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OBSL1_MOUSE
ID   OBSL1_MOUSE             Reviewed;        1804 AA.
AC   D3YYU8; F7AD47; Q80WA6;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Obscurin-like protein 1;
GN   Name=Obsl1;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Limb;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, and Pancreas;
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).
CC   -!- FUNCTION: Core component of the 3M complex, a complex required to
CC       regulate microtubule dynamics and genome integrity. It is unclear how
CC       the 3M complex regulates microtubules, it could act by controlling the
CC       level of a microtubule stabilizer. Acts as a regulator of the Cul7-
CC       RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the
CC       ubiquitin ligase pathway that regulates Golgi morphogenesis and
CC       dendrite patterning in brain. Required to localize CUL7 to the Golgi
CC       apparatus in neurons (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the 3M complex, composed of core components CUL7,
CC       CCDC8 and OBSL1. Interacts with CCDC8. Interacts with CUL7; the
CC       interaction is direct. Interacts with FBXW8. Interacts (via N-terminal
CC       Ig-like domain) with TTN/titin (via C-terminal Ig-like domain); the
CC       interaction is direct (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75147}.
CC       Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75147}. Golgi
CC       apparatus {ECO:0000250|UniProtKB:O75147}. Note=Colocalizes with CUL7 at
CC       the Golgi apparatus in neurons. {ECO:0000250|UniProtKB:O75147}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=D3YYU8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=D3YYU8-2; Sequence=VSP_055905, VSP_055906, VSP_055907;
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DR   EMBL; AC115011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC051643; AAH51643.1; -; mRNA.
DR   CCDS; CCDS15077.2; -. [D3YYU8-1]
DR   RefSeq; NP_849215.3; NM_178884.5.
DR   AlphaFoldDB; D3YYU8; -.
DR   SMR; D3YYU8; -.
DR   BioGRID; 221115; 2.
DR   STRING; 10090.ENSMUSP00000109197; -.
DR   iPTMnet; D3YYU8; -.
DR   PhosphoSitePlus; D3YYU8; -.
DR   MaxQB; D3YYU8; -.
DR   PaxDb; D3YYU8; -.
DR   PeptideAtlas; D3YYU8; -.
DR   PRIDE; D3YYU8; -.
DR   ProteomicsDB; 294060; -. [D3YYU8-1]
DR   ProteomicsDB; 294061; -. [D3YYU8-2]
DR   Antibodypedia; 52509; 16 antibodies from 7 providers.
DR   DNASU; 98733; -.
DR   GeneID; 98733; -.
DR   KEGG; mmu:98733; -.
DR   UCSC; uc007bpn.2; mouse. [D3YYU8-1]
DR   UCSC; uc007bpp.3; mouse. [D3YYU8-2]
DR   CTD; 23363; -.
DR   MGI; MGI:2138628; Obsl1.
DR   VEuPathDB; HostDB:ENSMUSG00000026211; -.
DR   eggNOG; KOG0613; Eukaryota.
DR   HOGENOM; CLU_000630_0_0_1; -.
DR   InParanoid; D3YYU8; -.
DR   OrthoDB; 15947at2759; -.
DR   PhylomeDB; D3YYU8; -.
DR   Reactome; R-MMU-8951664; Neddylation.
DR   BioGRID-ORCS; 98733; 0 hits in 72 CRISPR screens.
DR   ChiTaRS; Obsl1; mouse.
DR   PRO; PR:D3YYU8; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; D3YYU8; protein.
DR   ExpressionAtlas; D3YYU8; baseline and differential.
DR   Genevisible; D3YYU8; MM.
DR   GO; GO:1990393; C:3M complex; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR   GO; GO:0034067; P:protein localization to Golgi apparatus; ISO:MGI.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
DR   GO; GO:0010842; P:retina layer formation; IBA:GO_Central.
DR   GO; GO:0007416; P:synapse assembly; IBA:GO_Central.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 19.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF07679; I-set; 13.
DR   SMART; SM00409; IG; 17.
DR   SMART; SM00408; IGc2; 14.
