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SEN2_HUMAN
ID   SEN2_HUMAN              Reviewed;         465 AA.
AC   Q8NCE0; B7Z6K1; C9IZI7; G5E9Q3; Q8WTW7; Q9BPU7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=tRNA-splicing endonuclease subunit Sen2;
DE            EC=4.6.1.16;
DE   AltName: Full=tRNA-intron endonuclease Sen2;
DE            Short=HsSen2;
GN   Name=TSEN2; Synonyms=SEN2;
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] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
RP   FUNCTION, SUBCELLULAR LOCATION, COMPONENT OF A COMPLEX WITH SEN15; SEN34;
RP   SEN54 AND CLP1, AND TISSUE SPECIFICITY.
RX   PubMed=15109492; DOI=10.1016/s0092-8674(04)00342-3;
RA   Paushkin S.V., Patel M., Furia B.S., Peltz S.W., Trotta C.R.;
RT   "Identification of a human endonuclease complex reveals a link between tRNA
RT   splicing and pre-mRNA 3' end formation.";
RL   Cell 117:311-321(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC   TISSUE=Placenta, and Teratocarcinoma;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon, Eye, and Skin;
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   [7]
RP   VARIANT PCH2B CYS-309.
RX   PubMed=18711368; DOI=10.1038/ng.204;
RA   Budde B.S., Namavar Y., Barth P.G., Poll-The B.T., Nuernberg G., Becker C.,
RA   van Ruissen F., Weterman M.A.J., Fluiter K., te Beek E.T., Aronica E.,
RA   van der Knaap M.S., Hoehne W., Toliat M.R., Crow Y.J., Steinling M.,
RA   Voit T., Roelenso F., Brussel W., Brockmann K., Kyllerman M.,
RA   Boltshauser E., Hammersen G., Willemsen M., Basel-Vanagaite L.,
RA   Kraegeloh-Mann I., de Vries L.S., Sztriha L., Muntoni F., Ferrie C.D.,
RA   Battini R., Hennekam R.C.M., Grillo E., Beemer F.A., Stoets L.M.E.,
RA   Wollnik B., Nuernberg P., Baas F.;
RT   "tRNA splicing endonuclease mutations cause pontocerebellar hypoplasia.";
RL   Nat. Genet. 40:1113-1118(2008).
CC   -!- FUNCTION: Constitutes one of the two catalytic subunit of the tRNA-
CC       splicing endonuclease complex, a complex responsible for identification
CC       and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at
CC       the 5'- and 3'-splice sites to release the intron. The products are an
CC       intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and
CC       5'-OH termini. There are no conserved sequences at the splice sites,
CC       but the intron is invariably located at the same site in the gene,
CC       placing the splice sites an invariant distance from the constant
CC       structural features of the tRNA body. Isoform 1 probably carries the
CC       active site for 5'-splice site cleavage. The tRNA splicing endonuclease
CC       is also involved in mRNA processing via its association with pre-mRNA
CC       3'-end processing factors, establishing a link between pre-tRNA
CC       splicing and pre-mRNA 3'-end formation, suggesting that the
CC       endonuclease subunits function in multiple RNA-processing events.
CC       Isoform 2 is responsible for processing a yet unknown RNA substrate.
CC       The complex containing isoform 2 is not able to cleave pre-tRNAs
CC       properly, although it retains endonucleolytic activity.
CC       {ECO:0000269|PubMed:15109492}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-
CC         half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with
CC         a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.; EC=4.6.1.16;
CC   -!- SUBUNIT: tRNA splicing endonuclease is a heterotetramer composed of
CC       isoform 1 of TSEN2, TSEN15, TSEN34/LENG5 and TSEN54. tRNA splicing
CC       endonuclease complex also contains proteins of the pre-mRNA 3'-end
CC       processing machinery such as CLP1, CPSF1, CPSF4 and CSTF2. Isoform 2
CC       belongs to a different complex that contains TSEN54 but low level of
CC       TSEN15 and TSEN34/LENG5.
