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Q96FJ0

- STALP_HUMAN

UniProt

Q96FJ0 - STALP_HUMAN

Protein

AMSH-like protease

Gene

STAMBPL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (23 Nov 2004)
      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.1 Publication

    Cofactori

    Binds 2 zinc ions per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei292 – 2921Indirect zinc-binding
    Metal bindingi347 – 3471Zinc 1; catalytic
    Metal bindingi349 – 3491Zinc 1; catalytic
    Metal bindingi360 – 3601Zinc 1; catalytic
    Metal bindingi362 – 3621Zinc 2
    Metal bindingi402 – 4021Zinc 2
    Metal bindingi408 – 4081Zinc 2
    Metal bindingi410 – 4101Zinc 2

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. metallopeptidase activity Source: UniProtKB-KW
    3. protein binding Source: IntAct

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM67.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AMSH-like protease (EC:3.4.19.-)
    Short name:
    AMSH-LP
    Alternative name(s):
    STAM-binding protein-like 1
    Gene namesi
    Name:STAMBPL1
    Synonyms:AMSHLP, KIAA1373
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:24105. STAMBPL1.

    Subcellular locationi

    GO - Cellular componenti

    1. membrane Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi292 – 2921E → A: Complete loss of catalytic activity. 1 Publication
    Mutagenesisi329 – 3291E → A: 3-fold decrease in substrate affinity. 1 Publication
    Mutagenesisi332 – 3321F → A: 12-fold decrease in substrate affinity, little effect on catalytic activity. 1 Publication
    Mutagenesisi353 – 3531T → A: 19-fold decrease in activity, no change in substrate affinity. 1 Publication
    Mutagenesisi355 – 3551F → A: 161-fold decrease in activity, no change in substrate affinity. 1 Publication
    Mutagenesisi357 – 3571S → A: 34-fold decrease in activity. 1 Publication
    Mutagenesisi358 – 3581S → A: 10-fold decrease in activity, no change in substrate affinity. 1 Publication
    Mutagenesisi360 – 3601D → A: Complete loss of catalytic activity. 1 Publication
    Mutagenesisi370 – 3701M → A: 18-fold decrease in substrate affinity, little effect on catalytic activity. 1 Publication
    Mutagenesisi402 – 4021C → S: 402-fold decrease in activity, slight increase in substrate affinity. 1 Publication
    Mutagenesisi407 – 4071F → A: 35-fold decrease in activity, slight increase in substrate affinity. 1 Publication

    Organism-specific databases

    PharmGKBiPA142670864.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 436436AMSH-like proteasePRO_0000194874Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei25 – 251Phosphoserine1 Publication
    Modified residuei242 – 2421Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96FJ0.
    PaxDbiQ96FJ0.
    PRIDEiQ96FJ0.

    PTM databases

    PhosphoSiteiQ96FJ0.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ96FJ0.
    BgeeiQ96FJ0.
    CleanExiHS_STAMBPL1.
    GenevestigatoriQ96FJ0.

    Organism-specific databases

    HPAiHPA040202.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RNF32Q9H0A62EBI-745021,EBI-724829

    Protein-protein interaction databases

    BioGridi121614. 17 interactions.
    IntActiQ96FJ0. 13 interactions.
    MINTiMINT-1444179.
    STRINGi9606.ENSP00000360992.

    Structurei

    Secondary structure

    1
    436
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi269 – 2724
    Helixi275 – 28713
    Turni288 – 2903
    Beta strandi294 – 3029
    Beta strandi305 – 3139
    Beta strandi316 – 3194
    Beta strandi322 – 3254
    Helixi328 – 33811
    Beta strandi341 – 3488
    Beta strandi350 – 3523
    Helixi358 – 37013
    Beta strandi375 – 3806
    Helixi381 – 3833
    Beta strandi385 – 3917
    Helixi393 – 4019
    Beta strandi416 – 4194
    Beta strandi421 – 4266
    Beta strandi431 – 4344

