLYPCG NACTIDGLPV RQPTRLTQGC
     MLCLGQSTFL RFNHPAEAKW MKSMIPAGGR APGPPYSPVP AESESLVNGN HTPQTATRGP
     SACASHSSLV SSIEKDLQEI MDSLVLEEPG AAGKKPAATS PLSPMANGGR YLLSPPTSPG
     AMSVGSSYEN TSPAFSPLSS PASSGSCASH SPSGQEPGPS VPPLVPARSS SYHLALQPPQ
     SRPSGARSES PRLSRKGGHE RPPSPGLRGL LTDSPAATVL AEARRATESP RLGGQLPVVA
     ISLSEYPASG ALSQPTSIPG SPKFQPPVPA PRNKIGTLQD RPPSPFREPP GSERVLTTSP
     SRQLVGRTFS DGLATRTLQP PESPRLGRRG LDSMRELPPL SPSLSRRALS PLPTRTTPDP
     KLNREVAESP RPRRWAAHGA SPEDFSLTLG ARGRRTRSPS PTLGESLAPH KGSFSGRLSP
     AYSLGSLTGA SPCQSPCVQR KLSSGDLRVP VTRERKNSIT EISDNEDDLL EYHRRQRQER
     LREQEMERLE RQRLETILNL CAEYSRADGG PEAGELPSIG EATAALALAG RRPSRGLAGA
     SGRSSEEPGV ATQRLWESME RSDEENLKEE CSSTESTQQE HEDAPSTKLQ GEVLALEEER
     AQVLGHVEQL KVRVKELEQQ LQESAREAEM ERALLQGERE AERALLQKEQ KAVDQLQEKL
     VALETGIQKE RDKEAEALET ETKLFEDLEF QQLERESRVE EERELAGQGL LRSKAELLRS
     IAKRKERLAI LDSQAGQIRA QAVQESERLA RDKNASLQLL QKEKEKLTVL ERRYHSLTGG
     RPFPKTTSTL KEMEKLLLPA VDLEQWYQEL MAGLGTGPAA ASPHSSPPPL PAKASRQLQV
     YRSKMDGEAT SPLPRTRSGP LPSSSGSSSS SSQLSVATLG RSPSPKSALL TQNGTGSLPR
     NLAATLQDIE TKRQLALQQK GQQVIEEQRR RLAELKQKAA AEAQCQWDAL HGAAPFPAGP
     SGFPPLMHHS ILHHLPAGRE RGEEGEHAYD TLSLESSDSM ETSISTGGNS ACSPDNMSSA
     SGLDMGKIEE MEKMLKEAHA EKNRLMESRE REMELRRQAL EEERRRREQV ERRLQSESAR
     RQQLVEKEVK MREKQFSQAR PLTRYLPIRK EDFDLKTHIE SSGHGVDTCL HVVLSSKVCR
     GYLVKMGGKI KSWKKRWFVF DRLKRTLSYY VDKHETKLKG VIYFQAIEEV YYDHLRSAAK
     KRFFRFTMVT ESPNPALTFC VKTHDRLYYM VAPSAEAMRI WMDVIVTGAE GYTQFMN
//