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Q8IWV7

- UBR1_HUMAN

UniProt

Q8IWV7 - UBR1_HUMAN

Protein

E3 ubiquitin-protein ligase UBR1

Gene

UBR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. May be involved in pancreatic homeostasis. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth.4 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri97 – 16872UBR-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1098 – 1201104RING-type; atypicalAdd
    BLAST

    GO - Molecular functioni

    1. leucine binding Source: UniProtKB
    2. ligase activity Source: UniProtKB-KW
    3. ubiquitin-protein transferase activity Source: Ensembl
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular response to leucine Source: UniProtKB
    2. negative regulation of TOR signaling Source: UniProtKB
    3. ubiquitin-dependent protein catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase UBR1 (EC:6.3.2.-)
    Alternative name(s):
    N-recognin-1
    Ubiquitin-protein ligase E3-alpha-1
    Ubiquitin-protein ligase E3-alpha-I
    Gene namesi
    Name:UBR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:16808. UBR1.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. proteasome complex Source: Ensembl
    3. ubiquitin ligase complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Johanson-Blizzard syndrome (JBS) [MIM:243800]: This disorder includes congenital exocrine pancreatic insufficiency, multiple malformations such as nasal wing aplasia, and frequent mental retardation. Pancreas of individuals with JBS do not express UBR1 and show intrauterine-onset destructive pancreatitis.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti136 – 1361H → R in JBS; prevents proper folding of the UBR-type zinc finger. 2 Publications
    VAR_024741
    Natural varianti1279 – 12791G → S in JBS. 1 Publication
    VAR_024742

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi243800. phenotype.
    Orphaneti2315. Johanson-Blizzard syndrome.
    PharmGKBiPA38187.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 17491748E3 ubiquitin-protein ligase UBR1PRO_0000056136Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei21 – 211Phosphothreonine3 Publications
    Modified residuei1179 – 11791Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8IWV7.
    PaxDbiQ8IWV7.
    PRIDEiQ8IWV7.

    PTM databases

    PhosphoSiteiQ8IWV7.

    Expressioni

    Tissue specificityi

    Broadly expressed, with highest levels in skeletal muscle, kidney and pancreas. Present in acinar cells of the pancreas (at protein level).3 Publications

    Developmental stagei

    Expressed in fetal pancreas.1 Publication

    Gene expression databases

    ArrayExpressiQ8IWV7.
    BgeeiQ8IWV7.
    CleanExiHS_UBR1.
    GenevestigatoriQ8IWV7.

    Organism-specific databases

    HPAiHPA038838.

    Interactioni

    Subunit structurei

    Interacts with RECQL4.2 Publications

    Protein-protein interaction databases

    BioGridi128238. 47 interactions.
    DIPiDIP-47033N.
    IntActiQ8IWV7. 29 interactions.
    MINTiMINT-1417571.
    STRINGi9606.ENSP00000290650.

    Structurei

    Secondary structure

    1
    1749
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi108 – 1125
    Turni113 – 1153
    Beta strandi116 – 1183
    Helixi125 – 1284
    Helixi132 – 1354
    Beta strandi138 – 1425
    Beta strandi156 – 1594
    Turni164 – 1663

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NY1X-ray2.08A/B97-168[»]
    ProteinModelPortaliQ8IWV7.
    SMRiQ8IWV7. Positions 97-167.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IWV7.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi864 – 8696Poly-Pro

    Domaini

    The RING-H2 zinc finger is an atypical RING finger with a His ligand in place of the fourth Cys of the classical motif.
    The UBR-type zinc finger forms a pocket that mediates recognition of type 1 N-degrons. It exhibits preference for Arginine in first position, has poor affinity for histidine, and doesn't bind acetylated peptides.

    Sequence similaritiesi

    Belongs to the UBR1 family.Curated
    Contains 1 RING-type zinc finger.Curated
    Contains 1 UBR-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri97 – 16872UBR-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1098 – 1201104RING-type; atypicalAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG310244.
    HOVERGENiHBG080426.
    InParanoidiQ8IWV7.
    KOiK10625.
    OMAiICLKEEA.
    OrthoDBiEOG7RNJZB.
    PhylomeDBiQ8IWV7.
    TreeFamiTF323875.