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZNRX-ray1.20A264-436[»]
    2ZNVX-ray1.60A/D264-436[»]
    ProteinModelPortaliQ96FJ0.
    SMRiQ96FJ0. Positions 18-136, 263-436.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96FJ0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini264 – 373110MPNAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi347 – 36014JAMM motifAdd
    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.
    KOiK11867.
    OMAiDLCHKFL.
    OrthoDBiEOG7NW698.
    PhylomeDBiQ96FJ0.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96FJ0-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDQPFTVNSL KKLAAMPDHT DVSLSPEERV RALSKLGCNI TISEDITPRR    50
    YFRSGVEMER MASVYLEEGN LENAFVLYNK FITLFVEKLP NHRDYQQCAV 100
    PEKQDIMKKL KEIAFPRTDE LKNDLLKKYN VEYQEYLQSK NKYKAEILKK 150
    LEHQRLIEAE RKRIAQMRQQ QLESEQFLFF EDQLKKQELA RGQMRSQQTS 200
    GLSEQIDGSA LSCFSTHQNN SLLNVFADQP NKSDATNYAS HSPPVNRALT 250
    PAATLSAVQN LVVEGLRCVV LPEDLCHKFL QLAESNTVRG IETCGILCGK 300
    LTHNEFTITH VIVPKQSAGP DYCDMENVEE LFNVQDQHDL LTLGWIHTHP 350
    TQTAFLSSVD LHTHCSYQLM LPEAIAIVCS PKHKDTGIFR LTNAGMLEVS 400
    ACKKKGFHPH TKEPRLFSIC KHVLVKDIKI IVLDLR 436
    Length:436
    Mass (Da):49,783
    Last modified:November 23, 2004 - v2
    Checksum:i722662C76A734102
    GO
    Isoform 2 (identifier: Q96FJ0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         420-436: CKHVLVKDIKIIVLDLR → QKFLSGIISGTALEMEPLKIGYGPNGFPLLGISRSSSPSEQL

    Show »
    Length:461
    Mass (Da):52,199
    Checksum:i266828EB12055970
    GO

    Sequence cautioni

    The sequence BAA92611.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI13863.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti196 – 1961S → N.
    Corresponds to variant rs12254856 [ dbSNP | Ensembl ].
    VAR_051817
    Natural varianti204 – 2041E → K.
    Corresponds to variant rs34270879 [ dbSNP | Ensembl ].
    VAR_051818
    Natural varianti210 – 2101A → T.
    Corresponds to variant rs9988723 [ dbSNP | Ensembl ].
    VAR_051819

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei420 – 43617CKHVL…VLDLR → QKFLSGIISGTALEMEPLKI GYGPNGFPLLGISRSSSPSE QL in isoform 2. 1 PublicationVSP_014648Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB010120 mRNA. Translation: BAC77766.1.
    AB037794 mRNA. Translation: BAA92611.1. Different initiation.
    AK056086 mRNA. Translation: BAG51619.1.
    AL157394 Genomic DNA. Translation: CAI13861.1.
    AL157394 Genomic DNA. Translation: CAI13862.1.
    AL157394 Genomic DNA. Translation: CAI13863.1. Sequence problems.
    CH471066 Genomic DNA. Translation: EAW50156.1.
    BC010846 mRNA. Translation: AAH10846.2.
    CCDSiCCDS7391.1. [Q96FJ0-1]
    RefSeqiNP_065850.1. NM_020799.3. [Q96FJ0-1]
    XP_006717991.1. XM_006717928.1. [Q96FJ0-1]
    XP_006717992.1. XM_006717929.1. [Q96FJ0-1]
    XP_006717993.1. XM_006717930.1. [Q96FJ0-1]
    UniGeneiHs.16229.
    Hs.701879.

    Genome annotation databases

    EnsembliENST00000371924; ENSP00000360992; ENSG00000138134. [Q96FJ0-1]
    ENST00000371926; ENSP00000360994; ENSG00000138134. [Q96FJ0-1]
    ENST00000371927; ENSP00000360995; ENSG00000138134. [Q96FJ0-2]
    GeneIDi57559.
    KEGGihsa:57559.
    UCSCiuc001kfk.4. human. [Q96FJ0-1]
    uc010qmx.2. human. [Q96FJ0-2]

