PCY1B_HUMAN
ID PCY1B_HUMAN Reviewed; 369 AA.
AC Q9Y5K3; A8IX00; B2RCX8; B4DK10; E9PD84; O60621; Q86XC9;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Choline-phosphate cytidylyltransferase B;
DE EC=2.7.7.15 {ECO:0000269|PubMed:10480912, ECO:0000269|PubMed:9593753};
DE AltName: Full=CCT-beta;
DE AltName: Full=CTP:phosphocholine cytidylyltransferase B;
DE Short=CCT B;
DE Short=CT B;
DE AltName: Full=Phosphorylcholine transferase B;
GN Name=PCYT1B; Synonyms=CCTB;
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), FUNCTION (ISOFORM 1), CATALYTIC
RP ACTIVITY (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), AND TISSUE
RP SPECIFICITY(ISOFORM 1).
RX PubMed=9593753; DOI=10.1074/jbc.273.22.14022;
RA Lykidis A., Murti K.G., Jackowski S.;
RT "Cloning and characterization of a second human CTP:phosphocholine
RT cytidylyltransferase.";
RL J. Biol. Chem. 273:14022-14029(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORMS 1 AND 2),
RP CATALYTIC ACTIVITY (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION (ISOFORMS 1 AND
RP 2), AND PHOSPHORYLATION (ISOFORMS 1 AND 2).
RX PubMed=10480912; DOI=10.1074/jbc.274.38.26992;
RA Lykidis A., Baburina I., Jackowski S.;
RT "Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms.
RT Identification of a new CCTbeta splice variant.";
RL J. Biol. Chem. 274:26992-27001(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Hippocampus, and Thalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319 AND SER-362, 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).
CC -!- FUNCTION: [Isoform 1]: Catalyzes the key rate-limiting step in the CDP-
CC choline pathway for phosphatidylcholine biosynthesis.
CC {ECO:0000269|PubMed:10480912, ECO:0000269|PubMed:9593753}.
CC -!- FUNCTION: [Isoform 2]: Catalyzes the key rate-limiting step in the CDP-
CC choline pathway for phosphatidylcholine biosynthesis.
CC {ECO:0000269|PubMed:10480912}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + phosphocholine = CDP-choline + diphosphate;
CC Xref=Rhea:RHEA:18997, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:58779, ChEBI:CHEBI:295975;
CC EC=2.7.7.15; Evidence={ECO:0000269|PubMed:10480912,
CC ECO:0000269|PubMed:9593753};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18998;
CC Evidence={ECO:0000305|PubMed:9593753};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 1/2.
CC {ECO:0000269|PubMed:10480912, ECO:0000269|PubMed:9593753}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P19836}.
CC -!- INTERACTION:
CC Q9Y5K3-3; P49585: PCYT1A; NbExp=6; IntAct=EBI-12280028, EBI-2563309;
CC Q9Y5K3-3; Q9Y5K3-3: PCYT1B; NbExp=3; IntAct=EBI-12280028, EBI-12280028;
CC Q9Y5K3-3; Q9BTV4: TMEM43; NbExp=3; IntAct=EBI-12280028, EBI-721293;
CC Q9Y5K3-3; Q8N0U8: VKORC1L1; NbExp=8; IntAct=EBI-12280028, EBI-11337915;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:9593753}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:10480912}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum
CC {ECO:0000269|PubMed:10480912}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=2; Synonyms=Beta-2 {ECO:0000303|PubMed:10480912};
CC IsoId=Q9Y5K3-1; Sequence=Displayed;
CC Name=1; Synonyms=Beta-1 {ECO:0000303|PubMed:10480912};
CC IsoId=Q9Y5K3-2; Sequence=VSP_001226;
CC Name=3;
CC IsoId=Q9Y5K3-3; Sequence=VSP_020045, VSP_020046;
CC Name=4;
CC IsoId=Q9Y5K3-4; Sequence=VSP_044659;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Highly expressed in testis, placenta,
CC brain, ovary, liver and fetal lung. {ECO:0000269|PubMed:10480912,
CC ECO:0000269|PubMed:9593753}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in brain, liver and fetal
CC lung. {ECO:0000269|PubMed:10480912}.
CC -!- PTM: [Isoform 1]: Phosphorylated. {ECO:0000269|PubMed:10480912}.
CC -!- PTM: [Isoform 2]: Extensively phosphorylated.
CC {ECO:0000269|PubMed:10480912}.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/pcyt1b/";
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DR EMBL; AF052510; AAC39754.1; -; mRNA.
DR EMBL; AF148464; AAD35088.1; -; mRNA.
DR EMBL; AK296333; BAG59022.1; -; mRNA.
DR EMBL; AK315323; BAG37725.1; -; mRNA.
DR EMBL; EU181262; ABW03924.1; -; Genomic_DNA.
DR EMBL; AC079168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW99021.1; -; Genomic_DNA.
DR EMBL; BC045634; AAH45634.2; -; mRNA.
DR CCDS; CCDS14213.1; -. [Q9Y5K3-1]
DR CCDS; CCDS55391.1; -. [Q9Y5K3-2]
DR CCDS; CCDS55392.1; -. [Q9Y5K3-4]
DR RefSeq; NP_001156736.1; NM_001163264.1. [Q9Y5K3-4]
DR RefSeq; NP_001156737.1; NM_001163265.1. [Q9Y5K3-2]
DR RefSeq; NP_004836.2; NM_004845.4. [Q9Y5K3-1]
DR AlphaFoldDB; Q9Y5K3; -.
DR SMR; Q9Y5K3; -.
DR BioGRID; 114854; 12.
