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O95630

- STABP_HUMAN

UniProt

O95630 - STABP_HUMAN

Protein

STAM-binding protein

Gene

STAMBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains By similarity. Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. Has a key role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization By similarity. Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways.By similarity5 Publications

    Cofactori

    Binds 2 zinc ions per subunit.By similarity

    Enzyme regulationi

    Inhibited by N-ethylmaleimide.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei280 – 2801Indirect zinc-bindingBy similarity
    Metal bindingi335 – 3351Zinc 1; catalyticBy similarity
    Metal bindingi337 – 3371Zinc 1; catalyticBy similarity
    Metal bindingi348 – 3481Zinc 1; catalyticBy similarity
    Metal bindingi350 – 3501Zinc 2By similarity
    Metal bindingi390 – 3901Zinc 2By similarity
    Metal bindingi396 – 3961Zinc 2By similarity
    Metal bindingi398 – 3981Zinc 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. metallopeptidase activity Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. ubiquitin-specific protease activity Source: MGI

    GO - Biological processi

    1. JAK-STAT cascade Source: ProtInc
    2. mitotic cytokinesis Source: MGI
    3. negative regulation of neuron apoptotic process Source: Ensembl
    4. negative regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    5. negative regulation of Ras protein signal transduction Source: UniProtKB
    6. positive regulation of cell proliferation Source: ProtInc
    7. protein deubiquitination Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiO95630.

    Protein family/group databases

    MEROPSiM67.006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    STAM-binding protein (EC:3.4.19.-)
    Alternative name(s):
    Associated molecule with the SH3 domain of STAM
    Endosome-associated ubiquitin isopeptidase
    Gene namesi
    Name:STAMBP
    Synonyms:AMSH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:16950. STAMBP.

    Subcellular locationi

    GO - Cellular componenti

    1. cleavage furrow Source: MGI
    2. cytoplasm Source: HPA
    3. early endosome Source: UniProtKB-SubCell
    4. extracellular vesicular exosome Source: UniProt
    5. nucleus Source: HPA
    6. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Microcephaly-capillary malformation syndrome (MICCAP) [MIM:614261]: A congenital disorder characterized by severe progressive microcephaly, early-onset refractory epilepsy, profound developmental delay, and multiple small capillary malformations spread diffusely on the body. Additional more variable features include dysmorphic facial features, distal limb abnormalities, and mild heart defects.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141R → P in MICCAP. 1 Publication
    VAR_069806
    Natural varianti38 – 381R → C in MICCAP. 1 Publication
    VAR_069807
    Natural varianti42 – 421E → G in MICCAP. 1 Publication
    VAR_069808
    Natural varianti63 – 631Y → C in MICCAP. 1 Publication
    VAR_069809
    Natural varianti100 – 1001F → Y in MICCAP. 1 Publication
    VAR_069810
    Natural varianti313 – 3131T → I in MICCAP. 1 Publication
    VAR_069811

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi348 – 3481D → A: Promotes accumulation of ubiquitin on endosomes, ablates enzymatic activity toward polyubiquitin substrate and allows ubiquitinated STAM stabilization. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614261. phenotype.
    Orphaneti294016. Microcephaly-capillary malformation syndrome.
    PharmGKBiPA134955569.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 424424STAM-binding proteinPRO_0000194869Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei48 – 481Phosphoserine1 Publication
    Modified residuei243 – 2431Phosphoserine1 Publication
    Modified residuei245 – 2451Phosphoserine1 Publication
    Modified residuei247 – 2471Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated after BMP type I receptor activation.1 Publication
    Ubiquitinated by SMURF2 in the presence of RNF11.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO95630.
    PaxDbiO95630.
    PeptideAtlasiO95630.
    PRIDEiO95630.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00007943.

    PTM databases

    PhosphoSiteiO95630.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.

    Gene expression databases

    ArrayExpressiO95630.
    BgeeiO95630.
    CleanExiHS_STAMBP.
    GenevestigatoriO95630.

    Organism-specific databases

    HPAiHPA035800.

