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Terminal uridylyltransferase 7 (TUTase 7) (EC 2.7.7.52) (Zinc finger CCHC domain-containing protein 6)

 TUT7_HUMAN              Reviewed;        1495 AA.
Q5VYS8; Q5H9T0; Q5VYS5; Q5VYS7; Q658Z9; Q659A2; Q6MZJ3; Q8N5F0;
Q96N57; Q96NE8; Q9C0F2; Q9H8M6;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 1.
27-SEP-2017, entry version 121.
RecName: Full=Terminal uridylyltransferase 7;
Short=TUTase 7;
EC=2.7.7.52;
AltName: Full=Zinc finger CCHC domain-containing protein 6;
Name=ZCCHC6; Synonyms=HS2, KIAA1711, TUT7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
TISSUE=Cervix, Endometrial tumor, Fetal kidney, and Skeletal muscle;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1385 (ISOFORM 1), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1019-1495 (ISOFORM 6).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 406-1495 (ISOFORM 1).
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:347-355(2000).
[6]
ABSENCE OF FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
PubMed=18172165; DOI=10.1101/gad.1622708;
Mullen T.E., Marzluff W.F.;
"Degradation of histone mRNA requires oligouridylation followed by
decapping and simultaneous degradation of the mRNA both 5' to 3' and
3' to 5'.";
Genes Dev. 22:50-65(2008).
[7]
CATALYTIC ACTIVITY.
PubMed=17353264; DOI=10.1128/MCB.02209-06;
Rissland O.S., Mikulasova A., Norbury C.J.;
"Efficient RNA polyuridylation by noncanonical poly(A) polymerases.";
Mol. Cell. Biol. 27:3612-3624(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; THR-64; SER-172 AND
SER-844, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
FUNCTION.
PubMed=19703396; DOI=10.1016/j.cell.2009.08.002;
Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H.,
Han J., Kim V.N.;
"TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through
pre-microRNA uridylation.";
Cell 138:696-708(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
FUNCTION IN PRE-LET-7 URIDYLATION.
PubMed=22898984; DOI=10.1261/rna.034538.112;
Thornton J.E., Chang H.M., Piskounova E., Gregory R.I.;
"Lin28-mediated control of let-7 microRNA expression by alternative
TUTases Zcchc11 (TUT4) and Zcchc6 (TUT7).";
RNA 18:1875-1885(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-64 AND SER-600, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25480299; DOI=10.1016/j.cell.2014.10.055;
Lim J., Ha M., Chang H., Kwon S.C., Simanshu D.K., Patel D.J.,
Kim V.N.;
"Uridylation by TUT4 and TUT7 marks mRNA for degradation.";
Cell 159:1365-1376(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Uridylyltransferase that mediates the terminal
uridylation of mRNAs with short (less than 25 nucleotides) poly(A)
tails, hence facilitating global mRNA decay (PubMed:19703396,
PubMed:25480299). Involved in microRNA (miRNA)-induced gene
silencing through uridylation of deadenylated miRNA targets
(PubMed:25480299). Also acts as a suppressor of miRNA biogenesis
by mediating the terminal uridylation of some miRNA precursors,
including that of let-7 (pre-let-7). Uridylated pre-let-7 RNA is
not processed by Dicer and undergo degradation. Pre-let-7
uridylation is strongly enhanced in the presence of LIN28A
(PubMed:22898984). Due to functional redundancy between ZCCHC6 and
ZCCHC11, the identification of the specific role of each of these
proteins is difficult. {ECO:0000269|PubMed:19703396,
ECO:0000269|PubMed:22898984, ECO:0000269|PubMed:25480299}.
-!- CATALYTIC ACTIVITY: UTP + RNA(n) = diphosphate + RNA(n+1).
{ECO:0000269|PubMed:17353264}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25480299}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q5VYS8-1; Sequence=Displayed;
Name=2;
IsoId=Q5VYS8-2; Sequence=VSP_013837, VSP_013838;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q5VYS8-3; Sequence=VSP_013835, VSP_013836;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q5VYS8-4; Sequence=VSP_013832, VSP_013839;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q5VYS8-5; Sequence=VSP_013833, VSP_013834;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q5VYS8-6; Sequence=VSP_013840;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB14584.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB71052.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AL832026; CAH56219.1; -; mRNA.
