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 24-JAN-2024, entry version 106.
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; 10116-ENSRNOP00000028348; -.
DR Ensembl; ENSRNOT00000028348.8; ENSRNOP00000028348.4; ENSRNOG00000020882.8.
DR GeneID; 292735; -.
DR KEGG; rno:292735; -.
DR UCSC; RGD:1309281; rat.
DR AGR; RGD:1309281; -.
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; MIRAHIC; -.
DR OrthoDB; 5312378at2759; -.
DR PhylomeDB; P0C5J9; -.
DR TreeFam; TF313754; -.
DR PRO; PR:P0C5J9; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020882; Expressed in thymus and 19 other cell types or 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 CDD; cd18393; BTB_POZ_SHKBP1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR047876; SHKBP1/KCTD3.
DR InterPro; IPR047825; SHKBP1_KCTD3_BTB_POZ.
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 PANTHER; PTHR15859; SETA BINDING PROTEIN 1; 1.
DR PANTHER; PTHR15859:SF5; SH3KBP1-BINDING PROTEIN 1; 1.
DR Pfam; PF02214; BTB_2; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 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
//