    Interactioni

    Subunit structurei

    Interacts with STAM1. Interacts with SMAD6 and SMAD7. Interacts with CHMP3; the interaction appears to relieve the autoinhibition of CHMP3. Interacts with SMURF2 and RNF11; this interaction promotes ubiquitination.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CHMP1AQ9HD423EBI-396676,EBI-1057156
    CHMP1BQ7LBR15EBI-396676,EBI-2118090
    CHMP3Q9Y3E75EBI-396676,EBI-2118119
    CHMP5Q9NZZ32EBI-396676,EBI-751303
    GRB2P629933EBI-396676,EBI-401755
    RNF11Q9Y3C52EBI-396676,EBI-396669
    SMAD6O43541-22EBI-396676,EBI-4324970
    STAMQ927836EBI-396676,EBI-752333
    STAM2O758863EBI-396676,EBI-373258

    Protein-protein interaction databases

    BioGridi115863. 44 interactions.
    DIPiDIP-33062N.
    IntActiO95630. 29 interactions.
    MINTiMINT-96921.
    STRINGi9606.ENSP00000344742.

    Structurei

    Secondary structure

    1
    424
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 2212
    Helixi33 – 5321
    Helixi56 – 7116
    Helixi74 – 763
    Turni78 – 825
    Helixi88 – 9710
    Helixi99 – 13739
    Beta strandi257 – 2604
    Helixi263 – 27614
    Beta strandi282 – 2909
    Beta strandi293 – 3019
    Beta strandi304 – 3063
    Beta strandi311 – 3133
    Helixi316 – 32611
    Beta strandi329 – 3368
    Beta strandi338 – 3403
    Helixi346 – 35813
    Beta strandi363 – 3686
    Turni369 – 3724
    Beta strandi373 – 3797
    Helixi381 – 3899
    Beta strandi404 – 4074
    Beta strandi409 – 4146
    Beta strandi419 – 4224

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XZEX-ray1.75A/B1-146[»]
    3RZUX-ray2.50A/B/C/D/E/F/G243-424[»]
    3RZVX-ray1.67A219-424[»]
    ProteinModelPortaliO95630.
    SMRiO95630. Positions 2-142, 248-424.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini252 – 361110MPNAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 127127Interaction with CHMP3Add
    BLAST
    Regioni227 – 2315Interaction with STAM1

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi335 – 34814JAMM motifAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi104 – 17774Glu-richAdd
    BLAST

    Domaini

    The JAMM motif is essential for the protease activity.By similarity

    Sequence similaritiesi

    Belongs to the peptidase M67C family.Curated
    Contains 1 MPN (JAB/Mov34) domain.Curated

    Phylogenomic databases

    eggNOGiCOG1310.
    HOGENOMiHOG000195792.
    HOVERGENiHBG058519.
    InParanoidiO95630.
    KOiK11866.
    OMAiPSDCHTT.
    OrthoDBiEOG7NW698.
    PhylomeDBiO95630.
    TreeFamiTF323215.

