FA76B_HUMAN
ID FA76B_HUMAN Reviewed; 339 AA.
AC Q5HYJ3; B2R9C2; Q6PIU3; Q8TC53;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein FAM76B;
GN Name=FAM76B;
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] (ISOFORM 3).
RC TISSUE=Brain;
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 MRNA] (ISOFORM 1).
RC TISSUE=Fetal skin;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION BY
RP 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 [9]
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=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=19266028; DOI=10.1371/journal.pgen.1000397;
RA Salichs E., Ledda A., Mularoni L., Alba M.M., de la Luna S.;
RT "Genome-wide analysis of histidine repeats reveals their role in the
RT localization of human proteins to the nuclear speckles compartment.";
RL PLoS Genet. 5:E1000397-E1000397(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-193, 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-193, 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 [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=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION BY
RP 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).
CC -!- INTERACTION:
CC Q5HYJ3; P60412: KRTAP10-11; NbExp=3; IntAct=EBI-751192, EBI-10217483;
CC Q5HYJ3; P60370: KRTAP10-5; NbExp=5; IntAct=EBI-751192, EBI-10172150;
CC Q5HYJ3; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-751192, EBI-10172290;
CC Q5HYJ3; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-751192, EBI-10171774;
CC Q5HYJ3; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-751192, EBI-10172052;
CC Q5HYJ3; Q9BYR0: KRTAP4-7; NbExp=3; IntAct=EBI-751192, EBI-10302547;
CC Q5HYJ3; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-751192, EBI-3958099;
CC Q5HYJ3; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-751192, EBI-1044640;
CC Q5HYJ3-3; Q6P9H4: CNKSR3; NbExp=3; IntAct=EBI-11956087, EBI-10253274;
CC Q5HYJ3-3; O15354: GPR37; NbExp=3; IntAct=EBI-11956087, EBI-15639515;
CC Q5HYJ3-3; P28799: GRN; NbExp=6; IntAct=EBI-11956087, EBI-747754;
CC Q5HYJ3-3; P28799-2: GRN; NbExp=3; IntAct=EBI-11956087, EBI-25860013;
CC Q5HYJ3-3; P42858: HTT; NbExp=6; IntAct=EBI-11956087, EBI-466029;
CC Q5HYJ3-3; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-11956087, EBI-11959885;
CC Q5HYJ3-3; P60412: KRTAP10-11; NbExp=3; IntAct=EBI-11956087, EBI-10217483;
CC Q5HYJ3-3; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-11956087, EBI-10172150;
CC Q5HYJ3-3; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-11956087, EBI-10171774;
CC Q5HYJ3-3; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-11956087, EBI-10172052;
CC Q5HYJ3-3; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-11956087, EBI-10302392;
CC Q5HYJ3-3; Q9BYR2: KRTAP4-5; NbExp=3; IntAct=EBI-11956087, EBI-11993254;
CC Q5HYJ3-3; Q6L8G4: KRTAP5-11; NbExp=3; IntAct=EBI-11956087, EBI-11993296;
CC Q5HYJ3-3; Q701N4: KRTAP5-2; NbExp=3; IntAct=EBI-11956087, EBI-11958178;
CC Q5HYJ3-3; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-11956087, EBI-3958099;
CC Q5HYJ3-3; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-11956087, EBI-1044640;
CC Q5HYJ3-3; O76024: WFS1; NbExp=3; IntAct=EBI-11956087, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:19266028}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5HYJ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5HYJ3-2; Sequence=VSP_022679, VSP_022680;
CC Name=3;
CC IsoId=Q5HYJ3-3; Sequence=VSP_057354;
CC -!- DOMAIN: The polyhistidine repeat acts as a targeting signal to nuclear
CC speckles. {ECO:0000269|PubMed:19266028}.
CC -!- SIMILARITY: Belongs to the FAM76 family. {ECO:0000305}.
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DR EMBL; AK313727; BAG36469.1; -; mRNA.
DR EMBL; BX647586; CAI46088.1; -; mRNA.
DR EMBL; AP001877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW66962.1; -; Genomic_DNA.
DR EMBL; CH471065; EAW66963.1; -; Genomic_DNA.
DR EMBL; BC026013; AAH26013.1; -; mRNA.
DR EMBL; BC028727; AAH28727.1; -; mRNA.
DR CCDS; CCDS41700.1; -. [Q5HYJ3-1]
DR RefSeq; NP_653265.3; NM_144664.4. [Q5HYJ3-1]
DR AlphaFoldDB; Q5HYJ3; -.
DR SMR; Q5HYJ3; -.
DR BioGRID; 126816; 90.
DR IntAct; Q5HYJ3; 32.
DR MINT; Q5HYJ3; -.
DR STRING; 9606.ENSP00000351631; -.
DR GlyGen; Q5HYJ3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5HYJ3; -.
DR PhosphoSitePlus; Q5HYJ3; -.
DR BioMuta; FAM76B; -.
DR DMDM; 296439347; -.
DR EPD; Q5HYJ3; -.
