ZC3H1_HUMAN
ID ZC3H1_HUMAN Reviewed; 1989 AA.
AC O60293; Q6GMU1; Q6P2S9; Q6ZV36; Q96BE7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger C3H1 domain-containing protein;
DE AltName: Full=Coiled-coil domain-containing protein 131;
DE AltName: Full=Proline/serine-rich coiled-coil protein 2;
GN Name=ZFC3H1; Synonyms=CCDC131, KIAA0546, PSRC2;
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 2).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-396 (ISOFORMS 1/2).
RC TISSUE=Blood, and Lymph;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 730-1989 (ISOFORM 1).
RC TISSUE=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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-34, AND
RP IDENTIFICATION BY 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-352; SER-714;
RP SER-717; SER-719; SER-809; SER-949; SER-953; SER-998; SER-1046; SER-1303
RP AND SER-1304, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-15; SER-28; SER-352; SER-949; SER-1303 AND SER-1304,
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-352; SER-714;
RP SER-717; SER-719; SER-1303 AND SER-1304, AND IDENTIFICATION BY MASS
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-128; SER-251;
RP SER-352; SER-383; SER-662; THR-766; SER-805; SER-809; SER-948; SER-949;
RP SER-1046; SER-1301; SER-1303 AND SER-1304, AND IDENTIFICATION BY MASS
RP 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 [12]
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).
RN [13]
RP FUNCTION, SUBUNIT, INTERACTION WITH NCBP1/CBP80; PABPC4; PABPC1; PABPN1;
RP ZC3H14; MTREX AND ZC3H18, AND SUBCELLULAR LOCATION.
RX PubMed=27871484; DOI=10.1016/j.molcel.2016.09.025;
RA Meola N., Domanski M., Karadoulama E., Chen Y., Gentil C., Pultz D.,
RA Vitting-Seerup K., Lykke-Andersen S., Andersen J.S., Sandelin A.,
RA Jensen T.H.;
RT "Identification of a nuclear exosome decay pathway for processed
RT transcripts.";
RL Mol. Cell 64:520-533(2016).
CC -!- FUNCTION: Subunit of the trimeric poly(A) tail exosome targeting (PAXT)
CC complex, a complex that directs a subset of long and polyadenylated
CC poly(A) RNAs for exosomal degradation. The RNA exosome is fundamental
CC for the degradation of RNA in eukaryotic nuclei. Substrate targeting is
CC facilitated by its cofactor MTREX, which links to RNA-binding protein
CC adapters. {ECO:0000269|PubMed:27871484}.
CC -!- SUBUNIT: Component of the poly(A) tail exosome targeting (PAXT) complex
CC made of accessory factors, such as PABPN1, ZFC3H1 and MTREX, and which
CC directs a subset of long and polyadenylated poly(A) RNAs for exosomal
CC degradation (PubMed:27871484). Co-localizes with component of the CBC-
CC ARS2 (CBCA) complex. Binds to RNA exosome components. Interacts with
CC NCBP1/CBP80, ZC3H18, MTREX and PABPN1 in a RNase-insensitive manner,
CC and with PABPC4, PABPC1 and ZC3H14 in a RNase-sensitive manner
CC (PubMed:27871484). {ECO:0000269|PubMed:27871484}.
CC -!- INTERACTION:
CC O60293; P10242: MYB; NbExp=2; IntAct=EBI-746701, EBI-298355;
CC O60293-2; P23560-2: BDNF; NbExp=3; IntAct=EBI-25833374, EBI-12275524;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27871484}.
CC Note=Excluded from the nucleolus. {ECO:0000269|PubMed:27871484}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O60293-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60293-2; Sequence=VSP_024995;
CC Name=4;
CC IsoId=O60293-4; Sequence=VSP_024992, VSP_024993;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25472.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC86028.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB011118; BAA25472.2; ALT_INIT; mRNA.
DR EMBL; BC064336; AAH64336.1; ALT_TERM; mRNA.
DR EMBL; BC073843; AAH73843.1; -; mRNA.
DR EMBL; AK125035; BAC86028.1; ALT_INIT; mRNA.
DR CCDS; CCDS41813.1; -. [O60293-1]
DR PIR; T00325; T00325.
DR RefSeq; NP_659419.3; NM_144982.4. [O60293-1]
DR AlphaFoldDB; O60293; -.
DR BioGRID; 128206; 155.
DR IntAct; O60293; 93.
DR MINT; O60293; -.
DR STRING; 9606.ENSP00000368017; -.
DR iPTMnet; O60293; -.
DR PhosphoSitePlus; O60293; -.
DR BioMuta; ZFC3H1; -.
DR EPD; O60293; -.
DR jPOST; O60293; -.
