PHLB1_HUMAN
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 03-AUG-2022, entry version 152.
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; 28.
DR IntAct; Q86UU1; 16.
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; Q86UU1; -.
DR PeptideAtlas; Q86UU1; -.
DR PRIDE; Q86UU1; -.
DR ProteomicsDB; 69894; -. [Q86UU1-1]
DR ProteomicsDB; 69895; -. [Q86UU1-2]
DR ProteomicsDB; 69896; -. [Q86UU1-3]
DR Antibodypedia; 45815; 72 antibodies from 14 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 CTD; 23187; -.
DR DisGeNET; 23187; -.
DR GeneCards; PHLDB1; -.
DR HGNC; HGNC:23697; PHLDB1.
DR HPA; ENSG00000019144; Tissue enhanced (brain).
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; QEYVTLE; -.
DR OrthoDB; 70229at2759; -.
DR PhylomeDB; Q86UU1; -.
DR TreeFam; TF329165; -.
DR PathwayCommons; Q86UU1; -.
DR SignaLink; Q86UU1; -.
DR BioGRID-ORCS; 23187; 16 hits in 1082 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 203 other tissues.
DR ExpressionAtlas; Q86UU1; baseline and differential.
DR Genevisible; Q86UU1; HS.
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; cd00060; FHA; 1.
DR CDD; cd14673; PH_PHLDB1_2; 1.
DR Gene3D; 2.30.29.30; -; 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 Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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