DR jPOST; Q5HYJ3; -.
DR MassIVE; Q5HYJ3; -.
DR MaxQB; Q5HYJ3; -.
DR PaxDb; Q5HYJ3; -.
DR PeptideAtlas; Q5HYJ3; -.
DR PRIDE; Q5HYJ3; -.
DR ProteomicsDB; 3416; -.
DR ProteomicsDB; 62940; -. [Q5HYJ3-1]
DR ProteomicsDB; 62941; -. [Q5HYJ3-2]
DR Antibodypedia; 31661; 109 antibodies from 18 providers.
DR DNASU; 143684; -.
DR Ensembl; ENST00000358780.10; ENSP00000351631.5; ENSG00000077458.13. [Q5HYJ3-1]
DR Ensembl; ENST00000398187.6; ENSP00000381248.2; ENSG00000077458.13. [Q5HYJ3-3]
DR Ensembl; ENST00000543641.5; ENSP00000444087.1; ENSG00000077458.13. [Q5HYJ3-3]
DR GeneID; 143684; -.
DR KEGG; hsa:143684; -.
DR MANE-Select; ENST00000358780.10; ENSP00000351631.5; NM_144664.5; NP_653265.3.
DR UCSC; uc001pfn.3; human. [Q5HYJ3-1]
DR CTD; 143684; -.
DR DisGeNET; 143684; -.
DR GeneCards; FAM76B; -.
DR HGNC; HGNC:28492; FAM76B.
DR HPA; ENSG00000077458; Tissue enhanced (bone).
DR neXtProt; NX_Q5HYJ3; -.
DR OpenTargets; ENSG00000077458; -.
DR PharmGKB; PA142671838; -.
DR VEuPathDB; HostDB:ENSG00000077458; -.
DR eggNOG; KOG3990; Eukaryota.
DR GeneTree; ENSGT00940000159074; -.
DR HOGENOM; CLU_029220_1_0_1; -.
DR InParanoid; Q5HYJ3; -.
DR OMA; KECRGAF; -.
DR OrthoDB; 1061935at2759; -.
DR PhylomeDB; Q5HYJ3; -.
DR TreeFam; TF313644; -.
DR PathwayCommons; Q5HYJ3; -.
DR SignaLink; Q5HYJ3; -.
DR BioGRID-ORCS; 143684; 18 hits in 1083 CRISPR screens.
DR GeneWiki; FAM76B; -.
DR GenomeRNAi; 143684; -.
DR Pharos; Q5HYJ3; Tdark.
DR PRO; PR:Q5HYJ3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q5HYJ3; protein.
DR Bgee; ENSG00000077458; Expressed in sperm and 174 other tissues.
DR ExpressionAtlas; Q5HYJ3; baseline and differential.
DR Genevisible; Q5HYJ3; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR InterPro; IPR032017; FAM76.
DR InterPro; IPR029661; FAM76B.
DR PANTHER; PTHR46176; PTHR46176; 1.
DR PANTHER; PTHR46176:SF3; PTHR46176:SF3; 1.
DR Pfam; PF16046; FAM76; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..339
FT /note="Protein FAM76B"
FT /id="PRO_0000245763"
FT REGION 144..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 248..328
FT /evidence="ECO:0000255"
FT COMPBIAS 167..187
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80XP8"
FT VAR_SEQ 231..339
FT /note="SSSINQSADSGGTDNFVLISQLKEEVMSLKRLLQQRDQTILEKDKKLTELKA
FT DFQYQESNLRTKMNSMEKAHKETVEQLQAKNRELLKQVAALSKGKKFDKSGSILTSP
FT -> RCM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057354"
FT VAR_SEQ 231..233
FT /note="SSS -> RSM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022679"
FT VAR_SEQ 234..339
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022680"
FT CONFLICT 228
FT /note="N -> K (in Ref. 2; CAI46088)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="K -> E (in Ref. 2; CAI46088)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="G -> R (in Ref. 2; CAI46088)"
FT /evidence="ECO:0000305"
FT CONFLICT Q5HYJ3-2:232
FT /note="S -> C (in Ref. 3; AAH26013)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 38708 MW; 4ED7FEE05F23790C CRC64;
MAASALYACT KCTQRYPFEE LSQGQQLCKE CRIAHPIVKC TYCRSEFQQE SKTNTICKKC
AQNVKQFGTP KPCQYCNIIA AFIGTKCQRC TNSEKKYGPP QTCEQCKQQC AFDRKEEGRR
KVDGKLLCWL CTLSYKRVLQ KTKEQRKSLG SSHSNSSSSS LTEKDQHHPK HHHHHHHHHH
RHSSSHHKIS NLSPEEEQGL WKQSHKSSAT IQNETPKKKP KLESKPSNGD SSSINQSADS
GGTDNFVLIS QLKEEVMSLK RLLQQRDQTI LEKDKKLTEL KADFQYQESN LRTKMNSMEK
AHKETVEQLQ AKNRELLKQV AALSKGKKFD KSGSILTSP