DR IntAct; Q9Y5K3; 4.
DR STRING; 9606.ENSP00000368439; -.
DR DrugBank; DB00122; Choline.
DR DrugBank; DB14006; Choline salicylate.
DR SwissLipids; SLP:000001754; -.
DR iPTMnet; Q9Y5K3; -.
DR PhosphoSitePlus; Q9Y5K3; -.
DR BioMuta; PCYT1B; -.
DR DMDM; 12643330; -.
DR EPD; Q9Y5K3; -.
DR jPOST; Q9Y5K3; -.
DR MassIVE; Q9Y5K3; -.
DR MaxQB; Q9Y5K3; -.
DR PaxDb; Q9Y5K3; -.
DR PeptideAtlas; Q9Y5K3; -.
DR PRIDE; Q9Y5K3; -.
DR ProteomicsDB; 19606; -.
DR ProteomicsDB; 86427; -. [Q9Y5K3-1]
DR ProteomicsDB; 86428; -. [Q9Y5K3-2]
DR ProteomicsDB; 86429; -. [Q9Y5K3-3]
DR Antibodypedia; 505; 56 antibodies from 20 providers.
DR DNASU; 9468; -.
DR Ensembl; ENST00000356768.8; ENSP00000349211.4; ENSG00000102230.14. [Q9Y5K3-2]
DR Ensembl; ENST00000379144.7; ENSP00000368439.2; ENSG00000102230.14. [Q9Y5K3-1]
DR Ensembl; ENST00000379145.5; ENSP00000368440.1; ENSG00000102230.14. [Q9Y5K3-4]
DR GeneID; 9468; -.
DR KEGG; hsa:9468; -.
DR MANE-Select; ENST00000379144.7; ENSP00000368439.2; NM_004845.5; NP_004836.2.
DR UCSC; uc004dbi.4; human. [Q9Y5K3-1]
DR CTD; 9468; -.
DR DisGeNET; 9468; -.
DR GeneCards; PCYT1B; -.
DR HGNC; HGNC:8755; PCYT1B.
DR HPA; ENSG00000102230; Group enriched (brain, choroid plexus, retina, testis).
DR MIM; 300948; gene.
DR neXtProt; NX_Q9Y5K3; -.
DR OpenTargets; ENSG00000102230; -.
DR PharmGKB; PA33100; -.
DR VEuPathDB; HostDB:ENSG00000102230; -.
DR eggNOG; KOG2804; Eukaryota.
DR GeneTree; ENSGT00940000156040; -.
DR HOGENOM; CLU_034585_4_2_1; -.
DR InParanoid; Q9Y5K3; -.
DR OMA; FEDFSIC; -.
DR OrthoDB; 1172502at2759; -.
DR PhylomeDB; Q9Y5K3; -.
DR TreeFam; TF106336; -.
DR PathwayCommons; Q9Y5K3; -.
DR Reactome; R-HSA-1483191; Synthesis of PC.
DR SignaLink; Q9Y5K3; -.
DR UniPathway; UPA00753; UER00739.
DR BioGRID-ORCS; 9468; 7 hits in 692 CRISPR screens.
DR ChiTaRS; PCYT1B; human.
DR GeneWiki; PCYT1B; -.
DR GenomeRNAi; 9468; -.
DR Pharos; Q9Y5K3; Tbio.
DR PRO; PR:Q9Y5K3; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9Y5K3; protein.
DR Bgee; ENSG00000102230; Expressed in ventricular zone and 144 other tissues.
DR ExpressionAtlas; Q9Y5K3; baseline and differential.
DR Genevisible; Q9Y5K3; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0006657; P:CDP-choline pathway; IDA:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR CDD; cd02174; CCT; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR041723; CCT.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR045049; Pcy1-like.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR10739; PTHR10739; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Nucleotidyltransferase; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..369
FT /note="Choline-phosphate cytidylyltransferase B"
FT /id="PRO_0000208456"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84..92
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 122
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 168..169
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 173
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 196..200
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811Q9"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZC4"
FT MOD_RES 345
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811Q9"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..39
FT /note="MPVVTTDAESETGIPKSLSNEPPSETMEEIEHTCPQPRL -> MVGHQECIM
FT EEDNRAPQLWRK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044659"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020045"
FT VAR_SEQ 17..39
FT /note="SLSNEPPSETMEEIEHTCPQPRL -> MVGNQECIMEEDNRAPQLWRK (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020046"
FT VAR_SEQ 321..369
FT /note="VSSPTRSRSPSRSPSPTFSWLPLKTSPPSSPKAASASISSMSEGDEDEK ->
FT LKSWARCRDF (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:9593753"
FT /id="VSP_001226"
FT CONFLICT 154
FT /note="T -> S (in Ref. 3; BAG59022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 41940 MW; 87A00617DF690DD1 CRC64;
MPVVTTDAES ETGIPKSLSN EPPSETMEEI EHTCPQPRLT LTAPAPFADE TNCQCQAPHE
KLTIAQARLG TPADRPVRVY ADGIFDLFHS GHARALMQAK TLFPNSYLLV GVCSDDLTHK
FKGFTVMNEA ERYEALRHCR YVDEVIRDAP WTLTPEFLEK HKIDFVAHDD IPYSSAGSDD
VYKHIKEAGM FVPTQRTEGI STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKRY
RFQNQVDKMK EKVKNVEERS KEFVNRVEEK SHDLIQKWEE KSREFIGNFL ELFGPDGAWK
QMFQERSSRM LQALSPKQSP VSSPTRSRSP SRSPSPTFSW LPLKTSPPSS PKAASASISS
MSEGDEDEK
