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UTP4_HUMAN
ID   UTP4_HUMAN              Reviewed;         686 AA.
AC   Q969X6; Q8NCD9; Q8TF14; Q96SP0; Q96SR9; Q96SZ9; Q96T13; Q9BWK6;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 185.
DE   RecName: Full=U3 small nucleolar RNA-associated protein 4 homolog;
DE   AltName: Full=Cirhin;
DE   AltName: Full=UTP4 small subunit processome component;
GN   Name=UTP4 {ECO:0000312|HGNC:HGNC:1983};
GN   Synonyms=CIRH1A, cPERP-E {ECO:0000303|PubMed:20813266}, KIAA1988;
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 3).
RC   TISSUE=Brain;
RX   PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA   Nagase T., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XXII. The
RT   complete sequences of 50 new cDNA clones which code for large proteins.";
RL   DNA Res. 8:319-327(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 95-686 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP   SCALE MRNA] OF 444-686 (ISOFORM 3).
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 1).
RC   TISSUE=Muscle, and Placenta;
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   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA   Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA   Greco A., Hochstrasser D.F., Diaz J.-J.;
RT   "Functional proteomic analysis of human nucleolus.";
RL   Mol. Biol. Cell 13:4100-4109(2002).
RN   [5]
RP   SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT TRP-565.
RX   PubMed=16225863; DOI=10.1016/j.yexcr.2005.08.012;
RA   Yu B., Mitchell G.A., Richter A.;
RT   "Nucleolar localization of cirhin, the protein mutated in North American
RT   Indian childhood cirrhosis.";
RL   Exp. Cell Res. 311:218-228(2005).
RN   [6]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=17699751; DOI=10.1101/gad.436707;
RA   Prieto J.L., McStay B.;
RT   "Recruitment of factors linking transcription and processing of pre-rRNA to
RT   NOR chromatin is UBF-dependent and occurs independent of transcription in
RT   human cells.";
RL   Genes Dev. 21:2041-2054(2007).
RN   [7]
RP   FUNCTION, INTERACTION WITH HIVEP1, AND CHARACTERIZATION OF VARIANT TRP-565.
RX   PubMed=19732766; DOI=10.1016/j.yexcr.2009.08.017;
RA   Yu B., Mitchell G.A., Richter A.;
RT   "Cirhin up-regulates a canonical NF-kappaB element through strong
RT   interaction with Cirip/HIVEP1.";
RL   Exp. Cell Res. 315:3086-3098(2009).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
RA   Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L.,
RA   Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T.,
RA   Earnshaw W.C., Rappsilber J.;
RT   "The protein composition of mitotic chromosomes determined using
RT   multiclassifier combinatorial proteomics.";
RL   Cell 142:810-821(2010).
RN   [9]
RP   FUNCTION, INTERACTION WITH NOL11, AND POSSIBLE ASSOCIATION IN THE SSU
RP   PROCESSOME T-UTP SUBCOMPLEX.
RX   PubMed=22916032; DOI=10.1371/journal.pgen.1002892;
RA   Freed E.F., Prieto J.L., McCann K.L., McStay B., Baserga S.J.;
RT   "NOL11, implicated in the pathogenesis of North American Indian childhood
RT   cirrhosis, is required for pre-rRNA transcription and processing.";
RL   PLoS Genet. 8:E1002892-E1002892(2012).
RN   [10]
RP   SUBCELLULAR LOCATION, INTERACTION WITH UTP15 AND WDR43, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RX   PubMed=24219289; DOI=10.1139/bcb-2013-0062;
RA   Sato M., Araki N., Kumeta M., Takeyasu K., Taguchi Y., Asai T.,
RA   Furukawa K., Horigome T.;
RT   "Interaction, mobility, and phosphorylation of human orthologues of WD
RT   repeat-containing components of the yeast SSU processome t-UTP sub-
RT   complex.";
RL   Biochem. Cell Biol. 91:466-475(2013).
RN   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-321, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [12]
RP   VARIANT TRP-565.
RX   PubMed=12417987; DOI=10.1086/344580;
RA   Chagnon P., Michaud J., Mitchell G., Mercier J., Marion J.-F., Drouin E.,
RA   Rasquin-Weber A., Hudson T.J., Richter A.;
RT   "A missense mutation (R565W) in cirhin (FLJ14728) in North American Indian
RT   childhood cirrhosis.";
RL   Am. J. Hum. Genet. 71:1443-1449(2002).
