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CUL9_MOUSE
ID   CUL9_MOUSE              Reviewed;        1865 AA.
AC   Q80TT8; Q8BKL9; Q8CGC0; Q8R363;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Cullin-9;
DE            Short=CUL-9;
DE   AltName: Full=p53-associated parkin-like cytoplasmic protein;
GN   Name=Cul9; Synonyms=Kiaa0708, Parc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   TISSUE=Brain, and Mammary tumor;
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 102-1865 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15964813; DOI=10.1128/mcb.25.13.5579-5589.2005;
RA   Skaar J.R., Arai T., DeCaprio J.A.;
RT   "Dimerization of CUL7 and PARC is not required for all CUL7 functions and
RT   mouse development.";
RL   Mol. Cell. Biol. 25:5579-5589(2005).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=21487039; DOI=10.1158/0008-5472.can-10-4300;
RA   Pei X.H., Bai F., Li Z., Smith M.D., Whitewolf G., Jin R., Xiong Y.;
RT   "Cytoplasmic CUL9/PARC ubiquitin ligase is a tumor suppressor and promotes
RT   p53-dependent apoptosis.";
RL   Cancer Res. 71:2969-2977(2011).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH RBX1 AND CUL7.
RX   PubMed=24793696; DOI=10.1016/j.molcel.2014.03.046;
RA   Li Z., Pei X.H., Yan J., Yan F., Cappell K.M., Whitehurst A.W., Xiong Y.;
RT   "CUL9 mediates the functions of the 3M complex and ubiquitylates survivin
RT   to maintain genome integrity.";
RL   Mol. Cell 54:805-819(2014).
CC   -!- FUNCTION: Core component of a Cul9-RING ubiquitin-protein ligase
CC       complex, a complex that mediates ubiquitination and subsequent
CC       degradation of BIRC5 and is required to maintain microtubule dynamics
CC       and genome integrity. Acts downstream of the 3M complex, which inhibits
CC       CUL9 activity, leading to prevent ubiquitination of BIRC5
CC       (PubMed:24793696). Cytoplasmic anchor protein in p53/TP53-associated
CC       protein complex. Regulates the subcellular localization of p53/TP53 and
CC       subsequent function. {ECO:0000269|PubMed:24793696}.
CC   -!- SUBUNIT: Part of a Cul9-RING complex at least composed of CUL9 and
CC       RBX1. Interacts with CUL7: interaction with CUL7 component of the 3M
CC       complex leads to inhibition of CUL9 activity. The CUL7-CUL9 heterodimer
CC       seems to interact specifically with TP53. Forms a complex with p53/TP53
CC       in the cytoplasm of unstressed cells. Interacts with UBCH7 and UBCH8
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21487039}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q80TT8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TT8-2; Sequence=VSP_009576;
CC       Name=3;
CC         IsoId=Q80TT8-3; Sequence=VSP_009577, VSP_009578;
CC       Name=4;
CC         IsoId=Q80TT8-4; Sequence=VSP_009579, VSP_009580;
CC   -!- DOMAIN: The IBR domain is required for interaction with UBCH7 and
CC       UBCH8.
CC   -!- DISRUPTION PHENOTYPE: Mice were born at the expected Mendelian ratio
CC       and do not show apparent phenotype. They are however more susceptible
CC       to carcinogenesis and develop spontaneous tumor. Cells display
CC       polyploidy and aneuploidy. {ECO:0000269|PubMed:15964813,
CC       ECO:0000269|PubMed:21487039, ECO:0000269|PubMed:24793696}.
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00330}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK051474; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK051474; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC026469; AAH26469.1; -; mRNA.
DR   EMBL; BC041674; AAH41674.1; -; mRNA.
DR   EMBL; AK122351; BAC65633.1; -; Transcribed_RNA.
DR   AlphaFoldDB; Q80TT8; -.
DR   SMR; Q80TT8; -.
DR   STRING; 10090.ENSMUSP00000138418; -.
DR   MaxQB; Q80TT8; -.
DR   PaxDb; Q80TT8; -.
DR   PeptideAtlas; Q80TT8; -.
DR   PRIDE; Q80TT8; -.
