ID SHKB1_MOUSE Reviewed; 704 AA.
AC Q6P7W2; Q3TUN8; Q9ES31;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 148.
DE RecName: Full=SH3KBP1-binding protein 1;
DE AltName: Full=SETA-binding protein 1;
GN Name=Shkbp1; Synonyms=Sb1;
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 [MRNA] (ISOFORM 1), AND 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 FUNCTION, INTERACTION WITH SH3KBP1, DOMAIN PXXXPR MOTIF, AND MUTAGENESIS OF
RP ARG-623 AND ARG-683.
RX PubMed=21830225; DOI=10.1002/cbf.1792;
RA Feng L., Wang J.T., Jin H., Qian K., Geng J.G.;
RT "SH3KBP1-binding protein 1 prevents epidermal growth factor receptor
RT degradation by the interruption of c-Cbl-CIN85 complex.";
RL Cell Biochem. Funct. 29:589-596(2011).
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 (PubMed:21830225).
CC {ECO:0000269|PubMed:21830225}.
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 PubMed:21830225). Directly interacts with cathepsin B/CTSB (By
CC similarity). {ECO:0000250|UniProtKB:Q8TBC3,
CC ECO:0000269|PubMed:11152963, ECO:0000269|PubMed:21830225}.
CC -!- INTERACTION:
CC Q6P7W2; Q9JJ40: Pdzk1; Xeno; NbExp=7; IntAct=EBI-7713890, EBI-7713572;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q8TBC3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P7W2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P7W2-2; Sequence=VSP_028875, VSP_028876;
CC -!- SIMILARITY: Belongs to the KCTD3 family. {ECO:0000305}.
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DR EMBL; AF246218; AAG13656.1; -; mRNA.
DR EMBL; AK160641; BAE35933.1; -; mRNA.
DR EMBL; BC061477; AAH61477.1; -; mRNA.
DR CCDS; CCDS21018.1; -. [Q6P7W2-1]
DR RefSeq; NP_619617.2; NM_138676.2. [Q6P7W2-1]
DR AlphaFoldDB; Q6P7W2; -.
DR SMR; Q6P7W2; -.
DR BioGRID; 228669; 1.
DR IntAct; Q6P7W2; 2.
DR MINT; Q6P7W2; -.
DR STRING; 10090.ENSMUSP00000003857; -.
DR iPTMnet; Q6P7W2; -.
DR PhosphoSitePlus; Q6P7W2; -.
DR EPD; Q6P7W2; -.
DR MaxQB; Q6P7W2; -.
DR PaxDb; 10090-ENSMUSP00000003857; -.
DR PeptideAtlas; Q6P7W2; -.
DR ProteomicsDB; 257003; -. [Q6P7W2-1]
DR ProteomicsDB; 257004; -. [Q6P7W2-2]
DR Pumba; Q6P7W2; -.
DR Antibodypedia; 45190; 87 antibodies from 20 providers.
DR DNASU; 192192; -.
DR Ensembl; ENSMUST00000003857.7; ENSMUSP00000003857.7; ENSMUSG00000089832.9. [Q6P7W2-1]
DR GeneID; 192192; -.
DR KEGG; mmu:192192; -.
DR UCSC; uc009fvv.1; mouse. [Q6P7W2-1]
DR UCSC; uc009fvy.1; mouse. [Q6P7W2-2]
DR AGR; MGI:2385803; -.
DR CTD; 92799; -.
DR MGI; MGI:2385803; Shkbp1.
DR VEuPathDB; HostDB:ENSMUSG00000089832; -.
DR eggNOG; KOG2714; Eukaryota.
DR GeneTree; ENSGT00940000153881; -.
DR HOGENOM; CLU_012214_0_1_1; -.
DR InParanoid; Q6P7W2; -.
DR OMA; MIRAHIC; -.
DR OrthoDB; 5312378at2759; -.
DR PhylomeDB; Q6P7W2; -.
DR TreeFam; TF313754; -.
DR BioGRID-ORCS; 192192; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Shkbp1; mouse.
DR PRO; PR:Q6P7W2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q6P7W2; Protein.
DR Bgee; ENSMUSG00000089832; Expressed in granulocyte and 254 other cell types or tissues.