EMBL; AL832193; CAH56214.1; -; mRNA.
EMBL; BX641077; CAE46038.1; -; mRNA.
EMBL; CR933643; CAI45944.1; -; mRNA.
EMBL; CR933644; CAI45945.1; -; mRNA.
EMBL; CR936608; CAI56753.1; -; mRNA.
EMBL; AL353678; CAH71514.1; ALT_SEQ; Genomic_DNA.
EMBL; AL137849; CAH71514.1; JOINED; Genomic_DNA.
EMBL; AL353678; CAH71515.1; ALT_SEQ; Genomic_DNA.
EMBL; AL137849; CAH71515.1; JOINED; Genomic_DNA.
EMBL; AL353678; CAH71518.1; -; Genomic_DNA.
EMBL; AL137849; CAH71518.1; JOINED; Genomic_DNA.
EMBL; AL353678; CAH71519.1; -; Genomic_DNA.
EMBL; AL137849; CAH71519.1; JOINED; Genomic_DNA.
EMBL; AL137849; CAI14918.1; ALT_SEQ; Genomic_DNA.
EMBL; AL353678; CAI14918.1; JOINED; Genomic_DNA.
EMBL; AL137849; CAI14919.1; -; Genomic_DNA.
EMBL; AL353678; CAI14919.1; JOINED; Genomic_DNA.
EMBL; AL137849; CAI14920.1; -; Genomic_DNA.
EMBL; AL353678; CAI14920.1; JOINED; Genomic_DNA.
EMBL; AL137849; CAI14921.1; -; Genomic_DNA.
EMBL; AL353678; CAI14921.1; JOINED; Genomic_DNA.
EMBL; BC032456; AAH32456.1; -; mRNA.
EMBL; AK023471; BAB14584.1; ALT_INIT; mRNA.
EMBL; AK055546; BAB70951.1; -; mRNA.
EMBL; AK055948; BAB71052.1; ALT_INIT; mRNA.
EMBL; AB051498; BAB21802.1; -; mRNA.
CCDS; CCDS35057.1; -. [Q5VYS8-1]
CCDS; CCDS55323.1; -. [Q5VYS8-4]
RefSeq; NP_001171988.1; NM_001185059.1. [Q5VYS8-1]
RefSeq; NP_001172003.1; NM_001185074.1. [Q5VYS8-4]
RefSeq; NP_001317647.1; NM_001330718.1.
RefSeq; NP_078893.2; NM_024617.3. [Q5VYS8-1]
RefSeq; XP_016870619.1; XM_017015130.1. [Q5VYS8-1]
RefSeq; XP_016870620.1; XM_017015131.1. [Q5VYS8-1]
UniGene; Hs.597057; -.
ProteinModelPortal; Q5VYS8; -.
SMR; Q5VYS8; -.
BioGrid; 122795; 31.
IntAct; Q5VYS8; 18.
MINT; MINT-4718069; -.
STRING; 9606.ENSP00000365130; -.
iPTMnet; Q5VYS8; -.
PhosphoSitePlus; Q5VYS8; -.
BioMuta; ZCCHC6; -.
DMDM; 67462100; -.
EPD; Q5VYS8; -.
MaxQB; Q5VYS8; -.
PaxDb; Q5VYS8; -.
PeptideAtlas; Q5VYS8; -.
PRIDE; Q5VYS8; -.
DNASU; 79670; -.
Ensembl; ENST00000375960; ENSP00000365127; ENSG00000083223. [Q5VYS8-4]
Ensembl; ENST00000375963; ENSP00000365130; ENSG00000083223. [Q5VYS8-1]
GeneID; 79670; -.
KEGG; hsa:79670; -.
UCSC; uc004aoq.4; human. [Q5VYS8-1]
CTD; 79670; -.
EuPathDB; HostDB:ENSG00000083223.17; -.
GeneCards; ZCCHC6; -.
H-InvDB; HIX0008144; -.
HGNC; HGNC:25817; ZCCHC6.
HPA; HPA020615; -.
HPA; HPA020620; -.