DR   ProteomicsDB; 279298; -. [Q80TT8-1]
DR   ProteomicsDB; 279299; -. [Q80TT8-2]
DR   ProteomicsDB; 279300; -. [Q80TT8-3]
DR   ProteomicsDB; 279301; -. [Q80TT8-4]
DR   UCSC; uc008ctb.2; mouse. [Q80TT8-1]
DR   UCSC; uc008ctf.2; mouse. [Q80TT8-3]
DR   MGI; MGI:1925559; Cul9.
DR   eggNOG; KOG1815; Eukaryota.
DR   InParanoid; Q80TT8; -.
DR   PhylomeDB; Q80TT8; -.
DR   Reactome; R-MMU-8951664; Neddylation.
DR   ChiTaRS; Cul9; mouse.
DR   PRO; PR:Q80TT8; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q80TT8; protein.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR004939; APC_su10/DOC_dom.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR031222; CUL9.
DR   InterPro; IPR016157; Cullin_CS.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR036317; Cullin_homology_sf.
DR   InterPro; IPR019559; Cullin_neddylation_domain.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR22771:SF2; PTHR22771:SF2; 1.
DR   Pfam; PF03256; ANAPC10; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM01337; APC10; 1.
DR   SMART; SM00884; Cullin_Nedd8; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF75632; SSF75632; 1.
DR   PROSITE; PS01256; CULLIN_1; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
DR   PROSITE; PS51284; DOC; 1.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..1865
FT                   /note="Cullin-9"
FT                   /id="PRO_0000119816"
FT   DOMAIN          480..659
FT                   /note="DOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT   ZN_FING         1409..1459
FT                   /note="RING-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ZN_FING         1479..1542
FT                   /note="IBR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ZN_FING         1575..1604
FT                   /note="RING-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   REGION          265..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1002..1025
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1405..1622
FT                   /note="TRIAD supradomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   REGION          1778..1865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1794..1835
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        272..286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..795
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1002..1018
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1778..1797
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1798..1841
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1588
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         700..707
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         1409
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1412
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1427
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1429
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1432
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1435
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1454
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1459
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1499
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1505
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1520
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1523
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1528
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1531
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1537
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1542
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1575
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1578
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1593
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1596
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1601
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1604
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1612
