STABP_MOUSE
ID STABP_MOUSE Reviewed; 424 AA.
AC Q9CQ26; Q3UTI9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
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 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], DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=11713295; DOI=10.1128/mcb.21.24.8626-8637.2001;
RA Ishii N., Owada Y., Yamada M., Miura S., Murata K., Asao H., Kondo H.,
RA Sugamura K.;
RT "Loss of neurons in the hippocampus and cerebral cortex of AMSH-deficient
RT mice.";
RL Mol. Cell. Biol. 21:8626-8637(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Embryo, and Pituitary;
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].
RC STRAIN=129, and FVB/N; TISSUE=Liver, and Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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: 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 -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:11713295}.
CC -!- DEVELOPMENTAL STAGE: Highest expression at 18.5 dpc, followed by a
CC gradual decrease. {ECO:0000269|PubMed:11713295}.
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 -!- DISRUPTION PHENOTYPE: Mice show a loss of neurons and apoptotic cells
CC in the hippocampus. {ECO:0000269|PubMed:11713295}.
CC -!- SIMILARITY: Belongs to the peptidase M67C family. {ECO:0000305}.
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DR EMBL; AB010123; BAB78604.1; -; mRNA.
DR EMBL; AK017600; BAB30832.1; -; mRNA.
DR EMBL; AK019907; BAB31909.1; -; mRNA.
DR EMBL; AK136961; BAE23188.1; -; mRNA.
DR EMBL; AK139391; BAE23991.1; -; mRNA.
DR EMBL; BC003497; AAH03497.1; -; mRNA.
DR EMBL; BC006939; AAH06939.1; -; mRNA.
DR EMBL; BC025111; AAH25111.1; -; mRNA.
DR CCDS; CCDS20280.1; -.
DR RefSeq; NP_077201.1; NM_024239.2.
DR RefSeq; XP_006506646.1; XM_006506583.2.
DR RefSeq; XP_006506647.1; XM_006506584.2.
DR RefSeq; XP_006506648.1; XM_006506585.1.
DR AlphaFoldDB; Q9CQ26; -.
DR SMR; Q9CQ26; -.
DR BioGRID; 214112; 1.
DR STRING; 10090.ENSMUSP00000070876; -.
DR MEROPS; M67.003; -.
DR iPTMnet; Q9CQ26; -.
DR PhosphoSitePlus; Q9CQ26; -.
DR SwissPalm; Q9CQ26; -.
DR EPD; Q9CQ26; -.
DR MaxQB; Q9CQ26; -.
DR PaxDb; Q9CQ26; -.
DR PRIDE; Q9CQ26; -.
DR ProteomicsDB; 257447; -.
DR Antibodypedia; 31376; 307 antibodies from 35 providers.
DR DNASU; 70527; -.
DR Ensembl; ENSMUST00000068054; ENSMUSP00000070876; ENSMUSG00000006906.
DR Ensembl; ENSMUST00000206400; ENSMUSP00000145871; ENSMUSG00000006906.
DR Ensembl; ENSMUST00000206592; ENSMUSP00000146294; ENSMUSG00000006906.
DR GeneID; 70527; -.
DR KEGG; mmu:70527; -.
DR UCSC; uc009cns.1; mouse.
DR CTD; 10617; -.
DR MGI; MGI:1917777; Stambp.
DR VEuPathDB; HostDB:ENSMUSG00000006906; -.
DR eggNOG; KOG2880; Eukaryota.
DR GeneTree; ENSGT00940000153710; -.
DR HOGENOM; CLU_023304_0_1_1; -.
DR InParanoid; Q9CQ26; -.
DR OMA; CNTMHEE; -.
DR OrthoDB; 411229at2759; -.
DR PhylomeDB; Q9CQ26; -.
DR TreeFam; TF323215; -.
DR Reactome; R-MMU-5689901; Metalloprotease DUBs.
DR BioGRID-ORCS; 70527; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Stambp; mouse.
DR PRO; PR:Q9CQ26; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9CQ26; protein.
DR Bgee; ENSMUSG00000006906; Expressed in interventricular septum and 231 other tissues.
DR Genevisible; Q9CQ26; MM.
DR GO; GO:0032154; C:cleavage furrow; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0101005; F:deubiquitinase activity; ISO:MGI.
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:MGI.
DR GO; GO:0110088; P:hippocampal neuron apoptotic process; IMP:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:MGI.
DR GO; GO:0110091; P:negative regulation of hippocampal neuron apoptotic process; IMP:MGI.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISO:MGI.
DR GO; GO:0016579; P:protein deubiquitination; IMP:MGI.
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 1: Evidence at protein 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_0000194870"
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; 48514 MW; D3A9C2B5F65B7C5E CRC64;
MSDHGDVSLP PQDRVRILSQ LGSAVELNED IPPRRYYRSG VEIIRMASVY SEEGNIEHAF
ILYNKYITLF IEKLPKHRDY KSAIIPEKKD AVKKLKSVAF PKAEELKTEL LRRYTKEYEQ
YKERKKKEEE ELARNIAIQQ ELEKEKQRVA QQKQKQLEQE QFHAFEEMIQ RQELEKERLK
IVQEFGKVDP GPCGPLLPDL EKPCVDVAPS SPFSPTQTPD CNTGMRPAKP PVVDRSLKPG
ALSVIENVPT IEGLRHIVVP RNLCSEFLQL ASANTAKGIE TCGVLCGKLM RNEFTITHVL
IPRQNGGPDY CHTENEEEIF FMQDDLGLLT LGWIHTHPTQ TAFLSSVDLH THCSYQMMLP
ESIAIVCSPK FQETGFFKLT DYGLQEISTC RQKGFHPHGR DPPLFCDCSH VTVKDRIVTI
TDLR