RN   [13]
RP   VARIANT TRP-565.
RX   PubMed=27535533; DOI=10.1038/nature19057;
RG   Exome Aggregation Consortium;
RA   Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
RA   O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
RA   Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
RA   Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
RA   Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
RA   Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
RA   Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
RA   Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
RA   Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
RA   Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA   Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
RA   McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
RA   Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
RA   Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
RA   Daly M.J., MacArthur D.G.;
RT   "Analysis of protein-coding genetic variation in 60,706 humans.";
RL   Nature 536:285-291(2016).
CC   -!- FUNCTION: Ribosome biogenesis factor. Involved in nucleolar processing
CC       of pre-18S ribosomal RNA. Involved in small subunit (SSU) pre-rRNA
CC       processing at sites A', A0, 1 and 2b. Required for optimal pre-
CC       ribosomal RNA transcription by RNA polymerase (PubMed:17699751,
CC       PubMed:19732766). May be a transcriptional regulator. Acts as a
CC       positive regulator of HIVEP1 which specifically binds to the DNA
CC       sequence 5'-GGGACTTTCC-3' found in enhancer elements of numerous viral
CC       promoters such as those of HIV-1, SV40, or CMV (PubMed:19732766).
CC       {ECO:0000269|PubMed:17699751, ECO:0000269|PubMed:19732766,
CC       ECO:0000269|PubMed:22916032}.
CC   -!- SUBUNIT: Interacts with HIVEP1 (PubMed:19732766) Interacts with NOL11
CC       (PubMed:22916032). Interacts directly with UTP15 and WDR43
CC       (PubMed:24219289). May be a component of the proposed t-UTP subcomplex
CC       of the ribosomal small subunit (SSU) processome containing at least
CC       UTP4, WDR43, HEATR1, UTP15, WDR75 (PubMed:17699751, PubMed:22916032).
CC       {ECO:0000269|PubMed:19732766, ECO:0000269|PubMed:22916032,
CC       ECO:0000269|PubMed:24219289, ECO:0000305|PubMed:17699751}.
CC   -!- INTERACTION:
CC       Q969X6; P15822: HIVEP1; NbExp=3; IntAct=EBI-2602591, EBI-722264;
CC       Q969X6; Q9H8H0: NOL11; NbExp=6; IntAct=EBI-2602591, EBI-725885;
CC       Q969X6; Q8TED0: UTP15; NbExp=3; IntAct=EBI-2602591, EBI-1048301;
CC       Q969X6; Q15061: WDR43; NbExp=3; IntAct=EBI-2602591, EBI-2563523;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC       ECO:0000269|PubMed:16225863, ECO:0000269|PubMed:24219289}. Chromosome
CC       {ECO:0000269|PubMed:20813266}. Note=Found predominantly at the
CC       fibrillar center. {ECO:0000269|PubMed:24219289}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q969X6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q969X6-2; Sequence=VSP_009201;
CC       Name=3;
CC         IsoId=Q969X6-3; Sequence=VSP_009202, VSP_009203;
CC   -!- PTM: May be phosphorylated during mitosis; may control the association
CC       of this protein with WRD43 and UTP15. {ECO:0000269|PubMed:24219289}.
CC   -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB55100.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB55116.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB55212.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB85574.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB075868; BAB85574.2; ALT_INIT; mRNA.
DR   EMBL; AK027419; BAB55100.1; ALT_INIT; mRNA.
DR   EMBL; AK027445; BAB55116.1; ALT_INIT; mRNA.
DR   EMBL; AK027584; BAB55212.1; ALT_INIT; mRNA.
DR   EMBL; AK027634; BAB55251.1; -; mRNA.
DR   EMBL; AK027675; BAB55287.1; -; mRNA.
DR   EMBL; AK074795; BAC11214.1; -; mRNA.
DR   EMBL; BC000167; AAH00167.1; -; mRNA.
DR   EMBL; BC009348; AAH09348.1; -; mRNA.
DR   CCDS; CCDS10872.1; -. [Q969X6-1]
DR   RefSeq; NP_116219.2; NM_032830.2. [Q969X6-1]
DR   PDB; 7MQ8; EM; 3.60 A; LN=1-686.
DR   PDB; 7MQ9; EM; 3.87 A; LN=1-686.
DR   PDB; 7MQA; EM; 2.70 A; LN=1-686.
