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Q9H0F6

- SHRPN_HUMAN

UniProt

Q9H0F6 - SHRPN_HUMAN

Protein

Sharpin

Gene

SHARPIN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri348 – 37730RanBP2-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. polyubiquitin binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic nuclear changes Source: Ensembl
    2. brain development Source: Ensembl
    3. keratinization Source: Ensembl
    4. mitochondrion organization Source: Ensembl
    5. negative regulation of inflammatory response Source: UniProtKB
    6. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    7. protein homooligomerization Source: Ensembl
    8. protein linear polyubiquitination Source: UniProtKB
    9. regulation of CD40 signaling pathway Source: UniProtKB
    10. regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sharpin
    Alternative name(s):
    Shank-associated RH domain-interacting protein
    Shank-interacting protein-like 1
    Short name:
    hSIPL1
    Gene namesi
    Name:SHARPIN
    Synonyms:SIPL1
    ORF Names:PSEC0216
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:25321. SHARPIN.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Cell junctionsynapse By similarity
    Note: Enriched at synaptic sites in mature neurons where it colocalizes with SHANK1.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytosol Source: UniProtKB
    3. dendrite Source: Ensembl
    4. LUBAC complex Source: UniProtKB
    5. postsynaptic density Source: Ensembl

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi114 – 1141V → D: Abolishes homodimerization. 1 Publication
    Mutagenesisi272 – 2721I → A: Abolishes interaction with RNF31 and ability to mediate linear polyubiquitination. 1 Publication
    Mutagenesisi354 – 3541C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-357. 1 Publication
    Mutagenesisi357 – 3571C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-354. 1 Publication
    Mutagenesisi358 – 3592TF → LV: Abolishes binding to ubiquitin and ability to mediate linear polyubiquitination.
    Mutagenesisi368 – 3681C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-371. 1 Publication
    Mutagenesisi371 – 3711C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-368. 1 Publication

    Organism-specific databases

    PharmGKBiPA142670925.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 387387SharpinPRO_0000280634Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei165 – 1651Phosphoserine1 Publication
    Modified residuei312 – 3121Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9H0F6.
    PaxDbiQ9H0F6.
    PRIDEiQ9H0F6.

    PTM databases

    PhosphoSiteiQ9H0F6.

    Expressioni

    Tissue specificityi

    Highly expressed in skeletal muscle and placenta and at lower levels in brain, heart, colon without mucosa, thymus, spleen, kidney, liver, small intestine, lung and peripheral blood leukocytes. Up-regulated in various tumor tissues such as kidney, liver, ovary and pancreas tumors.1 Publication

    Gene expression databases

    ArrayExpressiQ9H0F6.
    BgeeiQ9H0F6.
    CleanExiHS_SHARPIN.
    GenevestigatoriQ9H0F6.

    Organism-specific databases

    HPAiHPA044453.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31. LUBAC has a MW of approximative 600 kDa suggesting a heteromultimeric assembly of its subunits. Associates with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-dependent manner. Interacts with EYA1, EYA2, SHANK1 and SHANK3 (via ANK repeats).4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IKBKGQ9Y6K94EBI-3942966,EBI-81279
    ITGA2P173015EBI-3942966,EBI-702960
    ITGA5P086484EBI-3942966,EBI-1382311
    RNF31Q96EP02EBI-3942966,EBI-948111

    Protein-protein interaction databases

    BioGridi123608. 18 interactions.
    DIPiDIP-57842N.
    IntActiQ9H0F6. 11 interactions.
    MINTiMINT-7034570.
    STRINGi9606.ENSP00000381698.

    Structurei

    Secondary structure

    1
    387
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi20 – 3011
    Helixi31 – 333
    Beta strandi40 – 489
    Beta strandi56 – 605
    Beta strandi70 – 734
    Helixi74 – 763
    Beta strandi77 – 837
    Beta strandi86 – 905
    Beta strandi99 – 1057
    Helixi106 – 11914

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4EMOX-ray2.00A/B/C/D1-127[»]
    ProteinModelPortaliQ9H0F6.
    SMRiQ9H0F6. Positions 18-121, 219-302.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini219 – 28870Ubiquitin-likeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 180180Self-associationBy similarityAdd
    BLAST
    Regioni175 – 310136Interaction with SHANK1By similarityAdd
    BLAST

    Domaini

    The Ubiquitin-like domain is required for the interaction with RNF31.
    The RanBP2-type zinc fingers mediate the specific interaction with ubiquitin. Binds preferentially linear polyubiquitin chains and 'Lys-63'-linked polyubiquitin chains over 'Lys-48'-linked polyubiquitin chains. Also binds monoubiquitin.

    Sequence similaritiesi

    Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation
    Contains 1 ubiquitin-like domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri348 – 37730RanBP2-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG278522.
    HOVERGENiHBG093954.
    OMAiHELQPPP.
    PhylomeDBiQ9H0F6.
    TreeFamiTF323486.

