PAR3L_HUMAN
ID PAR3L_HUMAN Reviewed; 1205 AA.
AC Q8TEW8; E9PE87; Q8IUC7; Q8IUC9; Q96DK9; Q96N09; Q96NX6; Q96NX7; Q96Q29;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Partitioning defective 3 homolog B;
DE AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 19 protein;
DE AltName: Full=PAR3-beta;
DE AltName: Full=Partitioning defective 3-like protein;
DE Short=PAR3-L protein;
GN Name=PARD3B; Synonyms=ALS2CR19, PAR3B, PAR3L;
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 4).
RX PubMed=11586298; DOI=10.1038/ng1001-166;
RA Hadano S., Hand C.K., Osuga H., Yanagisawa Y., Otomo A., Devon R.S.,
RA Miyamoto N., Showguchi-Miyata J., Okada Y., Singaraja R., Figlewicz D.A.,
RA Kwiatkowski T., Hosler B.A., Sagie T., Skaug J., Nasir J., Brown R.H. Jr.,
RA Scherer S.W., Rouleau G.A., Hayden M.R., Ikeda J.-E.;
RT "A gene encoding a putative GTPase regulator is mutated in familial
RT amyotrophic lateral sclerosis 2.";
RL Nat. Genet. 29:166-173(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), AND VARIANT PRO-165.
RX PubMed=12459187; DOI=10.1016/s0006-291x(02)02698-0;
RA Kohjima M., Noda Y., Takeya R., Saito N., Takeuchi K., Sumimoto H.;
RT "PAR3beta, a novel homologue of the cell polarity protein PAR3, localizes
RT to tight junctions.";
RL Biochem. Biophys. Res. Commun. 299:641-646(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), CHARACTERIZATION, AND
RP INTERACTION WITH PARD6B.
RX PubMed=12234671; DOI=10.1016/s0378-1119(02)00681-9;
RA Gao L., Macara I.G., Joberty G.;
RT "Multiple splice variants of Par3 and of a novel related gene, Par3L,
RT produce proteins with different binding properties.";
RL Gene 294:99-107(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-901 (ISOFORM 1), AND VARIANTS
RP PRO-165 AND LYS-192.
RC TISSUE=Gastric mucosa, and Neuron;
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 [6]
RP INTERACTION WITH INSC.
RX PubMed=16458856; DOI=10.1016/j.bbrc.2006.01.050;
RA Izaki T., Kamakura S., Kohjima M., Sumimoto H.;
RT "Two forms of human Inscuteable-related protein that links Par3 to the Pins
RT homologues LGN and AGS3.";
RL Biochem. Biophys. Res. Commun. 341:1001-1006(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746 AND SER-801, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352; SER-368 AND SER-746, AND
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100 AND SER-1184, 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: Putative adapter protein involved in asymmetrical cell
CC division and cell polarization processes. May play a role in the
CC formation of epithelial tight junctions.
CC -!- SUBUNIT: Interacts with PARD6B. Interacts with INSC/inscuteable.
CC {ECO:0000269|PubMed:12234671, ECO:0000269|PubMed:16458856}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system. Cell junction. Cell
CC junction, tight junction. Note=Partially localized along the cell-cell
CC contact region. Colocalizes with TJP1 to epithelial tight junctions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Par3La, a;
CC IsoId=Q8TEW8-1; Sequence=Displayed;
CC Name=2; Synonyms=Par3Lb, b;
CC IsoId=Q8TEW8-2; Sequence=VSP_007478;
CC Name=3; Synonyms=Par3Lc, c;
CC IsoId=Q8TEW8-3; Sequence=VSP_007479;
CC Name=4;
CC IsoId=Q8TEW8-4; Sequence=VSP_007476, VSP_007477;
CC Name=5;
CC IsoId=Q8TEW8-5; Sequence=VSP_007543;
CC Name=6;
CC IsoId=Q8TEW8-6; Sequence=VSP_054048;
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, lung and skeletal
CC muscle. Expressed at intermediate levels in brain, heart, placenta,
CC liver and pancreas. Isoform 1 is predominant, while isoform 2 and
CC isoform 3 are expressed at lower levels.
CC -!- DOMAIN: The N-terminal part (1-351) part blocks the association of the
CC tight junction marker TJP1 with the cell-cell boundary when it is
CC overexpressed.
CC -!- SIMILARITY: Belongs to the PAR3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71106.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB71623.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB053321; BAB69028.1; -; mRNA.
DR EMBL; AB073472; BAC54035.1; -; mRNA.
DR EMBL; AB092439; BAC54285.1; -; mRNA.
DR EMBL; AF428250; AAL30664.1; -; mRNA.
DR EMBL; AF428251; AAL30665.1; -; mRNA.
DR EMBL; AF466152; AAL79827.1; -; mRNA.