DR MassIVE; O60293; -.
DR MaxQB; O60293; -.
DR PaxDb; O60293; -.
DR PeptideAtlas; O60293; -.
DR PRIDE; O60293; -.
DR ProteomicsDB; 49324; -. [O60293-1]
DR ProteomicsDB; 49325; -. [O60293-2]
DR ProteomicsDB; 49326; -. [O60293-4]
DR Antibodypedia; 1479; 71 antibodies from 19 providers.
DR DNASU; 196441; -.
DR Ensembl; ENST00000378743.9; ENSP00000368017.4; ENSG00000133858.17. [O60293-1]
DR Ensembl; ENST00000548100.1; ENSP00000450044.1; ENSG00000133858.17. [O60293-4]
DR Ensembl; ENST00000552994.5; ENSP00000446995.1; ENSG00000133858.17. [O60293-2]
DR GeneID; 196441; -.
DR KEGG; hsa:196441; -.
DR MANE-Select; ENST00000378743.9; ENSP00000368017.4; NM_144982.5; NP_659419.3.
DR UCSC; uc001swo.4; human. [O60293-1]
DR CTD; 196441; -.
DR DisGeNET; 196441; -.
DR GeneCards; ZFC3H1; -.
DR HGNC; HGNC:28328; ZFC3H1.
DR HPA; ENSG00000133858; Low tissue specificity.
DR neXtProt; NX_O60293; -.
DR OpenTargets; ENSG00000133858; -.
DR PharmGKB; PA164727644; -.
DR VEuPathDB; HostDB:ENSG00000133858; -.
DR eggNOG; KOG4839; Eukaryota.
DR GeneTree; ENSGT00390000001116; -.
DR HOGENOM; CLU_002490_0_0_1; -.
DR InParanoid; O60293; -.
DR OMA; SNAFTKP; -.
DR OrthoDB; 167870at2759; -.
DR PhylomeDB; O60293; -.
DR TreeFam; TF331613; -.
DR PathwayCommons; O60293; -.
DR SignaLink; O60293; -.
DR BioGRID-ORCS; 196441; 310 hits in 1086 CRISPR screens.
DR ChiTaRS; ZFC3H1; human.
DR GenomeRNAi; 196441; -.
DR Pharos; O60293; Tbio.
DR PRO; PR:O60293; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O60293; protein.
DR Bgee; ENSG00000133858; Expressed in sperm and 197 other tissues.
DR ExpressionAtlas; O60293; baseline and differential.
DR Genevisible; O60293; HS.
DR GO; GO:0000178; C:exosome (RNase complex); IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR019607; Putative_zinc-finger_domain.
DR InterPro; IPR039278; Red1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR21563; PTHR21563; 1.
DR Pfam; PF10650; zf-C3H1; 1.
DR SMART; SM00386; HAT; 5.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CHAIN 2..1989
FT /note="Zinc finger C3H1 domain-containing protein"
FT /id="PRO_0000286103"
FT REPEAT 1361..1400
FT /note="TPR 1"
FT REPEAT 1401..1434
FT /note="TPR 2"
FT REPEAT 1438..1471
FT /note="TPR 3"
FT REPEAT 1478..1511
FT /note="TPR 4"
FT REPEAT 1602..1635
FT /note="TPR 5"
FT REPEAT 1636..1669
FT /note="TPR 6"
FT REPEAT 1745..1778
FT /note="TPR 7"
FT ZN_FING 1185..1206
FT /note="C3H1-type"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 219..259
FT /evidence="ECO:0000255"
FT COILED 358..389
FT /evidence="ECO:0000255"
FT COILED 432..487
FT /evidence="ECO:0000255"
FT COILED 847..909
FT /evidence="ECO:0000255"
FT COILED 965..989
FT /evidence="ECO:0000255"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..578
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..612
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 766
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 998