MIM; 613467; gene.
neXtProt; NX_Q5VYS8; -.
OpenTargets; ENSG00000083223; -.
PharmGKB; PA134971144; -.
eggNOG; KOG2277; Eukaryota.
eggNOG; COG5260; LUCA.
GeneTree; ENSGT00550000074490; -.
InParanoid; Q5VYS8; -.
KO; K13291; -.
OMA; KYFALPH; -.
OrthoDB; EOG091G01G7; -.
PhylomeDB; Q5VYS8; -.
TreeFam; TF315661; -.
BRENDA; 2.7.7.52; 2681.
Reactome; R-HSA-429947; Deadenylation of mRNA.
ChiTaRS; ZCCHC6; human.
GeneWiki; ZCCHC6; -.
GenomeRNAi; 79670; -.
PRO; PR:Q5VYS8; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000083223; -.
CleanEx; HS_ZCCHC6; -.
ExpressionAtlas; Q5VYS8; baseline and differential.
Genevisible; Q5VYS8; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
GO; GO:0031123; P:RNA 3'-end processing; IDA:UniProtKB.
Gene3D; 4.10.60.10; -; 4.
InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
InterPro; IPR002058; PAP_assoc.
InterPro; IPR002934; Polymerase_NTP_transf_dom.
InterPro; IPR001878; Znf_CCHC.
Pfam; PF01909; NTP_transf_2; 1.
Pfam; PF03828; PAP_assoc; 2.
Pfam; PF00098; zf-CCHC; 3.
SMART; SM00343; ZnF_C2HC; 3.
SMART; SM00451; ZnF_U1; 1.
SUPFAM; SSF57756; SSF57756; 3.
PROSITE; PS50158; ZF_CCHC; 3.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Magnesium;
Manganese; Metal-binding; Nucleotidyltransferase; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transferase; Zinc;
Zinc-finger.
CHAIN 1 1495 Terminal uridylyltransferase 7.
/FTId=PRO_0000150957.
DOMAIN 551 600 PAP-associated 1.
DOMAIN 1233 1286 PAP-associated 2.
ZN_FING 963 980 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1345 1362 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1451 1468 CCHC-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
COMPBIAS 20 23 Poly-Asp.
COMPBIAS 815 936 Glu-rich.
COMPBIAS 1367 1370 Poly-Arg.
METAL 1058 1058 Magnesium or manganese; catalytic.
{ECO:0000250}.
METAL 1060 1060 Magnesium or manganese; catalytic.
{ECO:0000250}.
MOD_RES 57 57 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 64 64 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BLK4}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 600 600 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 844 844 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 893 893 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BLK4}.
MOD_RES 939 939 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
VAR_SEQ 363 486 MSQPDVLLLVQECLKNSDSFIDVDADFHARVPVVVCREKQS
GLLCKVSAGNENACLTTKHLTALGKLEPKLVPLVIAFRYWA
KLCSIDRPEEGGLPPYVFALMAIFFLQQRKEPLLPVYLGSW
I -> I (in isoform 4).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_013832.
VAR_SEQ 403 412 SGLLCKVSAG -> RSHFFKLFIY (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013833.
VAR_SEQ 413 1495 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013834.
VAR_SEQ 538 544 SLILDVK -> VSSLLCR (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_013835.
VAR_SEQ 545 1495 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_013836.
VAR_SEQ 597 615 DPYSVKRNVARTLNSQPVF -> GISKCLSYSPPLFFLKVP
V (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_013837.
VAR_SEQ 616 1495 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_013838.
VAR_SEQ 960 1072 Missing (in isoform 4).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_013839.
VAR_SEQ 1157 1194 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_013840.
VARIANT 40 40 A -> V (in dbSNP:rs2378695).
/FTId=VAR_053753.
CONFLICT 157 157 K -> R (in Ref. 4; BAB70951).
{ECO:0000305}.
CONFLICT 316 316 R -> T (in Ref. 1; CAE46038).
{ECO:0000305}.
CONFLICT 514 514 S -> N (in Ref. 1; CAE46038).
{ECO:0000305}.
CONFLICT 900 900 G -> V (in Ref. 1; CAI45944).
{ECO:0000305}.