CC   -!- INTERACTION:
CC       Q8NCE0; A2RRN7: CADPS; NbExp=3; IntAct=EBI-2559818, EBI-10179719;
CC       Q8NCE0; O75638-2: CTAG2; NbExp=3; IntAct=EBI-2559818, EBI-12265122;
CC       Q8NCE0; Q8TAK5: GABPB2; NbExp=3; IntAct=EBI-2559818, EBI-8468945;
CC       Q8NCE0; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-2559818, EBI-529518;
CC       Q8NCE0; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-2559818, EBI-11139477;
CC       Q8NCE0; Q7Z6J9: TSEN54; NbExp=11; IntAct=EBI-2559818, EBI-2559824;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15109492}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:15109492}. Note=May be transiently
CC       localized in the nucleolus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8NCE0-1; Sequence=Displayed;
CC       Name=2; Synonyms=SEN2deltaEx8, DeltaEx8;
CC         IsoId=Q8NCE0-2; Sequence=VSP_010986;
CC       Name=3;
CC         IsoId=Q8NCE0-3; Sequence=VSP_010985;
CC       Name=4;
CC         IsoId=Q8NCE0-4; Sequence=VSP_046192;
CC       Name=5;
CC         IsoId=Q8NCE0-5; Sequence=VSP_046193, VSP_046194;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are widely expressed at
CC       very low level. {ECO:0000269|PubMed:15109492}.
CC   -!- DISEASE: Pontocerebellar hypoplasia 2B (PCH2B) [MIM:612389]: A disorder
CC       characterized by an abnormally small cerebellum and brainstem, and
CC       progressive microcephaly from birth combined with extrapyramidal
CC       dyskinesia. Severe chorea occurs and epilepsy is frequent. There are no
CC       signs of spinal cord anterior horn cells degeneration.
CC       {ECO:0000269|PubMed:18711368}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; AK074794; BAC11213.1; -; mRNA.
DR   EMBL; AK300449; BAH13287.1; -; mRNA.
DR   EMBL; AK225875; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC018500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471055; EAW64129.1; -; Genomic_DNA.
DR   EMBL; BC004178; AAH04178.1; -; mRNA.
DR   EMBL; BC004211; AAH04211.1; -; mRNA.
DR   EMBL; BC019582; AAH19582.1; -; mRNA.
DR   EMBL; BC021975; AAH21975.2; -; mRNA.
DR   CCDS; CCDS2611.1; -. [Q8NCE0-1]
DR   CCDS; CCDS46757.1; -. [Q8NCE0-3]
DR   CCDS; CCDS46758.1; -. [Q8NCE0-4]
DR   RefSeq; NP_001138864.1; NM_001145392.1. [Q8NCE0-1]
DR   RefSeq; NP_001138865.1; NM_001145393.2. [Q8NCE0-3]
DR   RefSeq; NP_001138866.1; NM_001145394.1. [Q8NCE0-4]
DR   RefSeq; NP_001308206.1; NM_001321277.1. [Q8NCE0-1]
DR   RefSeq; NP_001308207.1; NM_001321278.1.
DR   RefSeq; NP_001308208.1; NM_001321279.1. [Q8NCE0-3]
DR   RefSeq; NP_079541.1; NM_025265.3. [Q8NCE0-1]
DR   RefSeq; XP_016862785.1; XM_017007296.1. [Q8NCE0-1]
DR   AlphaFoldDB; Q8NCE0; -.
DR   SMR; Q8NCE0; -.
DR   BioGRID; 123288; 85.
DR   CORUM; Q8NCE0; -.
DR   IntAct; Q8NCE0; 20.
DR   STRING; 9606.ENSP00000284995; -.
DR   iPTMnet; Q8NCE0; -.
DR   PhosphoSitePlus; Q8NCE0; -.
DR   BioMuta; TSEN2; -.
DR   DMDM; 50428914; -.
DR   EPD; Q8NCE0; -.
DR   jPOST; Q8NCE0; -.
DR   MassIVE; Q8NCE0; -.
DR   MaxQB; Q8NCE0; -.
DR   PaxDb; Q8NCE0; -.
DR   PeptideAtlas; Q8NCE0; -.
DR   PRIDE; Q8NCE0; -.
DR   ProteomicsDB; 34009; -.
DR   ProteomicsDB; 72878; -. [Q8NCE0-1]
DR   ProteomicsDB; 72879; -. [Q8NCE0-2]
DR   ProteomicsDB; 72880; -. [Q8NCE0-3]
DR   ProteomicsDB; 7810; -.