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1046
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 340..346
FT /note="LQDKEQN -> NGIKYFS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024992"
FT VAR_SEQ 347..1989
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024993"
FT VAR_SEQ 1910..1989
FT /note="IAIAAEIVLKGQREVHRLYQRALQKLPLCASLWKDQLLFEASEGGKTDNLRK
FT LVSKCQEIGVSLNELLNLNSNKTESKNH -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9628581"
FT /id="VSP_024995"
FT VARIANT 1006
FT /note="E -> K (in dbSNP:rs1011332)"
FT /id="VAR_032070"
FT VARIANT 1807
FT /note="K -> R (in dbSNP:rs11541286)"
FT /id="VAR_032071"
SQ SEQUENCE 1989 AA; 226356 MW; E5FED04FAE866FDB CRC64;
MATADTPAPA SSGLSPKEEG ELEDGEISDD DNNSQIRSRS SSSSSGGGLL PYPRRRPPHS
ARGGGSGGGG GSSSSSSSSQ QQLRNFSRSR HASERGHLRG PSSYRPKEPF RSHPPSVRMP
SSSLSESSPR PSFWERSHLA LDRFRFRGRP YRGGSRWSRG RGVGERGGKP GCRPPLGGGA
GSGFSSSQSW REPSPPRKSS KSFGRSPSRK QNYSSKNENC VEETFEDLLL KYKQIQLELE
CINKDEKLAL SSKEENVQED PKTLNFEDQT STDNVSITKD SSKEVAPEEK TQVKTFQAFE
LKPLRQKLTL PGDKNRLKKV KDGAKPLSLK SDTTDSSQGL QDKEQNLTRR ISTSDILSEK
KLGEDEEELS ELQLRLLALQ SASKKWQQKE QQVMKESKEK LTKTKTVQQK VKTSTKTHSA
KKVSTTAKQA LRKQQTKAWK KLQQQKEQER QKEEDQRKQA EEEERRKREE EIRKIRDLSN
QEEQYNRFMK LVGGKRRSRS KSSDPDLRRS LDKQPTDSGG GIYQYDNYEE VAMDTDSETS
SPAPSPVQPP FFSECSLGYF SPAPSLSLPP PPQVSSLPPL SQPYVEGLCV SLEPLPPLPP
LPPLPPEDPE QPPKPPFADE EEEEEMLLRE ELLKSLANKR AFKPEETSSN SDPPSPPVLN
NSHPVPRSNL SIVSINTVSQ PRIQNPKFHR GPRLPRTVIS LPKHKSVVVT LNDSDDSESD
GEASKSTNSV FGGLESMIKE ARRTAEQASK PKVPPKSEKE NDPLRTPEAL PEEKKIEYRL
LKEEIANREK QRLIKSDQLK TSSSSPANSD VEIDGIGRIA MVTKQVTDAE SKLKKHRILL
MKDESVLKNL VQQEAKKKES VRNAEAKITK LTEQLQATEK ILNVNRMFLK KLQEQIHRVQ
QRVTIKKALT LKYGEELARA KAVASKEIGK RKLEQDRFGP NKMMRLDSSP VSSPRKHSAE
LIAMEKRRLQ KLEYEYALKI QKLKEARALK AKEQQNISPV VEEEPEFSLP QPSLHDLTQD
KLTLDTEEND VDDEILSGSS RERRRSFLES NYFTKPNLKH TDTANKECIN KLNKNTVEKP
ELFLGLKIGE LQKLYSKADS LKQLILKTTT GITEKVLHGQ EISVDVDFVT AQSKTMEVKP
CPFRPYHSPL LVFKSYRFSP YYRTKEKLPL SSVSYSNMIE PDQCFCRFDL TGTCNDDDCQ
WQHIQDYTLS RKQLFQDILS YNLSLIGCAE TSTNEEITAS AEKYVEKLFG VNKDRMSMDQ
MAVLLVSNIN ESKGHTPPFT TYKDKRKWKP KFWRKPISDN SFSSDEEQST GPIKYAFQPE
NQINVPALDT VVTPDDVRYF TNETDDIANL EASVLENPSH VQLWLKLAYK YLNQNEGECS
ESLDSALNVL ARALENNKDN PEIWCHYLRL FSKRGTKDEV QEMCETAVEY APDYQSFWTF
LHLESTFEEK DYVCERMLEF LMGAAKQETS NILSFQLLEA LLFRVQLHIF TGRCQSALAI
LQNALKSAND GIVAEYLKTS DRCLAWLAYI HLIEFNILPS KFYDPSNDNP SRIVNTESFV
MPWQAVQDVK TNPDMLLAVF EDAVKACTDE SLAVEERIEA CLPLYTNMIA LHQLLERYEA
AMELCKSLLE SCPINCQLLE ALVALYLQTN QHDKARAVWL TAFEKNPQNA EVFYHMCKFF
ILQNRGDNLL PFLRKFIASF FKPGFEKYNN LDLFRYLLNI PGPIDIPSRL CKGNFDDDMF
NHQVPYLWLI YCLCHPLQSS IKETVEAYEA ALGVAMRCDI VQKIWMDYLV FANNRAAGSR
NKVQEFKFFT DLVNRCLVTV PARYPIPFSS ADYWSNYEFH NRVIFFYLSC VPKTQHSKTL
ERFCSVMPAN SGLALRLLQH EWEESNVQIL KLQAKMFTYN IPTCLATWKI AIAAEIVLKG
QREVHRLYQR ALQKLPLCAS LWKDQLLFEA SEGGKTDNLR KLVSKCQEIG VSLNELLNLN
SNKTESKNH
