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Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16 (EC 3.6.4.13) (ATP-dependent RNA helicase DHX38) (DEAH box protein 38)

 PRP16_HUMAN             Reviewed;        1227 AA.
Q92620; B4DVG8; D3DWS7; O75212; Q96HN7;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
24-JAN-2006, sequence version 2.
25-OCT-2017, entry version 175.
RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16;
EC=3.6.4.13;
AltName: Full=ATP-dependent RNA helicase DHX38;
AltName: Full=DEAH box protein 38;
Name=DHX38; Synonyms=DDX38, KIAA0224, PRP16;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-1217.
PubMed=9524131; DOI=10.1093/emboj/17.7.2095;
Zhou Z., Reed R.;
"Human homologs of yeast prp16 and prp17 reveal conservation of the
mechanism for catalytic step II of pre-mRNA splicing.";
EMBO J. 17:2095-2106(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-1217.
TISSUE=Bone marrow;
PubMed=9039502; DOI=10.1093/dnares/3.5.321;
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. VI.
The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
analysis of cDNA clones from cell line KG-1 and brain.";
DNA Res. 3:321-329(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10493829; DOI=10.1006/geno.1999.5927;
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R.,
Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L.,
Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E.,
Harris P.C., Venter J.C., Adams M.D.;
"Genome duplications and other features in 12 Mb of DNA sequence from
human chromosome 16p and 16q.";
Genomics 60:295-308(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Spleen;
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 GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Placenta;
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).
[8]
PROTEIN SEQUENCE OF 2-12 AND 692-707, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT GLY-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[9]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1194, 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).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-260, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, 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).
[14]
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; THR-117 AND SER-224,
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]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-482, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-482; LYS-483; LYS-504 AND
LYS-1166, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Probable ATP-binding RNA helicase involved in pre-mRNA
splicing.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Identified in the spliceosome C complex.
{ECO:0000269|PubMed:11991638}.
-!- INTERACTION:
O60231:DHX16; NbExp=2; IntAct=EBI-1043041, EBI-311446;
Q92917:GPKOW; NbExp=2; IntAct=EBI-1043041, EBI-746309;
Q96RS6:NUDCD1; NbExp=2; IntAct=EBI-1043041, EBI-2512429;
P98175:RBM10; NbExp=2; IntAct=EBI-1043041, EBI-721525;
Q9NYB0:TERF2IP; NbExp=2; IntAct=EBI-1043041, EBI-750109;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q92620-1; Sequence=Displayed;
Name=2;
IsoId=Q92620-2; Sequence=VSP_056045;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
subfamily. PRP16 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA13213.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF038391; AAC39729.1; -; mRNA.
EMBL; D86977; BAA13213.2; ALT_INIT; mRNA.
EMBL; AK301074; BAG62680.1; -; mRNA.
EMBL; AC009087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004682; AAC27431.1; -; Genomic_DNA.
EMBL; CH471166; EAW59180.1; -; Genomic_DNA.
EMBL; CH471166; EAW59190.1; -; Genomic_DNA.
EMBL; BC004235; AAH04235.1; -; mRNA.
EMBL; BC008340; AAH08340.1; -; mRNA.
CCDS; CCDS10907.1; -. [Q92620-1]
RefSeq; NP_054722.2; NM_014003.3. [Q92620-1]
RefSeq; XP_011521786.1; XM_011523484.1. [Q92620-1]
RefSeq; XP_011521787.1; XM_011523485.1. [Q92620-1]
UniGene; Hs.151218; -.
ProteinModelPortal; Q92620; -.
SMR; Q92620; -.
BioGrid; 115129; 52.
CORUM; Q92620; -.
IntAct; Q92620; 15.
MINT; MINT-2813093; -.
STRING; 9606.ENSP00000268482; -.
iPTMnet; Q92620; -.
PhosphoSitePlus; Q92620; -.
BioMuta; DHX38; -.
DMDM; 85700389; -.
EPD; Q92620; -.
MaxQB; Q92620; -.
PaxDb; Q92620; -.
PeptideAtlas; Q92620; -.
PRIDE; Q92620; -.
DNASU; 9785; -.
Ensembl; ENST00000268482; ENSP00000268482; ENSG00000140829. [Q92620-1]
GeneID; 9785; -.
KEGG; hsa:9785; -.
UCSC; uc002fcb.4; human. [Q92620-1]
CTD; 9785; -.
DisGeNET; 9785; -.
EuPathDB; HostDB:ENSG00000140829.11; -.
GeneCards; DHX38; -.
HGNC; HGNC:17211; DHX38.
HPA; HPA041347; -.
HPA; HPA041604; -.
MIM; 605584; gene.
neXtProt; NX_Q92620; -.
OpenTargets; ENSG00000140829; -.
PharmGKB; PA27225; -.
eggNOG; KOG0925; Eukaryota.
eggNOG; COG1643; LUCA.