    Family and domain databases

    InterProiIPR000555. JAMM/MPN+_dom.
    IPR015063. USP8_dimer.
    [Graphical view]
    PfamiPF01398. JAB. 1 hit.
    PF08969. USP8_dimer. 1 hit.
    [Graphical view]
    SMARTiSM00232. JAB_MPN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O95630-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDHGDVSLP PEDRVRALSQ LGSAVEVNED IPPRRYFRSG VEIIRMASIY    50
    SEEGNIEHAF ILYNKYITLF IEKLPKHRDY KSAVIPEKKD TVKKLKEIAF 100
    PKAEELKAEL LKRYTKEYTE YNEEKKKEAE ELARNMAIQQ ELEKEKQRVA 150
    QQKQQQLEQE QFHAFEEMIR NQELEKERLK IVQEFGKVDP GLGGPLVPDL 200
    EKPSLDVFPT LTVSSIQPSD CHTTVRPAKP PVVDRSLKPG ALSNSESIPT 250
    IDGLRHVVVP GRLCPQFLQL ASANTARGVE TCGILCGKLM RNEFTITHVL 300
    IPKQSAGSDY CNTENEEELF LIQDQQGLIT LGWIHTHPTQ TAFLSSVDLH 350
    THCSYQMMLP ESVAIVCSPK FQETGFFKLT DHGLEEISSC RQKGFHPHSK 400
    DPPLFCSCSH VTVVDRAVTI TDLR 424
    Length:424
    Mass (Da):48,077
    Last modified:May 1, 1999 - v1
    Checksum:i7B6E08A245BD9D43
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141R → P in MICCAP. 1 Publication
    VAR_069806
    Natural varianti38 – 381R → C in MICCAP. 1 Publication
    VAR_069807
    Natural varianti42 – 421E → G in MICCAP. 1 Publication
    VAR_069808
    Natural varianti63 – 631Y → C in MICCAP. 1 Publication
    VAR_069809
    Natural varianti100 – 1001F → Y in MICCAP. 1 Publication
    VAR_069810
    Natural varianti313 – 3131T → I in MICCAP. 1 Publication
    VAR_069811

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73522 mRNA. Translation: AAD05037.1.
    AC073046 Genomic DNA. Translation: AAX88908.1.
    CH471053 Genomic DNA. Translation: EAW99715.1.
    CH471053 Genomic DNA. Translation: EAW99716.1.
    BC007682 mRNA. Translation: AAH07682.1.
    BC065574 mRNA. Translation: AAH65574.1.
    BC101467 mRNA. Translation: AAI01468.1.
    BC101469 mRNA. Translation: AAI01470.1.
    CCDSiCCDS1929.1.
    RefSeqiNP_006454.1. NM_006463.4.
    NP_964010.1. NM_201647.2.
    NP_998787.1. NM_213622.2.
    XP_005264145.1. XM_005264088.1.
    UniGeneiHs.469018.

    Genome annotation databases

    EnsembliENST00000339566; ENSP00000344742; ENSG00000124356.
    ENST00000394070; ENSP00000377633; ENSG00000124356.
    ENST00000394073; ENSP00000377636; ENSG00000124356.
    ENST00000409707; ENSP00000386548; ENSG00000124356.
    GeneIDi10617.
    KEGGihsa:10617.
    UCSCiuc002sjs.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73522 mRNA. Translation: AAD05037.1 .
    AC073046 Genomic DNA. Translation: AAX88908.1 .
    CH471053 Genomic DNA. Translation: EAW99715.1 .
    CH471053 Genomic DNA. Translation: EAW99716.1 .
    BC007682 mRNA. Translation: AAH07682.1 .
    BC065574 mRNA. Translation: AAH65574.1 .
    BC101467 mRNA. Translation: AAI01468.1 .
    BC101469 mRNA. Translation: AAI01470.1 .
    CCDSi CCDS1929.1.
    RefSeqi NP_006454.1. NM_006463.4.
    NP_964010.1. NM_201647.2.
    NP_998787.1. NM_213622.2.
    XP_005264145.1. XM_005264088.1.
    UniGenei Hs.469018.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XZE X-ray 1.75 A/B 1-146 [» ]
    3RZU X-ray 2.50 A/B/C/D/E/F/G 243-424 [» ]
    3RZV X-ray 1.67 A 219-424 [» ]
    ProteinModelPortali O95630.
    SMRi O95630. Positions 2-142, 248-424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115863. 44 interactions.
    DIPi DIP-33062N.
    IntActi O95630. 29 interactions.
    MINTi MINT-96921.
    STRINGi 9606.ENSP00000344742.

    Protein family/group databases

    MEROPSi M67.006.

    PTM databases

    PhosphoSitei O95630.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00007943.

    Proteomic databases

    MaxQBi O95630.
    PaxDbi O95630.
    PeptideAtlasi O95630.
    PRIDEi O95630.