    Family and domain databases

    Gene3Di3.30.1390.10. 1 hit.
    3.30.40.10. 2 hits.
    InterProiIPR003769. ClpS_core.
    IPR014719. Ribosomal_L7/12_C/ClpS-like.
    IPR003126. Znf_N-recognin.
    IPR013993. Znf_N-recognin_met.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF02617. ClpS. 1 hit.
    PF02207. zf-UBR. 1 hit.
    [Graphical view]
    SMARTiSM00396. ZnF_UBR1. 1 hit.
    [Graphical view]
    SUPFAMiSSF54736. SSF54736. 1 hit.
    PROSITEiPS51157. ZF_UBR. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IWV7-1) [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

    MADEEAGGTE RMEISAELPQ TPQRLASWWD QQVDFYTAFL HHLAQLVPEI     50
    YFAEMDPDLE KQEESVQMSI FTPLEWYLFG EDPDICLEKL KHSGAFQLCG 100
    RVFKSGETTY SCRDCAIDPT CVLCMDCFQD SVHKNHRYKM HTSTGGGFCD 150
    CGDTEAWKTG PFCVNHEPGR AGTIKENSRC PLNEEVIVQA RKIFPSVIKY 200
    VVEMTIWEEE KELPPELQIR EKNERYYCVL FNDEHHSYDH VIYSLQRALD 250
    CELAEAQLHT TAIDKEGRRA VKAGAYAACQ EAKEDIKSHS ENVSQHPLHV 300
    EVLHSEIMAH QKFALRLGSW MNKIMSYSSD FRQIFCQACL REEPDSENPC 350
    LISRLMLWDA KLYKGARKIL HELIFSSFFM EMEYKKLFAM EFVKYYKQLQ 400
    KEYISDDHDR SISITALSVQ MFTVPTLARH LIEEQNVISV ITETLLEVLP 450
    EYLDRNNKFN FQGYSQDKLG RVYAVICDLK YILISKPTIW TERLRMQFLE 500
    GFRSFLKILT CMQGMEEIRR QVGQHIEVDP DWEAAIAIQM QLKNILLMFQ 550
    EWCACDEELL LVAYKECHKA VMRCSTSFIS SSKTVVQSCG HSLETKSYRV 600
    SEDLVSIHLP LSRTLAGLHV RLSRLGAVSR LHEFVSFEDF QVEVLVEYPL 650
    RCLVLVAQVV AEMWRRNGLS LISQVFYYQD VKCREEMYDK DIIMLQIGAS 700
    LMDPNKFLLL VLQRYELAEA FNKTISTKDQ DLIKQYNTLI EEMLQVLIYI 750
    VGERYVPGVG NVTKEEVTMR EIIHLLCIEP MPHSAIAKNL PENENNETGL 800
    ENVINKVATF KKPGVSGHGV YELKDESLKD FNMYFYHYSK TQHSKAEHMQ 850
    KKRRKQENKD EALPPPPPPE FCPAFSKVIN LLNCDIMMYI LRTVFERAID 900
    TDSNLWTEGM LQMAFHILAL GLLEEKQQLQ KAPEEEVTFD FYHKASRLGS 950
    SAMNIQMLLE KLKGIPQLEG QKDMITWILQ MFDTVKRLRE KSCLIVATTS 1000
    GSESIKNDEI THDKEKAERK RKAEAARLHR QKIMAQMSAL QKNFIETHKL 1050
    MYDNTSEMPG KEDSIMEEES TPAVSDYSRI ALGPKRGPSV TEKEVLTCIL 1100
    CQEEQEVKIE NNAMVLSACV QKSTALTQHR GKPIELSGEA LDPLFMDPDL 1150
    AYGTYTGSCG HVMHAVCWQK YFEAVQLSSQ QRIHVDLFDL ESGEYLCPLC 1200
    KSLCNTVIPI IPLQPQKINS ENADALAQLL TLARWIQTVL ARISGYNIRH 1250
    AKGENPIPIF FNQGMGDSTL EFHSILSFGV ESSIKYSNSI KEMVILFATT 1300
    IYRIGLKVPP DERDPRVPML TWSTCAFTIQ AIENLLGDEG KPLFGALQNR 1350
    QHNGLKALMQ FAVAQRITCP QVLIQKHLVR LLSVVLPNIK SEDTPCLLSI 1400
    DLFHVLVGAV LAFPSLYWDD PVDLQPSSVS SSYNHLYLFH LITMAHMLQI 1450
    LLTVDTGLPL AQVQEDSEEA HSASSFFAEI SQYTSGSIGC DIPGWYLWVS 1500
    LKNGITPYLR CAALFFHYLL GVTPPEELHT NSAEGEYSAL CSYLSLPTNL 1550
    FLLFQEYWDT VRPLLQRWCA DPALLNCLKQ KNTVVRYPRK RNSLIELPDD 1600
    YSCLLNQASH FRCPRSADDE RKHPVLCLFC GAILCSQNIC CQEIVNGEEV 1650
    GACIFHALHC GAGVCIFLKI RECRVVLVEG KARGCAYPAP YLDEYGETDP 1700
    GLKRGNPLHL SRERYRKLHL VWQQHCIIEE IARSQETNQM LFGFNWQLL 1749
    Length:1,749
    Mass (Da):200,211
    Last modified:March 1, 2003 - v1
    Checksum:i3AE0E1A749884971
    GO
    Isoform 2 (identifier: Q8IWV7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         795-803: NNETGLENV → TRCIRPWSL
         804-1749: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:803
    Mass (Da):93,184
    Checksum:i8E6D0EAA152D2906
    GO