DR EMBL; AC007385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK056157; BAB71106.1; ALT_FRAME; mRNA.
DR EMBL; AK057965; BAB71623.1; ALT_INIT; mRNA.
DR CCDS; CCDS42804.1; -. [Q8TEW8-5]
DR CCDS; CCDS42805.1; -. [Q8TEW8-6]
DR CCDS; CCDS42806.1; -. [Q8TEW8-2]
DR CCDS; CCDS77511.1; -. [Q8TEW8-1]
DR RefSeq; NP_001289698.1; NM_001302769.1. [Q8TEW8-1]
DR RefSeq; NP_476518.4; NM_057177.6. [Q8TEW8-6]
DR RefSeq; NP_689739.4; NM_152526.5. [Q8TEW8-2]
DR RefSeq; NP_995585.2; NM_205863.3. [Q8TEW8-5]
DR AlphaFoldDB; Q8TEW8; -.
DR SMR; Q8TEW8; -.
DR BioGRID; 125592; 34.
DR CORUM; Q8TEW8; -.
DR DIP; DIP-42276N; -.
DR IntAct; Q8TEW8; 6.
DR MINT; Q8TEW8; -.
DR STRING; 9606.ENSP00000351618; -.
DR iPTMnet; Q8TEW8; -.
DR PhosphoSitePlus; Q8TEW8; -.
DR BioMuta; PARD3B; -.
DR DMDM; 30913163; -.
DR EPD; Q8TEW8; -.
DR jPOST; Q8TEW8; -.
DR MassIVE; Q8TEW8; -.
DR MaxQB; Q8TEW8; -.
DR PeptideAtlas; Q8TEW8; -.
DR PRIDE; Q8TEW8; -.
DR ProteomicsDB; 19836; -.
DR ProteomicsDB; 74517; -. [Q8TEW8-1]
DR ProteomicsDB; 74518; -. [Q8TEW8-2]
DR ProteomicsDB; 74519; -. [Q8TEW8-3]
DR ProteomicsDB; 74520; -. [Q8TEW8-4]
DR ProteomicsDB; 74521; -. [Q8TEW8-5]
DR Antibodypedia; 34169; 40 antibodies from 18 providers.
DR DNASU; 117583; -.
DR Ensembl; ENST00000349953.7; ENSP00000340280.3; ENSG00000116117.19. [Q8TEW8-5]
DR Ensembl; ENST00000351153.5; ENSP00000317261.2; ENSG00000116117.19. [Q8TEW8-6]
DR Ensembl; ENST00000358768.6; ENSP00000351618.2; ENSG00000116117.19. [Q8TEW8-2]
DR Ensembl; ENST00000406610.7; ENSP00000385848.2; ENSG00000116117.19. [Q8TEW8-1]
DR Ensembl; ENST00000415947.1; ENSP00000407718.1; ENSG00000116117.19. [Q8TEW8-4]
DR GeneID; 117583; -.
DR KEGG; hsa:117583; -.
DR MANE-Select; ENST00000406610.7; ENSP00000385848.2; NM_001302769.2; NP_001289698.1.
DR UCSC; uc002vao.3; human. [Q8TEW8-1]
DR CTD; 117583; -.
DR DisGeNET; 117583; -.
DR GeneCards; PARD3B; -.
DR HGNC; HGNC:14446; PARD3B.
DR HPA; ENSG00000116117; Low tissue specificity.
DR MIM; 619353; gene.
DR neXtProt; NX_Q8TEW8; -.
DR OpenTargets; ENSG00000116117; -.
DR PharmGKB; PA162398721; -.
DR VEuPathDB; HostDB:ENSG00000116117; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00950000183214; -.
DR HOGENOM; CLU_2605385_0_0_1; -.
DR InParanoid; Q8TEW8; -.
DR OMA; MVPPYEE; -.
DR OrthoDB; 908238at2759; -.
DR PhylomeDB; Q8TEW8; -.
DR TreeFam; TF323729; -.
DR PathwayCommons; Q8TEW8; -.
DR SignaLink; Q8TEW8; -.
DR BioGRID-ORCS; 117583; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; PARD3B; human.
DR GeneWiki; PARD3B; -.
DR GenomeRNAi; 117583; -.
DR Pharos; Q8TEW8; Tbio.
DR PRO; PR:Q8TEW8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8TEW8; protein.
DR Bgee; ENSG00000116117; Expressed in sural nerve and 147 other tissues.
DR ExpressionAtlas; Q8TEW8; baseline and differential.
DR Genevisible; Q8TEW8; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0043296; C:apical junction complex; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030010; P:establishment of cell polarity; IBA:GO_Central.
DR GO; GO:0051660; P:establishment of centrosome localization; IBA:GO_Central.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 3.
DR InterPro; IPR021922; Par3/HAL_N.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF12053; Par3_HAL_N_term; 1.