    Polymorphism databases

    DMDMi71153542.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB010120 mRNA. Translation: BAC77766.1 .
    AB037794 mRNA. Translation: BAA92611.1 . Different initiation.
    AK056086 mRNA. Translation: BAG51619.1 .
    AL157394 Genomic DNA. Translation: CAI13861.1 .
    AL157394 Genomic DNA. Translation: CAI13862.1 .
    AL157394 Genomic DNA. Translation: CAI13863.1 . Sequence problems.
    CH471066 Genomic DNA. Translation: EAW50156.1 .
    BC010846 mRNA. Translation: AAH10846.2 .
    CCDSi CCDS7391.1. [Q96FJ0-1 ]
    RefSeqi NP_065850.1. NM_020799.3. [Q96FJ0-1 ]
    XP_006717991.1. XM_006717928.1. [Q96FJ0-1 ]
    XP_006717992.1. XM_006717929.1. [Q96FJ0-1 ]
    XP_006717993.1. XM_006717930.1. [Q96FJ0-1 ]
    UniGenei Hs.16229.
    Hs.701879.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZNR X-ray 1.20 A 264-436 [» ]
    2ZNV X-ray 1.60 A/D 264-436 [» ]
    ProteinModelPortali Q96FJ0.
    SMRi Q96FJ0. Positions 18-136, 263-436.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121614. 17 interactions.
    IntActi Q96FJ0. 13 interactions.
    MINTi MINT-1444179.
    STRINGi 9606.ENSP00000360992.

    Protein family/group databases

    MEROPSi M67.003.

    PTM databases

    PhosphoSitei Q96FJ0.

    Polymorphism databases

    DMDMi 71153542.

    Proteomic databases

    MaxQBi Q96FJ0.
    PaxDbi Q96FJ0.
    PRIDEi Q96FJ0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371924 ; ENSP00000360992 ; ENSG00000138134 . [Q96FJ0-1 ]
    ENST00000371926 ; ENSP00000360994 ; ENSG00000138134 . [Q96FJ0-1 ]
    ENST00000371927 ; ENSP00000360995 ; ENSG00000138134 . [Q96FJ0-2 ]
    GeneIDi 57559.
    KEGGi hsa:57559.
    UCSCi uc001kfk.4. human. [Q96FJ0-1 ]
    uc010qmx.2. human. [Q96FJ0-2 ]

    Organism-specific databases

    CTDi 57559.
    GeneCardsi GC10P090630.
    H-InvDB HIX0009014.
    HGNCi HGNC:24105. STAMBPL1.
    HPAi HPA040202.
    MIMi 612352. gene.
    neXtProti NX_Q96FJ0.
    PharmGKBi PA142670864.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1310.
    HOGENOMi HOG000195792.
    HOVERGENi HBG058519.
    KOi K11867.
    OMAi DLCHKFL.
    OrthoDBi EOG7NW698.
    PhylomeDBi Q96FJ0.
    TreeFami TF323215.

    Miscellaneous databases

    ChiTaRSi STAMBPL1. human.
    EvolutionaryTracei Q96FJ0.
    GeneWikii STAMBPL1.
    GenomeRNAii 57559.
    NextBioi 64054.
    PROi Q96FJ0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96FJ0.
    Bgeei Q96FJ0.
    CleanExi HS_STAMBPL1.
    Genevestigatori Q96FJ0.

    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. "Identification of AMSH-LP containing a Jab1/MPN domain metalloenzyme motif."
      Kikuchi K., Ishii N., Asano H., Sugamura K.
      Biochem. Biophys. Res. Commun. 306:637-643(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Peripheral blood lymphocyte.
    2. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Pancreas.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains."
      Sato Y., Yoshikawa A., Yamagata A., Mimura H., Yamashita M., Ookata K., Nureki O., Iwai K., Komada M., Fukai S.
      Nature 455:358-362(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 263-436 IN COMPLEXES WITH ZINC IONS AND WITH LYS-63-LINKED DI-UBIQUITIN, FUNCTION, COFACTOR, MUTAGENESIS OF GLU-292; GLU-329; PHE-332; THR-353; PHE-355; SER-357; SER-358; ASP-360; MET-370; CYS-402 AND PHE-407.

    Entry informationi

    Entry nameiSTALP_HUMAN
    AccessioniPrimary (citable) accession number: Q96FJ0
    Secondary accession number(s): B3KPA7
    , Q5T9N4, Q5T9N9, Q7Z420, Q9P2H4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 104 of the entry and version 2 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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