DR Genevisible; Q6P7W2; MM.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP: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 InterPro; IPR001680; WD40_rpt.
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 SMART; SM00320; WD40; 3.
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; Alternative splicing; Lysosome; Phosphoprotein;
KW Reference proteome; Repeat; 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_0000307933"
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|PubMed:21830225"
FT MOTIF 678..683
FT /note="PXXXPR"
FT /evidence="ECO:0000305|PubMed:21830225"
FT COMPBIAS 609..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..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"
FT MOD_RES 693
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TBC3"
FT VAR_SEQ 1..163
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028875"
FT VAR_SEQ 590
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028876"
FT MUTAGEN 623
FT /note="R->A: No loss of interaction with SH3KBP1, loss of
FT translocation of SH3KBP1 to EGFR containing vesicles upon
FT EGF stimulation, strong delay in the degradation of EGFR
FT upon EGF activation and enhancement of EGFR signaling
FT induced serum response element (SRE) transcriptional
FT reporter activity. Loss of interaction with SH3KBP1, no
FT loss of translocation of SH3KBP1 to EGFR containing
FT vesicles upon EGF stimulation, no effect on the degradation
FT of EGFR upon EGF activation and no effect on EGFR signaling
FT induced serum response element (SRE) transcriptional
FT reporter activity; when associated with A-683."
FT /evidence="ECO:0000269|PubMed:21830225"
FT MUTAGEN 683
FT /note="R->A: No loss of interaction with SH3KBP1, loss of
FT translocation of SH3KBP1 to EGFR containing vesicles upon
FT EGF stimulation, slight delay in the degradation of EGFR
FT upon EGF activation and enhancement of EGFR signaling
FT induced serum response element (SRE) transcriptional
FT reporter activity. Loss of interaction with SH3KBP1, no
FT loss of translocation of SH3KBP1 to EGFR containing
FT vesicles upon EGF stimulation, no effect on the degradation
FT of EGFR upon EGF activation and no effect on EGFR signaling
FT induced serum response element (SRE) transcriptional
FT reporter activity; when associated with A-623."
FT /evidence="ECO:0000269|PubMed:21830225"
FT CONFLICT 4
FT /note="A -> P (in Ref. 1; AAG13656)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="P -> R (in Ref. 1; AAG13656)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="R -> S (in Ref. 2; BAE35933)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 704 AA; 76103 MW; E6AB971825347A8C CRC64;
MAVATTAVEG VPSRGAPGEV IHLNVGGKRF STSRQTLTWI PDSFFSSLLS GRISTLKDET
GAIFIDRDPT VFAPILNFLR TKELDPRGVH GSSLLHEAQF YGLTPLVRRL QVREELDRSS
CGNVLFNGYL PPPVFPVKRR NRHSLVGPQQ IGGRPAPVRR SNTMPPNLGN AGLLGRMLDE
RAPPSPSGQP EEPGMVRLVC GHHNWIAVAY THFLVCYRLK EASGWQLAFS SPRLDWPIER
LALAARVLGG APGEHDKMVA AATGSEILLW ALQAQGGGSE IGVFHLGVPV EALFFVGNQL
IATSHTGRIG VWNAVTKHWQ VQEVQPITSY DAAGSFLLLG CSNGSIYYVD VQKFPLRMKD
NDLLVSELYR DPAEDGVTAL SVYLTPKTSD SGNWIEIAYG TSSGVVRVIV QHPETVGSGP
QLFQTFSVHR SPVTKIMLSE KHLISVCADN NHVRTWSVTR FRGMISTQPG STPLASFKIL
ALESVDGLGG CSAGNDIGPY GERDDQQVFI QKVVPNASQL FVRLSSTGQR VCSVRSVDGS
PTTAFTVLEC EGSRRLGSRP RRYLLTGQAN GSLAMWDLTT AMDGLGQTPA GGLTEEELMD
QLEQCELSPL ASSRGSFPSP SPRTSLTSLH SASSNTSLYG PRGSPSPPQA EARRRGAGSF
VDRCQELARG APELRWPPTP APRPSTSLGN PLTALKKTLN ETSF
//