DR   Antibodypedia; 26210; 203 antibodies from 25 providers.
DR   DNASU; 80746; -.
DR   Ensembl; ENST00000284995.11; ENSP00000284995.6; ENSG00000154743.19. [Q8NCE0-1]
DR   Ensembl; ENST00000402228.7; ENSP00000385976.3; ENSG00000154743.19. [Q8NCE0-1]
DR   Ensembl; ENST00000415684.6; ENSP00000416510.1; ENSG00000154743.19. [Q8NCE0-3]
DR   Ensembl; ENST00000454502.6; ENSP00000392029.2; ENSG00000154743.19. [Q8NCE0-4]
DR   Ensembl; ENST00000679425.1; ENSP00000505890.1; ENSG00000154743.19. [Q8NCE0-1]
DR   Ensembl; ENST00000679670.1; ENSP00000506080.1; ENSG00000154743.19. [Q8NCE0-3]
DR   Ensembl; ENST00000679699.1; ENSP00000505274.1; ENSG00000154743.19. [Q8NCE0-1]
DR   Ensembl; ENST00000679756.1; ENSP00000506391.1; ENSG00000154743.19. [Q8NCE0-2]
DR   Ensembl; ENST00000680598.1; ENSP00000506297.1; ENSG00000154743.19. [Q8NCE0-2]
DR   Ensembl; ENST00000680943.1; ENSP00000505442.1; ENSG00000154743.19. [Q8NCE0-2]
DR   Ensembl; ENST00000680986.1; ENSP00000505799.1; ENSG00000154743.19. [Q8NCE0-1]
DR   Ensembl; ENST00000681140.1; ENSP00000505099.1; ENSG00000154743.19. [Q8NCE0-1]
DR   Ensembl; ENST00000681471.1; ENSP00000505105.1; ENSG00000154743.19. [Q8NCE0-3]
DR   Ensembl; ENST00000681482.1; ENSP00000505436.1; ENSG00000154743.19. [Q8NCE0-1]
DR   Ensembl; ENST00000681676.1; ENSP00000506163.1; ENSG00000154743.19. [Q8NCE0-3]
DR   GeneID; 80746; -.
DR   KEGG; hsa:80746; -.
DR   MANE-Select; ENST00000284995.11; ENSP00000284995.6; NM_025265.4; NP_079541.1.
DR   UCSC; uc003bwz.4; human. [Q8NCE0-1]
DR   CTD; 80746; -.
DR   DisGeNET; 80746; -.
DR   GeneCards; TSEN2; -.
DR   HGNC; HGNC:28422; TSEN2.
DR   HPA; ENSG00000154743; Low tissue specificity.
DR   MalaCards; TSEN2; -.
DR   MIM; 608753; gene.
DR   MIM; 612389; phenotype.
DR   neXtProt; NX_Q8NCE0; -.
DR   OpenTargets; ENSG00000154743; -.
DR   Orphanet; 2524; Pontocerebellar hypoplasia type 2.
DR   PharmGKB; PA142670695; -.
DR   VEuPathDB; HostDB:ENSG00000154743; -.
DR   eggNOG; KOG4685; Eukaryota.
DR   GeneTree; ENSGT00390000013266; -.
DR   HOGENOM; CLU_046429_1_0_1; -.
DR   InParanoid; Q8NCE0; -.
DR   OMA; TFEETFF; -.
DR   OrthoDB; 1219366at2759; -.
DR   PhylomeDB; Q8NCE0; -.
DR   TreeFam; TF314679; -.
DR   BioCyc; MetaCyc:HS08007-MON; -.
DR   BRENDA; 4.6.1.16; 2681.
DR   PathwayCommons; Q8NCE0; -.
DR   Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR   SignaLink; Q8NCE0; -.
DR   BioGRID-ORCS; 80746; 534 hits in 1084 CRISPR screens.
DR   ChiTaRS; TSEN2; human.
DR   GeneWiki; TSEN2; -.
DR   GenomeRNAi; 80746; -.
DR   Pharos; Q8NCE0; Tbio.
DR   PRO; PR:Q8NCE0; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q8NCE0; protein.