DR   PDBsum; 7MQ8; -.
DR   PDBsum; 7MQ9; -.
DR   PDBsum; 7MQA; -.
DR   AlphaFoldDB; Q969X6; -.
DR   SMR; Q969X6; -.
DR   BioGRID; 124353; 166.
DR   IntAct; Q969X6; 36.
DR   MINT; Q969X6; -.
DR   STRING; 9606.ENSP00000327179; -.
DR   GlyGen; Q969X6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q969X6; -.
DR   PhosphoSitePlus; Q969X6; -.
DR   SwissPalm; Q969X6; -.
DR   BioMuta; UTP4; -.
DR   DMDM; 41016916; -.
DR   SWISS-2DPAGE; Q969X6; -.
DR   EPD; Q969X6; -.
DR   jPOST; Q969X6; -.
DR   MassIVE; Q969X6; -.
DR   MaxQB; Q969X6; -.
DR   PaxDb; Q969X6; -.
DR   PeptideAtlas; Q969X6; -.
DR   PRIDE; Q969X6; -.
DR   ProteomicsDB; 75873; -. [Q969X6-1]
DR   ProteomicsDB; 75874; -. [Q969X6-2]
DR   ProteomicsDB; 75875; -. [Q969X6-3]
DR   Antibodypedia; 29826; 123 antibodies from 21 providers.
DR   DNASU; 84916; -.
DR   Ensembl; ENST00000314423.12; ENSP00000327179.7; ENSG00000141076.18. [Q969X6-1]
DR   Ensembl; ENST00000352319.8; ENSP00000339164.4; ENSG00000141076.18. [Q969X6-2]
DR   Ensembl; ENST00000563094.5; ENSP00000456622.1; ENSG00000141076.18. [Q969X6-3]
DR   Ensembl; ENST00000575702.3; ENSP00000458843.2; ENSG00000262788.3.
DR   GeneID; 84916; -.
DR   KEGG; hsa:84916; -.
DR   MANE-Select; ENST00000314423.12; ENSP00000327179.7; NM_032830.3; NP_116219.2.
DR   UCSC; uc002ewr.3; human. [Q969X6-1]
DR   CTD; 84916; -.
DR   DisGeNET; 84916; -.
DR   GeneCards; UTP4; -.
DR   HGNC; HGNC:1983; UTP4.
DR   HPA; ENSG00000141076; Low tissue specificity.
DR   MalaCards; UTP4; -.
DR   MIM; 607456; gene.
DR   neXtProt; NX_Q969X6; -.
DR   OpenTargets; ENSG00000141076; -.
DR   Orphanet; 168583; Hereditary North American Indian childhood cirrhosis.
DR   PharmGKB; PA26520; -.
DR   VEuPathDB; HostDB:ENSG00000141076; -.
DR   eggNOG; KOG2048; Eukaryota.
DR   GeneTree; ENSGT00940000153533; -.
DR   HOGENOM; CLU_002392_3_0_1; -.
DR   InParanoid; Q969X6; -.
DR   OMA; PDANWIC; -.
DR   OrthoDB; 376282at2759; -.
DR   PhylomeDB; Q969X6; -.
DR   TreeFam; TF313159; -.
DR   PathwayCommons; Q969X6; -.
DR   Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR   Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   SignaLink; Q969X6; -.
DR   BioGRID-ORCS; 84916; 741 hits in 1073 CRISPR screens.
DR   ChiTaRS; UTP4; human.
DR   GeneWiki; CIRH1A; -.
DR   GenomeRNAi; 84916; -.
DR   Pharos; Q969X6; Tbio.
DR   PRO; PR:Q969X6; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q969X6; protein.
DR   Bgee; ENSG00000141076; Expressed in gastrocnemius and 102 other tissues.
DR   ExpressionAtlas; Q969X6; baseline and differential.
DR   Genevisible; Q969X6; HS.
DR   GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR   GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR   GO; GO:0001650; C:fibrillar center; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR   GO; GO:0034455; C:t-UTP complex; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IMP:UniProtKB.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 3.
DR   InterPro; IPR046351; UTP4.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR44163; PTHR44163; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 10.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromosome; Disease variant;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Ribosome biogenesis; rRNA processing; Transcription;
KW   Transcription regulation; Ubl conjugation; WD repeat.
