STABP_RAT
ID STABP_RAT Reviewed; 424 AA.
AC Q8R424;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=STAM-binding protein;
DE EC=3.4.19.- {ECO:0000250|UniProtKB:O95630};
DE AltName: Full=Associated molecule with the SH3 domain of STAM;
GN Name=Stambp; Synonyms=Amsh;
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 [MRNA].
RA Pawlak A., Guellaen G.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
CC -!- FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-
CC linked polyubiquitin chains. Does not cleave 'Lys-48'-linked
CC polyubiquitin chains. Plays a role in signal transduction for cell
CC growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP
CC (bone morphogenetic protein) signaling by antagonizing the inhibitory
CC action of SMAD6 and SMAD7. Has a key role in regulation of cell surface
CC receptor-mediated endocytosis and ubiquitin-dependent sorting of
CC receptors to lysosomes. Endosomal localization of STAMBP is required
CC for efficient EGFR degradation but not for its internalization.
CC Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP
CC signaling pathways. {ECO:0000250|UniProtKB:O95630}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O35864};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O35864};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide.
CC {ECO:0000250|UniProtKB:O95630}.
CC -!- SUBUNIT: Interacts with STAM. Interacts with SMAD6 and SMAD7. Interacts
CC with CHMP3; the interaction appears to relieve the autoinhibition of
CC CHMP3. Interacts with SMURF2 and RNF11; this interaction promotes
CC ubiquitination. {ECO:0000250|UniProtKB:O95630}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95630}. Membrane
CC {ECO:0000250|UniProtKB:O95630}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O95630}. Cytoplasm
CC {ECO:0000250|UniProtKB:O95630}. Early endosome
CC {ECO:0000250|UniProtKB:O95630}.
CC -!- DOMAIN: The JAMM motif is essential for the protease activity.
CC {ECO:0000250|UniProtKB:O35864}.
CC -!- PTM: Phosphorylated after BMP type I receptor activation.
CC {ECO:0000250|UniProtKB:O95630}.
CC -!- PTM: Ubiquitinated by SMURF2 in the presence of RNF11.
CC {ECO:0000250|UniProtKB:O95630}.
CC -!- SIMILARITY: Belongs to the peptidase M67C family. {ECO:0000305}.
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DR EMBL; AY083159; AAL92520.1; -; mRNA.
DR EMBL; BC061711; AAH61711.1; -; mRNA.
DR RefSeq; NP_612540.1; NM_138531.2.
DR RefSeq; XP_006236788.1; XM_006236726.3.
DR RefSeq; XP_006236789.1; XM_006236727.3.
DR RefSeq; XP_008761267.1; XM_008763045.2.
DR RefSeq; XP_008761268.1; XM_008763046.2.
DR RefSeq; XP_008761269.1; XM_008763047.2.
DR RefSeq; XP_008761270.1; XM_008763048.2.
DR AlphaFoldDB; Q8R424; -.
DR SMR; Q8R424; -.
DR IntAct; Q8R424; 2.
DR STRING; 10116.ENSRNOP00000014708; -.
DR MEROPS; M67.003; -.
DR iPTMnet; Q8R424; -.
DR PhosphoSitePlus; Q8R424; -.
DR PaxDb; Q8R424; -.
DR PRIDE; Q8R424; -.
DR Ensembl; ENSRNOT00000014708; ENSRNOP00000014708; ENSRNOG00000012227.
DR GeneID; 171565; -.
DR KEGG; rno:171565; -.
DR UCSC; RGD:619963; rat.
DR CTD; 10617; -.
DR RGD; 619963; Stambp.
DR eggNOG; KOG2880; Eukaryota.
DR GeneTree; ENSGT00940000153710; -.
DR HOGENOM; CLU_023304_0_1_1; -.
DR InParanoid; Q8R424; -.
DR OMA; CNTMHEE; -.
DR OrthoDB; 411229at2759; -.
DR PhylomeDB; Q8R424; -.
DR TreeFam; TF323215; -.
DR Reactome; R-RNO-5689901; Metalloprotease DUBs.
DR PRO; PR:Q8R424; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000012227; Expressed in testis and 20 other tissues.
DR Genevisible; Q8R424; RN.
DR GO; GO:0032154; C:cleavage furrow; ISO:RGD.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0101005; F:deubiquitinase activity; ISO:RGD.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0110088; P:hippocampal neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:RGD.
DR GO; GO:0110091; P:negative regulation of hippocampal neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISO:RGD.
DR GO; GO:0016579; P:protein deubiquitination; ISO:RGD.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IBA:GO_Central.
DR CDD; cd08066; MPN_AMSH_like; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR044098; STAMBP/STALP-like_MPN.
DR InterPro; IPR015063; USP8_dimer.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endosome; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Nucleus; Phosphoprotein; Protease; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..424
FT /note="STAM-binding protein"
FT /id="PRO_0000194871"
FT DOMAIN 257..388
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..127
FT /note="Interaction with CHMP3"
FT /evidence="ECO:0000250|UniProtKB:O95630"
FT REGION 227..231
FT /note="Interaction with STAM"
FT /evidence="ECO:0000250|UniProtKB:O95630"
FT MOTIF 335..348
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT SITE 280
FT /note="Indirect zinc-binding"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95630"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95630"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95630"
SQ SEQUENCE 424 AA; 48512 MW; 90BE083ADACF4B44 CRC64;
MSDHADVSLP PQDRVRILSQ LGSAVELNED IPPRRYFRSG VEIIRMASIY SEEGNIEHAF
ILYNKYITLF IEKLPKHRDY KSAIIPEKKD AVKKLKNVAF PKAEELKTEL LKRYTKEYEQ
YKERKKKEEE ELARNIAIQQ ELEKEKQRVA QQKQKQLEQE QFHAFEKMIQ KQELEKERLK
IVQEFGKVDP GPCGPLLPDL EKPCVDVAPS SPFSPTQTSD CNTTLRPAKP PVVDRSLKPG
ALSVIENVPT IEGLRHIVVP RNLCSEFLQL ASANTAKGIE TCGVLCGKLM RNEFTITHVL
IPRQNGGPDY CHTENEEEIF FMQDDLGLLT LGWIHTHPTQ TAFLSSVDLH THCSYQMMLP
ESIAIVCSPK FQETGFFKLT DYGLQEISTC RQKGFHPHGR DPPLFCDCSH VTVKDRIVTI
TDLR