GeneTree; ENSGT00900000140958; -.
HOGENOM; HOG000175261; -.
HOVERGEN; HBG039428; -.
InParanoid; Q92620; -.
KO; K12815; -.
OMA; PSRSTWE; -.
OrthoDB; EOG091G030Q; -.
PhylomeDB; Q92620; -.
TreeFam; TF105793; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72187; mRNA 3'-end processing.
ChiTaRS; DHX38; human.
GeneWiki; DHX38; -.
GenomeRNAi; 9785; -.
PRO; PR:Q92620; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000140829; -.
CleanEx; HS_DHX38; -.
ExpressionAtlas; Q92620; baseline and differential.
Genevisible; Q92620; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0006405; P:RNA export from nucleus; TAS:Reactome.
GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
CDD; cd00079; HELICc; 1.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
InterPro; IPR011709; DUF1605.
InterPro; IPR007502; Helicase-assoc_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00270; DEAD; 1.
Pfam; PF04408; HA2; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF07717; OB_NTP_bind; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00847; HA2; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Complete proteome;
Direct protein sequencing; Helicase; Hydrolase; Isopeptide bond;
mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Spliceosome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.8}.
CHAIN 2 1227 Pre-mRNA-splicing factor ATP-dependent
RNA helicase PRP16.
/FTId=PRO_0000055147.
DOMAIN 542 705 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 727 902 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 555 562 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 652 655 DEAH box.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.8}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 117 117 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 260 260 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1194 1194 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
CROSSLNK 482 482 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 483 483 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 504 504 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1166 1166 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 99 786 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056045.
VARIANT 1217 1217 T -> A. {ECO:0000269|PubMed:9039502,
ECO:0000269|PubMed:9524131}.
/FTId=VAR_015518.
SEQUENCE 1227 AA; 140503 MW; 80D06118D0D465E5 CRC64;
MGDTSEDASI HRLEGTDLDC QVGGLICKSK SAASEQHVFK APAPRPSLLG LDLLASLKRR
EREEKDDGED KKKSKVSSYK DWEESKDDQK DAEEEGGDQA GQNIRKDRHY RSARVETPSH
PGGVSEEFWE RSRQRERERR EHGVYASSKE EKDWKKEKSR DRDYDRKRDR DERDRSRHSS
RSERDGGSER SSRRNEPESP RHRPKDAATP SRSTWEEEDS GYGSSRRSQW ESPSPTPSYR
DSERSHRLST RDRDRSVRGK YSDDTPLPTP SYKYNEWADD RRHLGSTPRL SRGRGRREEG
EEGISFDTEE ERQQWEDDQR QADRDWYMMD EGYDEFHNPL AYSSEDYVRR REQHLHKQKQ
KRISAQRRQI NEDNERWETN RMLTSGVVHR LEVDEDFEED NAAKVHLMVH NLVPPFLDGR
IVFTKQPEPV IPVKDATSDL AIIARKGSQT VRKHREQKER KKAQHKHWEL AGTKLGDIMG
VKKEEEPDKA VTEDGKVDYR TEQKFADHMK RKSEASSEFA KKKSILEQRQ YLPIFAVQQE
LLTIIRDNSI VIVVGETGSG KTTQLTQYLH EDGYTDYGMI GCTQPRRVAA MSVAKRVSEE
MGGNLGEEVG YAIRFEDCTS ENTLIKYMTD GILLRESLRE ADLDHYSAII MDEAHERSLN
TDVLFGLLRE VVARRSDLKL IVTSATMDAE KFAAFFGNVP IFHIPGRTFP VDILFSKTPQ
EDYVEAAVKQ SLQVHLSGAP GDILIFMPGQ EDIEVTSDQI VEHLEELENA PALAVLPIYS
QLPSDLQAKI FQKAPDGVRK CIVATNIAET SLTVDGIMFV IDSGYCKLKV FNPRIGMDAL
QIYPISQANA NQRSGRAGRT GPGQCFRLYT QSAYKNELLT TTVPEIQRTN LANVVLLLKS
LGVQDLLQFH FMDPPPEDNM LNSMYQLWIL GALDNTGGLT STGRLMVEFP LDPALSKMLI
VSCDMGCSSE ILLIVSMLSV PAIFYRPKGR EEESDQIREK FAVPESDHLT YLNVYLQWKN
NNYSTIWCND HFIHAKAMRK VREVRAQLKD IMVQQRMSLA SCGTDWDIVR KCICAAYFHQ
AAKLKGIGEY VNIRTGMPCH LHPTSSLFGM GYTPDYIVYH ELVMTTKEYM QCVTAVDGEW
LAELGPMFYS VKQAGKSRQE NRRRAKEEAS AMEEEMALAE EQLRARRQEQ EKRSPLGSVR
STKIYTPGRK EQGEPMTPRR TPARFGL


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