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SHKB1_RAT
ID   SHKB1_RAT               Reviewed;         704 AA.
AC   P0C5J9;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=SH3KBP1-binding protein 1;
DE   AltName: Full=SETA-binding protein 1;
GN   Name=Shkbp1; Synonyms=Sb1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   INTERACTION WITH SH3KBP1.
RX   PubMed=11152963; DOI=10.1016/s0898-6568(00)00129-7;
RA   Borinstein S.C., Hyatt M.A., Sykes V.W., Straub R.E., Lipkowitz S.,
RA   Boulter J., Boegler O.;
RT   "SETA is a multifunctional adapter protein with three SH3 domains that
RT   binds Grb2, Cbl, and the novel SB1 proteins.";
RL   Cell. Signal. 12:769-779(2000).
CC   -!- FUNCTION: Inhibits CBL-SH3KBP1 complex mediated down-regulation of EGFR
CC       signaling by sequestration of SH3KBP1. Binds to SH3KBP1 and prevents
CC       its interaction with CBL and inhibits translocation of SH3KBP1 to EGFR
CC       containing vesicles upon EGF stimulation.
CC       {ECO:0000250|UniProtKB:Q6P7W2}.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with CUL3; interaction is
CC       direct and forms a 5:5 heterodecamer (By similarity). Interacts (via
CC       PXXXPR motifs) with SH3KBP1 (via SH3 domains) (PubMed:11152963).
CC       Directly interacts with cathepsin B/CTSB (By similarity).
CC       {ECO:0000250|UniProtKB:Q8TBC3, ECO:0000269|PubMed:11152963}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q8TBC3}.
CC   -!- SIMILARITY: Belongs to the KCTD3 family. {ECO:0000305}.
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DR   EMBL; AABR03002621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03004899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001258009.1; NM_001271080.1.
DR   AlphaFoldDB; P0C5J9; -.
DR   SMR; P0C5J9; -.
DR   STRING; 10116.ENSRNOP00000028348; -.
DR   PhosphoSitePlus; P0C5J9; -.
DR   PaxDb; P0C5J9; -.
DR   PRIDE; P0C5J9; -.
DR   Ensembl; ENSRNOT00000028348; ENSRNOP00000028348; ENSRNOG00000020882.
DR   GeneID; 292735; -.
DR   KEGG; rno:292735; -.
DR   UCSC; RGD:1309281; rat.
DR   CTD; 92799; -.
DR   RGD; 1309281; Shkbp1.
DR   eggNOG; KOG2714; Eukaryota.
DR   GeneTree; ENSGT00940000153881; -.
DR   HOGENOM; CLU_012214_0_1_1; -.
DR   InParanoid; P0C5J9; -.
DR   OMA; NWLEIAY; -.
DR   OrthoDB; 351369at2759; -.
DR   PhylomeDB; P0C5J9; -.
DR   TreeFam; TF313754; -.
DR   Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR   PRO; PR:P0C5J9; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000020882; Expressed in thymus and 19 other tissues.
DR   ExpressionAtlas; P0C5J9; baseline and differential.
DR   Genevisible; P0C5J9; RN.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR003131; T1-type_BTB.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF02214; BTB_2; 1.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Lysosome; Phosphoprotein; Reference proteome; Repeat;
KW   WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TBC3"
FT   CHAIN           2..704
FT                   /note="SH3KBP1-binding protein 1"
FT                   /id="PRO_0000307934"
FT   DOMAIN          19..88
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   REPEAT          233..280
FT                   /note="WD 1"
FT   REPEAT          283..322
FT                   /note="WD 2"
FT   REPEAT          324..359
FT                   /note="WD 3"
FT   REPEAT          428..466
FT                   /note="WD 4"
FT   REPEAT          548..586
FT                   /note="WD 5"
FT   REGION          146..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          609..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           618..623
FT                   /note="PXXXPR"
FT                   /evidence="ECO:0000305"
FT   MOTIF           678..683
FT                   /note="PXXXPR"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        609..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TBC3"
FT   MOD_RES         163
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TBC3"
FT   MOD_RES         644
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TBC3"
FT   MOD_RES         646
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TBC3"
SQ   SEQUENCE   704 AA;  75972 MW;  1055B9A0946B5CB1 CRC64;
     MAVPTTAVEG VRSRGAPGEV IHLNVGGKRF STSRQTLTWI PDSFFSSLLS GRISTLKDET
     GAIFIDRDPT VFAPILNFLR TKELDPRGVH GSSLLHEAQF YGLTPLVRRL QVREELDRSS
     CGNVLFNGYL PPPVFPVKRR NRHSLVGPQQ IGGRPAPVRR SNTMPPNLGN AGLLGRMLDD
     RAPPSPSGQP EEPGMVRLVC GHHNWIAVAY THFLVCYRLK EASGWQLAFS SPRLDWPIER
     LALTARVLGG APGEHDKMVA AATGSEILLW ALQAQGGGSE IGVFHLGVPV EALFFVGNQL
     IATSHTGRIG VWNAVTKHWQ VQEVQPITSY DAAGSFLLLG CSNGSIYYVD VQKFPLRMKD
     NDLLVSELYR DPAEDGVTAL SVYLTPKTSD SGNWIEIAYG TSSGVVRVIV QHPETVGSGP
     QLFQTFSVHR SPVTKIMLSE KHLISVCADN NHVRTWSVTR FRGMISTQPG STPLASFKIL
     ALESADGLGG CSAGNDIGPY GERDDQQVFI QKVVPNASQL FVRLSSTGQR VCSVRSVDGS
     ATTAFTVLEC EGSRRLGSRP RRYLLTGQAN GSLAMWDLTT AMDGLGQTPA GGLTEEELMD
     QLEQCELSPL TSSRASFPSP SPRTSLTSLH SASSNTSLCG HRGSPSPPQA GARSRGAGSF
     VDRFKELARG APELRGPPTP APRPSTSLGN PLILPKNTLN ETSF
 
 
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