    Family and domain databases

    InterProiIPR026168. SHARPIN.
    IPR029071. Ubiquitin-rel_dom.
    IPR001876. Znf_RanBP2.
    [Graphical view]
    PANTHERiPTHR22770:SF31. PTHR22770:SF31. 1 hit.
    PfamiPF00641. zf-RanBP. 1 hit.
    [Graphical view]
    SMARTiSM00547. ZnF_RBZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    PROSITEiPS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H0F6-1) [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

    MAPPAGGAAA AASDLGSAAV LLAVHAAVRP LGAGPDAEAQ LRRLQLSADP    50
    ERPGRFRLEL LGAGPGAVNL EWPLESVSYT IRGPTQHELQ PPPGGPGTLS 100
    LHFLNPQEAQ RWAVLVRGAT VEGQNGSKSN SPPALGPEAC PVSLPSPPEA 150
    STLKGPPPEA DLPRSPGNLT EREELAGSLA RAIAGGDEKG AAQVAAVLAQ 200
    HRVALSVQLQ EACFPPGPIR LQVTLEDAAS AASAASSAHV ALQVHPHCTV 250
    AALQEQVFSE LGFPPAVQRW VIGRCLCVPE RSLASYGVRQ DGDPAFLYLL 300
    SAPREAPATG PSPQHPQKMD GELGRLFPPS LGLPPGPQPA ASSLPSPLQP 350
    SWSCPSCTFI NAPDRPGCEM CSTQRPCTWD PLAAAST 387
    Length:387
    Mass (Da):39,949
    Last modified:March 1, 2001 - v1
    Checksum:i33EE4BF66936AB60
    GO
    Isoform 2 (identifier: Q9H0F6-2) [UniParc]FASTAAdd to Basket

    Also known as: hSIPL1A

    The sequence of this isoform differs from the canonical sequence as follows:
         309-326: TGPSPQHPQKMDGELGRL → QLVLSFLHLHQCPRPPWL
         327-387: Missing.

    Show »
    Length:326
    Mass (Da):33,878
    Checksum:iC92FE8845FD1EC3E
    GO

    Sequence cautioni

    The sequence BAC53798.1 differs from that shown. Reason: Aberrant splicing.
    The sequence BAC11666.1 differs from that shown. Reason: Frameshift at position 334.
    The sequence BAC53797.1 differs from that shown. Reason: Frameshift at position 218.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti238 – 2381A → P in AAH02688. 1 PublicationCurated
    Sequence conflicti243 – 2431Q → R in BAC11666. (PubMed:11230166)Curated
    Sequence conflicti257 – 2571V → A in AAH02688. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti282 – 2821S → T.
    Corresponds to variant rs11541804 [ dbSNP | Ensembl ].
    VAR_047799
    Natural varianti294 – 2941P → S.
    Corresponds to variant rs34674752 [ dbSNP | Ensembl ].
    VAR_047800
    Natural varianti311 – 3111P → R.
    Corresponds to variant rs35844464 [ dbSNP | Ensembl ].
    VAR_047801

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei309 – 32618TGPSP…ELGRL → QLVLSFLHLHQCPRPPWL in isoform 2. 2 PublicationsVSP_023837Add
    BLAST
    Alternative sequencei327 – 38761Missing in isoform 2. 2 PublicationsVSP_023838Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB052764 mRNA. Translation: BAC53797.1. Frameshift.
    AB052765 mRNA. Translation: BAC53798.1. Sequence problems.
    FJ655995 mRNA. Translation: ACN38058.1.
    AL136816 mRNA. Translation: CAB66750.1.
    AK075518 mRNA. Translation: BAC11666.1. Frameshift.
    AC104592 Genomic DNA. No translation available.
    CH471162 Genomic DNA. Translation: EAW82152.1.
    CH471162 Genomic DNA. Translation: EAW82153.1.
    CH471162 Genomic DNA. Translation: EAW82150.1.
    CH471162 Genomic DNA. Translation: EAW82151.1.
    BC002688 mRNA. Translation: AAH02688.2.
    BC025244 mRNA. Translation: AAH25244.1.
    BC034028 mRNA. Translation: AAH34028.1.
    CCDSiCCDS43777.1. [Q9H0F6-1]
    RefSeqiNP_112236.3. NM_030974.3. [Q9H0F6-1]
    UniGeneiHs.529755.