CONFLICT 937 937 Missing (in Ref. 1; CAI45944/CAH56219).
{ECO:0000305}.
CONFLICT 1104 1104 V -> M (in Ref. 1; CAH56219).
{ECO:0000305}.
CONFLICT 1319 1319 P -> S (in Ref. 1; CAH56219).
{ECO:0000305}.
CONFLICT 1474 1474 G -> D (in Ref. 1; CAI45944).
{ECO:0000305}.
SEQUENCE 1495 AA; 171229 MW; 1AAB0F5B37266FF9 CRC64;
MGDTAKPYFV KRTKDRGTMD DDDFRRGHPQ QDYLIIDDHA KGHGSKMEKG LQKKKITPGN
YGNTPRKGPC AVSSNPYAFK NPIYSQPAWM NDSHKDQSKR WLSDEHTGNS DNWREFKPGP
RIPVINRQRK DSFQENEDGY RWQDTRGCRT VRRLFHKDLT SLETTSEMEA GSPENKKQRS
RPRKPRKTRN EENEQDGDLE GPVIDESVLS TKELLGLQQA EERLKRDCID RLKRRPRNYP
TAKYTCRLCD VLIESIAFAH KHIKEKRHKK NIKEKQEEEL LTTLPPPTPS QINAVGIAID
KVVQEFGLHN ENLEQRLEIK RIMENVFQHK LPDCSLRLYG SSCSRLGFKN SDVNIDIQFP
AIMSQPDVLL LVQECLKNSD SFIDVDADFH ARVPVVVCRE KQSGLLCKVS AGNENACLTT
KHLTALGKLE PKLVPLVIAF RYWAKLCSID RPEEGGLPPY VFALMAIFFL QQRKEPLLPV
YLGSWIEGFS LSKLGNFNLQ DIEKDVVIWE HTDSAAGDTG ITKEEAPRET PIKRGQVSLI
LDVKHQPSVP VGQLWVELLR FYALEFNLAD LVISIRVKEL VSRELKDWPK KRIAIEDPYS
VKRNVARTLN SQPVFEYILH CLRTTYKYFA LPHKITKSSL LKPLNAITCI SEHSKEVINH
HPDVQTKDDK LKNSVLAQGP GATSSAANTC KVQPLTLKET AESFGSPPKE EMGNEHISVH
PENSDCIQAD VNSDDYKGDK VYHPETGRKN EKEKVGRKGK HLLTVDQKRG EHVVCGSTRN
NESESTLDLE GFQNPTAKEC EGLATLDNKA DLDGESTEGT EELEDSLNHF THSVQGQTSE
MIPSDEEEED DEEEEEEEEP RLTINQREDE DGMANEDELD NTYTGSGDED ALSEEDDELG
EAAKYEDVKE CGKHVERALL VELNKISLKE ENVCEEKNSP VDQSDFFYEF SKLIFTKGKS
PTVVCSLCKR EGHLKKDCPE DFKRIQLEPL PPLTPKFLNI LDQVCIQCYK DFSPTIIEDQ
AREHIRQNLE SFIRQDFPGT KLSLFGSSKN GFGFKQSDLD VCMTINGLET AEGLDCVRTI
EELARVLRKH SGLRNILPIT TAKVPIVKFF HLRSGLEVDI SLYNTLALHN TRLLSAYSAI
DPRVKYLCYT MKVFTKMCDI GDASRGSLSS YAYTLMVLYF LQQRNPPVIP VLQEIYKGEK
KPEIFVDGWN IYFFDQIDEL PTYWSECGKN TESVGQLWLG LLRFYTEEFD FKEHVISIRR
KSLLTTFKKQ WTSKYIVIED PFDLNHNLGA GLSRKMTNFI MKAFINGRRV FGIPVKGFPK
DYPSKMEYFF DPDVLTEGEL APNDRCCRIC GKIGHFMKDC PMRRKVRRRR DQEDALNQRY
PENKEKRSKE DKEIHNKYTE REVSTKEDKP IQCTPQKAKP MRAAADLGRE KILRPPVEKW
KRQDDKDLRE KRCFICGREG HIKKECPQFK GSSGSLSSKY MTQGKASAKR TQQES


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