DR   SUPFAM; SSF48726; SSF48726; 17.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 13.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Disulfide bond; Golgi apparatus;
KW   Immunoglobulin domain; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..1804
FT                   /note="Obscurin-like protein 1"
FT                   /id="PRO_0000430250"
FT   DOMAIN          12..100
FT                   /note="Ig-like 1"
FT   DOMAIN          128..225
FT                   /note="Ig-like 2"
FT   DOMAIN          241..330
FT                   /note="Ig-like 3"
FT   DOMAIN          339..425
FT                   /note="Ig-like 4"
FT   DOMAIN          517..615
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          720..800
FT                   /note="Ig-like 5"
FT   DOMAIN          804..891
FT                   /note="Ig-like 6"
FT   DOMAIN          902..982
FT                   /note="Ig-like 7"
FT   DOMAIN          986..1075
FT                   /note="Ig-like 8"
FT   DOMAIN          1078..1165
FT                   /note="Ig-like 9"
FT   DOMAIN          1176..1261
FT                   /note="Ig-like 10"
FT   DOMAIN          1266..1442
FT                   /note="Ig-like 11"
FT   DOMAIN          1536..1621
FT                   /note="Ig-like 12"
FT   DOMAIN          1625..1694
FT                   /note="Ig-like 13"
FT   DOMAIN          1702..1798
FT                   /note="Ig-like 14"
FT   REGION          17..19
FT                   /note="Interaction with TTN"
FT                   /evidence="ECO:0000250"
FT   REGION          85..94
FT                   /note="Interaction with TTN"
FT                   /evidence="ECO:0000250"
FT   REGION          227..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75147"
FT   DISULFID        33..84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        149..209
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        267..319
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        362..412
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        738..788
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        829..879
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        920..970
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        1011..1061
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        1103..1153
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        1195..1245
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        1289..1430
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        1558..1608
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         1..478
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055905"
FT   VAR_SEQ         985..1004
FT                   /note="EPPVRIIYPQDEVTLHAVSL -> GVGLSQPPESPEDNPEPQEC (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055906"
FT   VAR_SEQ         1005..1804
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055907"
FT   CONFLICT        786
FT                   /note="F -> I (in Ref. 2; AAH51643)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        858
FT                   /note="K -> E (in Ref. 2; AAH51643)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1804 AA;  197937 MW;  FDD14572E8FC10B2 CRC64;
     MKAGSGDQGS PPCFLRFPRP VRVVSGAEAE LKCVVLGEPP PTVVWEKGGQ QLVASERLSF
     PEDGAEHGLL LSGALPTDAG VYVCRARNAA GEAYAAAAVT VLEPPAPEPE PESSECPLPT
     PGTGEGAPKF LTGPQSQWVL RGEEVVLTCQ VGGLPEPKLY WEKDGMALDE VWDSSHFKLE
     PGRGASDEGA SLTLRILAAR LPDSGVYVCH ARNAHGHAQA GALLQVHQPR ESPPQDPDEN
     PKPVLEPLKG APKTFWVNEG KHAKFRCYVM GKPEPEIEWH LEGRPLLPDR RRLMYRDRDG
     GFVLKVLYCQ AKDRGLYVCA ARNSAGQTLS AVQLHVKEPR LRFTRPLQDV EGREHGIVVL
     ECKVPNSRIP TAWFREDQRL LPCRKYEQIE EGAVRRLVIH KLKADDDGVY LCEMRGRVRT
     VANVTVKGPI LKRLPRKLDV LEGENAVLLV ETQEAGVQGC WSRDGEDLPD TCQSSCGHMH
     ALVLPGVTRE DAGEITFSLG NSRTTTLLRV KCVKHSPPGP PVMVEMFKGQ KNKVLLTWKP
     PEPPPETSFI YRLERQEVGS DDWIQCFSIE KAGAVEVPGD CVPTEGDYHF RICTVSEHGR
     SPHVVFNGSA HLVPTARLVS GLEDVQVYDG EDAVFSLDLS AIIQGSWFLN GEQLQSNEPE
     GQVEPGALRY RIEQKGLQHR LILQAVKHRD SGALVGFSCP GVQDSAALTI QESSVHILSP
     QDKVSLTFTT SERVVLTCEL SRVDFPATWY KDGQKVEESE SLIVKTEGRK HRLILPEAQV
     RDSGEFECRT EGVSAFFGVT VQDPPVHIVN PQEHVFVHAI TSECVRLTCE VDREDTTVHW
     YKDGQEVEES DIIVLENKGP HHRLVLPAAR PSDGGEFQCV AGDERAYFTV TITDVFSWIV
     YPSSEVHVAA VRLERVVLTC ELCRPWAEVR WTKDGEEVVE SPALLLEKED TIRRLVLPSV
     QLEDSGEYLC EIHDESASFT ITVTEPPVRI IYPQDEVTLH AVSLECVVLT CELSREDAPV
     RWYKDGLEVE ESEALVLQSD GPRRRLVLPA AQPEDGGEFV CDAGDDSAFF TVTVTAPPER
     IVHPAARSLD LQFGAPGHVE LRCEVAPAGS QVRWYKDGLE VEVSDALQLG AEGPARTLTL
     PHAQPEDAGE YVCETRDEAV TFNVSLAELP VQFLAPEAAP NPLCVVPGEP VVLSCELSRA
     SAQVFWSHNG SPVQQGEGLE LRAEGPRRIL CIQAADLAHT GVYTCQSGAS PGAPSLSFNV
     QVAELPPVKL VSELTPLTVH EGDDATFQCE VSPPDAEVTW LRNGAVITAG PQLEMVQNGS
     SRTLIIRGCQ LKDAGTVTAR AGAADTSARL HVRETELLFL RRLQDVRAEE GQDVHLEVET
     GRVGAAGTVR WIRGGEPLPL DSRLTTAQDG HVHRLSIHGV LLTDQGTYGC ESRHDRTLAR
     LSVRPRQLRE LRPLEDVTVH EGGSATFQLE LSQEGVTGEW AQGGVRLHPG PKCHIQSEGR
     THRLVLSGLG LADSGCVSFT ADTLRCAARL TVREVPVTIV QGPQDLEVTE GDTATFECEL
     SQTLADVIWE KDGQALSLSP RLRLQALGTR RLLLLRRCCS SDAGTYSCVV GTARSEPARL
     TVREREVSVL RELRSVSARE GDGATFECTV SETEITGRWE LGGRALRPGG RVRIRQEGKK
     HILVLSELRT EDTGEVCFQA GPAQSLARLE VEALPLQMCR RPPREKTVLV NRRAVLEVTV
     SRPGGHVCWM REGVELCPGN KYETRRHGTT HSLVIHDVRP EDQGTYSCQA GQDSADTQLL
     VDGD
 
 
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