    Protocols and materials databases

    DNASUi 10617.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000339566 ; ENSP00000344742 ; ENSG00000124356 .
    ENST00000394070 ; ENSP00000377633 ; ENSG00000124356 .
    ENST00000394073 ; ENSP00000377636 ; ENSG00000124356 .
    ENST00000409707 ; ENSP00000386548 ; ENSG00000124356 .
    GeneIDi 10617.
    KEGGi hsa:10617.
    UCSCi uc002sjs.3. human.

    Organism-specific databases

    CTDi 10617.
    GeneCardsi GC02P074056.
    GeneReviewsi STAMBP.
    HGNCi HGNC:16950. STAMBP.
    HPAi HPA035800.
    MIMi 606247. gene.
    614261. phenotype.
    neXtProti NX_O95630.
    Orphaneti 294016. Microcephaly-capillary malformation syndrome.
    PharmGKBi PA134955569.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1310.
    HOGENOMi HOG000195792.
    HOVERGENi HBG058519.
    InParanoidi O95630.
    KOi K11866.
    OMAi PSDCHTT.
    OrthoDBi EOG7NW698.
    PhylomeDBi O95630.
    TreeFami TF323215.

    Enzyme and pathway databases

    SignaLinki O95630.

    Miscellaneous databases

    GeneWikii STAMBP.
    GenomeRNAii 10617.
    NextBioi 40340.
    PROi O95630.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95630.
    Bgeei O95630.
    CleanExi HS_STAMBP.
    Genevestigatori O95630.

    Family and domain databases

    InterProi IPR000555. JAMM/MPN+_dom.
    IPR015063. USP8_dimer.
    [Graphical view ]
    Pfami PF01398. JAB. 1 hit.
    PF08969. USP8_dimer. 1 hit.
    [Graphical view ]
    SMARTi SM00232. JAB_MPN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Possible involvement of a novel STAM-associated molecule 'AMSH' in intracellular signal transduction mediated by cytokines."
      Tanaka N., Kaneko K., Asao H., Kasai H., Endo Y., Fujita T., Takeshita T., Sugamura K.
      J. Biol. Chem. 274:19129-19135(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH STAM1.
      Tissue: Peripheral blood lymphocyte.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain, Eye and Lymph.
    5. "Promoting bone morphogenetic protein signaling through negative regulation of inhibitory Smads."
      Itoh F., Asao H., Sugamura K., Heldin C.-H., ten Dijke P., Itoh S.
      EMBO J. 20:4132-4142(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SMAD6 AND SMAD7, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2; SER-48; SER-243; SER-245 AND SER-247.
    6. "MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function."
      Maytal-Kivity V., Reis N., Hofmann K., Glickman M.H.
      BMC Biochem. 3:28-28(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT OF GLU-280; HIS-335 AND HIS-337 IN ZINC-BINDING.
    7. "AMSH is an endosome-associated ubiquitin isopeptidase."
      McCullough J., Clague M.J., Urbe S.
      J. Cell Biol. 166:487-492(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-348, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STAM1.
    8. "An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein."
      Li H., Seth A.K.
      Oncogene 23:1801-1808(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMURF2 AND RNF11, UBIQUITINATION.
    9. "Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding."
      Zamborlini A., Usami Y., Radoshitzky S.R., Popova E., Palu G., Goettlinger H.
      Proc. Natl. Acad. Sci. U.S.A. 103:19140-19145(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHMP3.
    10. "Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation."
      Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P., Goettlinger H.G., Kirchhausen T.
      J. Biol. Chem. 282:9805-9812(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHMP3, SUBCELLULAR LOCATION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: FUNCTION, VARIANTS MICCAP PRO-14; CYS-38; GLY-42; CYS-63; TYR-100 AND ILE-313.

    Entry informationi

    Entry nameiSTABP_HUMAN
    AccessioniPrimary (citable) accession number: O95630
    Secondary accession number(s): D6W5H7, Q3MJE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    X-ray crystallography studies of STAMBPL1, another member of the peptidase M67C family, has shown that Glu-280 binds zinc indirectly via a water molecule. Nevertheless, this residue is essential for catalytic activity.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3