FT   CHAIN           1..686
FT                   /note="U3 small nucleolar RNA-associated protein 4 homolog"
FT                   /id="PRO_0000050908"
FT   REPEAT          7..50
FT                   /note="WD 1"
FT   REPEAT          51..92
FT                   /note="WD 2"
FT   REPEAT          93..135
FT                   /note="WD 3"
FT   REPEAT          136..181
FT                   /note="WD 4"
FT   REPEAT          182..226
FT                   /note="WD 5"
FT   REPEAT          227..275
FT                   /note="WD 6"
FT   REPEAT          276..317
FT                   /note="WD 7"
FT   REPEAT          318..377
FT                   /note="WD 8"
FT   REPEAT          378..427
FT                   /note="WD 9"
FT   REPEAT          428..475
FT                   /note="WD 10"
FT   REPEAT          476..516
FT                   /note="WD 11"
FT   REPEAT          517..566
FT                   /note="WD 12"
FT   REPEAT          567..627
FT                   /note="WD 13"
FT   REPEAT          628..666
FT                   /note="WD 14"
FT   CROSSLNK        321
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         368..482
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_009201"
FT   VAR_SEQ         612..625
FT                   /note="PLPNDKTLLYNPFP -> VSSSLLPPKSSSES (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11853319,
FT                   ECO:0000303|PubMed:14702039"
FT                   /id="VSP_009202"
FT   VAR_SEQ         626..686
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11853319,
FT                   ECO:0000303|PubMed:14702039"
FT                   /id="VSP_009203"
FT   VARIANT         438
FT                   /note="R -> H (in dbSNP:rs8056684)"
FT                   /id="VAR_053388"
FT   VARIANT         565
FT                   /note="R -> W (found in patients with North American Indian
FT                   childhood cirrhosis; unknown pathological significance;
FT                   does not affect nucleolar protein location; decreased
FT                   interaction with HIVEP1 measured in yeast two-hybrid
FT                   screening; dbSNP:rs119465999)"
FT                   /evidence="ECO:0000269|PubMed:12417987,
FT                   ECO:0000269|PubMed:16225863, ECO:0000269|PubMed:19732766"
FT                   /id="VAR_017445"
FT   CONFLICT        101
FT                   /note="G -> V (in Ref. 2; BAB55116)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        290
FT                   /note="V -> M (in Ref. 2; BAB55251)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378
FT                   /note="N -> S (in Ref. 2; BAB55100)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        419
FT                   /note="N -> S (in Ref. 2; BAC11214)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        594
FT                   /note="M -> V (in Ref. 2; BAB55100)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        624
FT                   /note="F -> L (in Ref. 2; BAC11214)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   686 AA;  76890 MW;  595D8B2F47C03299 CRC64;
     MGEFKVHRVR FFNYVPSGIR CVAYNNQSNR LAVSRTDGTV EIYNLSANYF QEKFFPGHES
     RATEALCWAE GQRLFSAGLN GEIMEYDLQA LNIKYAMDAF GGPIWSMAAS PSGSQLLVGC
     EDGSVKLFQI TPDKIQFERN FDRQKSRILS LSWHPSGTHI AAGSIDYISV FDVKSGSAVH
     KMIVDRQYMG VSKRKCIVWG VAFLSDGTII SVDSAGKVQF WDSATGTLVK SHLIANADVQ
     SIAVADQEDS FVVGTAEGTV FHFQLVPVTS NSSEKQWVRT KPFQHHTHDV RTVAHSPTAL
     ISGGTDTHLV FRPLMEKVEV KNYDAALRKI TFPHRCLISC SKKRQLLLFQ FAHHLELWRL
     GSTVATGKNG DTLPLSKNAD HLLHLKTKGP ENIICSCISP CGSWIAYSTV SRFFLYRLNY
     EHDNISLKRV SKMPAFLRSA LQILFSEDST KLFVASNQGA LHIVQLSGGS FKHLHAFQPQ
     SGTVEAMCLL AVSPDGNWLA ASGTSAGVHV YNVKQLKLHC TVPAYNFPVT AMAIAPNTNN
     LVIAHSDQQV FEYSIPDKQY TDWSRTVQKQ GFHHLWLQRD TPITHISFHP KRPMHILLHD
     AYMFCIIDKS LPLPNDKTLL YNPFPPTNES DVIRRRTAHA FKISKIYKPL LFMDLLDERT
     LVAVERPLDD IIAQLPPPIK KKKFGT
 
 
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