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         1618
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   MOD_RES         313
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWT3"
FT   MOD_RES         794
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWT3"
FT   MOD_RES         1775
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWT3"
FT   VAR_SEQ         1..908
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_009576"
FT   VAR_SEQ         134..144
FT                   /note="ALKMLAIANSS -> VSTLGRAGQSD (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_009577"
FT   VAR_SEQ         145..1865
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_009578"
FT   VAR_SEQ         944..1009
FT                   /note="LLSLGSSWLEGAVLEQIGPCFPNRLPQLMLQSLHTSEELQHRFHLFQLQQLD
FT                   RQLLEQGDQEEWRP -> RLEENSLQTQDQPFPSWSCHRAAGRSPHCAICTTPESTYRR
FT                   SSAMPWSASPASTATVRSWGQEAGA (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_009579"
FT   VAR_SEQ         1010..1865
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_009580"
FT   CONFLICT        1102
FT                   /note="L -> F (in Ref. 1; AK051474)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1104..1119
FT                   /note="Missing (in Ref. 3; BAC65633)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1111..1119
FT                   /note="LNTVQMWLL -> TVQMWLLLN (in Ref. 1; AK051474)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1183
FT                   /note="F -> V (in Ref. 1; AK051474)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1592
FT                   /note="T -> N (in Ref. 1; AK051474)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1865 AA;  209160 MW;  9956A32BE5BC5803 CRC64;
     MARALRGPGP RSSLDQHVAA VLATVQISSL DTNLQLSGLC ALSQAVEEVT ERDHPLVRPD
     RPLREKLVKT LVDLLTNQVG EKMVVVMALR LLYLLMTKHE WRPLFAREGG IYAVLICMQE
     YKTSVLVQQA GLAALKMLAI ANSSDVPTFI PSRDSIQPLF DTQMTREIFA SIDSATRPGS
     ESLLLSVPAA VVLMLNTEGC SSAVRNGLLL LNLLLCNHHT LGDQIITQEL RDTLFRHSGI
     APGTEPMPTT RTILTMLLSR YSEPRGSPER AVLETPSTQG QDGSPESLIR SLVGDLSAEL
     FLDLERVLCH EGSPPAAVRP LLRRLQQETQ PFLLLLRTLD APGPNRTLLL TILRVMTRLL
     DHPETMVLPW HEVLEPCLNC LNGPSSDSEV VQEVTCFLHR LALMQKDYAV VLCCLGGKEA
     LSKVLDKHST QLLLASELRH LVAECEKYSQ LCSNLTSSIL AGCIQMVLGQ IEDHRRTYKP
     ITIPFFDVFL RHLCQGSSVE VKEDRCWEKV EVSSNPHRAS KLTDRNPKTY WESNGSTGSH
     SITLHMHRGV LIRQLTLLVA SEDSSYMPAR VVVFGGDNVG CISTELNTVN VMPSASRVTL
     LENLTRFWPI IQIRIKRCQQ GGIDTRVRGV EVLGPKPTFW PLFREQLCRR TCLFYTIRAQ
     AWSRDIAEDR QRLLQLYPRL NRVLRHEQNF ADRFLPDDEA AQALGKTCWE ALVSPLVQNI
     TSPDAGGVSS LGWLLDQYLE HRESTRSRQG PAASFASQVR RLCHLLVHVE APPGPSPEPS
     SQPLSKNSKG QDGSPTPAPT PVCPSTSLRN LTQCWLSVVQ GQVSRFLAAA WRASDFVPRY
     CSLYQRLQSA GSELFGPRAA FTLALRSGFS GALLQQSFLT AAHISEQFAR HIDQQIHGGL
     LGGAAGVGML GRLQRHLEPI MVLSGLELAT TFEHFYQHYM ADRLLSLGSS WLEGAVLEQI
     GPCFPNRLPQ LMLQSLHTSE ELQHRFHLFQ LQQLDRQLLE QGDQEEWRPE KVEEDDEGQE
     TGRELFTDPG PAISVLVLSP RCWPVSPLCY LHHPRKHLQA ELCDALERFS SFYSHSQNCP
     VLDIGPHRRL QWTWLGRAEL QLGDQTLHVS LNTVQMWLLF NQSEEVSVET LLRNSDLSPE
     LLHQALLPLT SDNGPLTLEE TQDYPQGGVL RLREPRSQTH EEFLWLIPPQ TYLSVEKDEG
     RTLEQKRNLL SCLLVRILKA HREKGLHIDQ LVCLVLEAWQ KGPDPPGRLG NAAAVGVACS
     STDVLSCILH LLGQGYVERR DDRPQVLMYA TPEPMGPCRG QADVPFCGNK NTETSRPSPE
     AVVALASLQL PAGRTMSPQE VEGLMEQTVR QVQETLNLEP DVAQHLLAHS HWGTEQLLQS
     YSDDPEPLLL AAGLRVPQAQ VVPTRPDQCP VCVTPLGPHD DSPSLCCLHC CCKSCWNEYL
     TTRIEQNFVL NCTCPIADCP AQPTGAFIRN IVSSPEVISK YEKALLRGYV ESCSNLTWCT
     NPQGCDRILC RQGLGSGTTC SKCGWASCFS CSFPEAHYPA SCGHMSQWVD DGGYYDGMSV
     EAQSKHLAKL ISKRCPSCQA PIEKNEGCLH MTCARCNHGF CWRCLKSWKP SHKDYYNCSA
     MVSKAARQEK RFQDYNERCT FHHQAREFAV NLRNQASAIQ EVPPPKSFTF LQDACRALEQ
     ARKVLAYACV YSFYSQDTEY MDVVEQQTEN LELHTNALQI LLEETLLRCR DLASSLRFLR
     ADCLSTGTEL LRRIQERLLA ILQHSTQDFR VGLQSPSVET REVKGSNVPS DQPQGSSGLE
     VEDEEEEEEE EEEEEEEEEE DVPEWQHEFD EELDNDSFSY DEESENLDRE TFFFGDEDED
     DESYD
 
 
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