DR   Bgee; ENSG00000154743; Expressed in buccal mucosa cell and 143 other tissues.
DR   ExpressionAtlas; Q8NCE0; baseline and differential.
DR   Genevisible; Q8NCE0; HS.
DR   GO; GO:0005813; C:centrosome; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0000214; C:tRNA-intron endonuclease complex; IBA:GO_Central.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000213; F:tRNA-intron endonuclease activity; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IDA:UniProtKB.
DR   GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IBA:GO_Central.
DR   Gene3D; 3.40.1350.10; -; 1.
DR   InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR   InterPro; IPR036167; tRNA_intron_Endo_cat-like_sf.
DR   InterPro; IPR006677; tRNA_intron_Endonuc_cat-like.
DR   InterPro; IPR006678; tRNA_intron_Endonuc_N.
DR   InterPro; IPR006676; tRNA_splic.
DR   InterPro; IPR016589; tRNA_splic_SEN2.
DR   PANTHER; PTHR21227; PTHR21227; 1.
DR   Pfam; PF01974; tRNA_int_endo; 1.
DR   Pfam; PF02778; tRNA_int_endo_N; 1.
DR   PIRSF; PIRSF011789; tRNA_splic_SEN2; 1.
DR   SUPFAM; SSF53032; SSF53032; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Lyase; mRNA processing; Neurodegeneration; Nucleus;
KW   Phosphoprotein; Pontocerebellar hypoplasia; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..465
FT                   /note="tRNA-splicing endonuclease subunit Sen2"
FT                   /id="PRO_0000109452"
FT   REGION          157..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        369
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        377
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        416
FT                   /evidence="ECO:0000250"
FT   MOD_RES         408
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P7W5"
FT   MOD_RES         411
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P7W5"
FT   MOD_RES         415
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P7W5"
FT   VAR_SEQ         173..231
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_046192"
FT   VAR_SEQ         276..301
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046193"
FT   VAR_SEQ         278..303
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_010985"
FT   VAR_SEQ         304..320
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15109492"
FT                   /id="VSP_010986"
FT   VAR_SEQ         417..465
FT                   /note="ELMLCYLIKPSTMTDKEMESPECMKRIKVQEVILSRWVSSRERSDQDDL ->
FT                   VTQHQLCHWSVT (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046194"
FT   VARIANT         41
FT                   /note="R -> H (in dbSNP:rs12495784)"
FT                   /id="VAR_048931"
FT   VARIANT         126
FT                   /note="R -> H (in dbSNP:rs33955793)"
FT                   /id="VAR_048932"
FT   VARIANT         309
FT                   /note="Y -> C (in PCH2B; dbSNP:rs113994149)"
FT                   /evidence="ECO:0000269|PubMed:18711368"
FT                   /id="VAR_054810"
FT   CONFLICT        138
FT                   /note="H -> Q (in Ref. 2; BAH13287)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        208
FT                   /note="K -> E (in Ref. 2; BAH13287)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   465 AA;  53247 MW;  FF523229B05A1345 CRC64;
     MAEAVFHAPK RKRRVYETYE SPLPIPFGQD HGPLKEFKIF RAEMINNNVI VRNAEDIEQL
     YGKGYFGKGI LSRSRPSFTI SDPKLVAKWK DMKTNMPIIT SKRYQHSVEW AAELMRRQGQ
     DESTVRRILK DYTKPLEHPP VKRNEEAQVH DKLNSGMVSN MEGTAGGERP SVVNGDSGKS
     GGVGDPREPL GCLQEGSGCH PTTESFEKSV REDASPLPHV CCCKQDALIL QRGLHHEDGS
     QHIGLLHPGD RGPDHEYVLV EEAECAMSER EAAPNEELVQ RNRLICRRNP YRIFEYLQLS
     LEEAFFLVYA LGCLSIYYEK EPLTIVKLWK AFTVVQPTFR TTYMAYHYFR SKGWVPKVGL
     KYGTDLLLYR KGPPFYHASY SVIIELVDDH FEGSLRRPLS WKSLAALSRV SVNVSKELML
     CYLIKPSTMT DKEMESPECM KRIKVQEVIL SRWVSSRERS DQDDL
 
 
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