    Genome annotation databases

    EnsembliENST00000359551; ENSP00000352551; ENSG00000179526. [Q9H0F6-2]
    ENST00000398712; ENSP00000381698; ENSG00000179526. [Q9H0F6-1]
    GeneIDi81858.
    KEGGihsa:81858.
    UCSCiuc003zba.3. human. [Q9H0F6-1]

    Polymorphism databases

    DMDMi74733523.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB052764 mRNA. Translation: BAC53797.1 . Frameshift.
    AB052765 mRNA. Translation: BAC53798.1 . Sequence problems.
    FJ655995 mRNA. Translation: ACN38058.1 .
    AL136816 mRNA. Translation: CAB66750.1 .
    AK075518 mRNA. Translation: BAC11666.1 . Frameshift.
    AC104592 Genomic DNA. No translation available.
    CH471162 Genomic DNA. Translation: EAW82152.1 .
    CH471162 Genomic DNA. Translation: EAW82153.1 .
    CH471162 Genomic DNA. Translation: EAW82150.1 .
    CH471162 Genomic DNA. Translation: EAW82151.1 .
    BC002688 mRNA. Translation: AAH02688.2 .
    BC025244 mRNA. Translation: AAH25244.1 .
    BC034028 mRNA. Translation: AAH34028.1 .
    CCDSi CCDS43777.1. [Q9H0F6-1 ]
    RefSeqi NP_112236.3. NM_030974.3. [Q9H0F6-1 ]
    UniGenei Hs.529755.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4EMO X-ray 2.00 A/B/C/D 1-127 [» ]
    ProteinModelPortali Q9H0F6.
    SMRi Q9H0F6. Positions 18-121, 219-302.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123608. 18 interactions.
    DIPi DIP-57842N.
    IntActi Q9H0F6. 11 interactions.
    MINTi MINT-7034570.
    STRINGi 9606.ENSP00000381698.

    PTM databases

    PhosphoSitei Q9H0F6.

    Polymorphism databases

    DMDMi 74733523.

    Proteomic databases

    MaxQBi Q9H0F6.
    PaxDbi Q9H0F6.
    PRIDEi Q9H0F6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359551 ; ENSP00000352551 ; ENSG00000179526 . [Q9H0F6-2 ]
    ENST00000398712 ; ENSP00000381698 ; ENSG00000179526 . [Q9H0F6-1 ]
    GeneIDi 81858.
    KEGGi hsa:81858.
    UCSCi uc003zba.3. human. [Q9H0F6-1 ]

    Organism-specific databases

    CTDi 81858.
    GeneCardsi GC08M145153.
    H-InvDB HIX0017281.
    HIX0124604.
    HGNCi HGNC:25321. SHARPIN.
    HPAi HPA044453.
    MIMi 611885. gene.
    neXtProti NX_Q9H0F6.
    PharmGKBi PA142670925.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG278522.
    HOVERGENi HBG093954.
    OMAi HELQPPP.
    PhylomeDBi Q9H0F6.
    TreeFami TF323486.

    Miscellaneous databases

    GenomeRNAii 81858.
    NextBioi 72187.
    PROi Q9H0F6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H0F6.
    Bgeei Q9H0F6.
    CleanExi HS_SHARPIN.
    Genevestigatori Q9H0F6.

    Family and domain databases

    InterProi IPR026168. SHARPIN.
    IPR029071. Ubiquitin-rel_dom.
    IPR001876. Znf_RanBP2.
    [Graphical view ]
    PANTHERi PTHR22770:SF31. PTHR22770:SF31. 1 hit.
    Pfami PF00641. zf-RanBP. 1 hit.
    [Graphical view ]
    SMARTi SM00547. ZnF_RBZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    PROSITEi PS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Novel human and mouse genes encoding a shank-interacting protein and its upregulation in gastric fundus of W/WV mouse."
      Daigo Y., Takayama I., Ward S.M., Sanders K.M., Fujino M.A.
      J. Gastroenterol. Hepatol. 18:712-718(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    4. "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).
      Tissue: Embryo.
    5. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1 AND 2).
      Tissue: Pancreas, Prostate and Uterus.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION, DOMAIN RANBP2-TYPE, DOMAIN UBIQUITIN-LIKE, UBIQUITIN-BINDING, MUTAGENESIS OF CYS-354; CYS-357; CYS-368 AND CYS-371.
    11. "SHARPIN is a component of the NF-kappaB-activating linear ubiquitin chain assembly complex."
      Tokunaga F., Nakagawa T., Nakahara M., Saeki Y., Taniguchi M., Sakata S., Tanaka K., Nakano H., Iwai K.
      Nature 471:633-636(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION, DOMAIN UBIQUITIN-LIKE.
    12. Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION, DOMAIN RANBP2-TYPE, DOMAIN UBIQUITIN-LIKE, UBIQUITIN-BINDING, MUTAGENESIS OF ILE-272 AND 358-THR-PHE-359.
    13. "Structural analysis of SHARPIN, a subunit of a large multi-protein E3 ubiquitin ligase, reveals a novel dimerization function for the pleckstrin homology superfold."
      Stieglitz B., Haire L.F., Dikic I., Rittinger K.
      J. Biol. Chem. 287:20823-20829(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-127, MUTAGENESIS OF VAL-114, SUBUNIT.

    Entry informationi

    Entry nameiSHRPN_HUMAN
    AccessioniPrimary (citable) accession number: Q9H0F6
    Secondary accession number(s): A6NEG3
    , C0L3L2, D3DWL3, Q8IXF5, Q8IXF6, Q8N2E7, Q8TB25, Q9BUE4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 99 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3