DR Pfam; PF00595; PDZ; 2.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF50156; SSF50156; 3.
DR PROSITE; PS50106; PDZ; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cell junction; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1205
FT /note="Partitioning defective 3 homolog B"
FT /id="PRO_0000185072"
FT DOMAIN 201..289
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 383..468
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 498..585
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 83..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..851
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CSB4"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CSB4"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CSB4"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CSB4"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CSB4"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CSB4"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 41..79
FT /note="GPGYWVKIHHLEYTDGGILDPDDVLADVVEDKDKLIAVF -> VSAARRSGA
FT RLQPRHLPGSWLLGEDSSLRIYRWRNPGSR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11586298"
FT /id="VSP_007476"
FT VAR_SEQ 80..1205
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11586298"
FT /id="VSP_007477"
FT VAR_SEQ 479..540
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12234671"
FT /id="VSP_007478"
FT VAR_SEQ 729..797
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_054048"
FT VAR_SEQ 730..798
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12234671"
FT /id="VSP_007479"
FT VAR_SEQ 914..1014
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12459187"
FT /id="VSP_007543"
FT VARIANT 165
FT /note="L -> P (in dbSNP:rs1510765)"
FT /evidence="ECO:0000269|PubMed:12459187,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_015664"
FT VARIANT 192
FT /note="R -> K (in dbSNP:rs2289025)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_015665"
FT VARIANT 295
FT /note="Q -> K (in dbSNP:rs1061522)"
FT /id="VAR_015666"
FT VARIANT 317
FT /note="K -> R (in dbSNP:rs34751010)"
FT /id="VAR_056642"
FT CONFLICT 893..901
FT /note="GTLKHGGLR -> WLINFVLIW (in Ref. 5; BAB71623)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1205 AA; 132494 MW; 26E6704CCDCE8CD8 CRC64;
MKVTVCFGRT GIVVPCKEGQ LRVGELTQQA LQRYLKTREK GPGYWVKIHH LEYTDGGILD
PDDVLADVVE DKDKLIAVFE EQEPLHKIES PSGNPADRQS PDAFETEVAA QLAAFKPIGG
EIEVTPSALK LGTPLLVRRS SDPVPGPPAD TQPSASHPGG QSLKLVVPDS TQNLEDREVL
NGVQTELLTS PRTKDTLSDM TRTVEISGEG GPLGIHVVPF FSSLSGRILG LFIRGIEDNS
RSKREGLFHE NECIVKINNV DLVDKTFAQA QDVFRQAMKS PSVLLHVLPP QNREQYEKSV
IGSLNIFGNN DGVLKTKVPP PVHGKSGLKT ANLTGTDSPE TDASASLQQN KSPRVPRLGG
KPSSPSLSPL MGFGSNKNAK KIKIDLKKGP EGLGFTVVTR DSSIHGPGPI FVKNILPKGA
AIKDGRLQSG DRILEVNGRD VTGRTQEELV AMLRSTKQGE TASLVIARQE GHFLPRELKG
EPDCCALSLE TSEQLTFEIP LNDSGSAGLG VSLKGNKSRE TGTDLGIFIK SIIHGGAAFK
DGRLRMNDQL IAVNGESLLG KSNHEAMETL RRSMSMEGNI RGMIQLVILR RPERPMEDPA
ECGAFSKPCF ENCQNAVTTS RRNDNSILHP LGTCSPQDKQ KGLLLPNDGW AESEVPPSPT
PHSALGLGLE DYSHSSGVDS AVYFPDQHIN FRSVTPARQP ESINLKASKS MDLVPDESKV
HSLAGQKSES PSKDFGPTLG LKKSSSLESL QTAVAEVRKN DLPFHRPRPH MVRGRGCNES
FRAAIDKSYD GPEEIEADGL SDKSSHSGQG ALNCESAPQG NSELEDMENK ARKVKKTKEK
EKKKEKGKLK VKEKKRKEEN EDPERKIKKK GFGAMLRFGK KKEDKGGKAE QKGTLKHGGL
REEELEKMKE ERERIGAKHQ ELREKQARGL LDYATGAIGS VYDMDDDEMD PNYARVNHFR
EPCTSANVFR SPSPPRAGPF GYPRDGHPLS PERDHLEGLY AKVNKPYHPL VPADSGRPTG
GSTDRIQKLR KEYYQARREG FPLYEDDEGR ARPSEYDLLW VPGRGPDGNA HNLRFEGMER
QYASLPRGGP ADPVDYLPAA PRGLYKEREL PYYPGAHPMH PPKGSYPRPT ELRVADLRYP
QHYPPPPAPQ HKGPFRQDVP PSPPQHQRMP AYQETGRPGP RGGSPDQYPY RTQDSRQKNP
MTAAV