    Sequence cautioni

    The sequence BAB55380.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti201 – 2011V → A(PubMed:14702039)Curated
    Sequence conflicti900 – 9001D → N in AAC39845. (PubMed:9653112)Curated
    Sequence conflicti973 – 9731D → T in AAO14997. (PubMed:12434312)Curated
    Sequence conflicti993 – 9931C → S in AAC23677. (PubMed:9653112)Curated
    Sequence conflicti1710 – 171910LSRERYRKLH → FLVSGTEAP(PubMed:12434312)Curated
    Sequence conflicti1722 – 17221W → R(PubMed:12434312)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti136 – 1361H → R in JBS; prevents proper folding of the UBR-type zinc finger. 2 Publications
    VAR_024741
    Natural varianti596 – 5961K → M.
    Corresponds to variant rs34568456 [ dbSNP | Ensembl ].
    VAR_034467
    Natural varianti899 – 8991I → V.
    Corresponds to variant rs35069201 [ dbSNP | Ensembl ].
    VAR_052116
    Natural varianti1279 – 12791G → S in JBS. 1 Publication
    VAR_024742
    Natural varianti1548 – 15481T → A.
    Corresponds to variant rs3917223 [ dbSNP | Ensembl ].
    VAR_061822

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei795 – 8039NNETGLENV → TRCIRPWSL in isoform 2. 1 PublicationVSP_015164
    Alternative sequencei804 – 1749946Missing in isoform 2. 1 PublicationVSP_015165Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY061886 mRNA. Translation: AAL32103.1.
    BC113505 mRNA. Translation: AAI13506.1.
    BC113507 mRNA. Translation: AAI13508.1.
    AF525401 mRNA. Translation: AAO14997.1.
    AK027803 mRNA. Translation: BAB55380.1. Different initiation.
    CR749326 mRNA. Translation: CAH18181.1.
    AF061556 mRNA. Translation: AAC39845.1.
    AH006181 Genomic DNA. Translation: AAC23677.1.
    CCDSiCCDS10091.1. [Q8IWV7-1]
    RefSeqiNP_777576.1. NM_174916.2. [Q8IWV7-1]
    UniGeneiHs.591121.

    Genome annotation databases

    EnsembliENST00000290650; ENSP00000290650; ENSG00000159459. [Q8IWV7-1]
    ENST00000569066; ENSP00000456327; ENSG00000159459.
    GeneIDi197131.
    KEGGihsa:197131.
    UCSCiuc001zqq.3. human. [Q8IWV7-1]

    Polymorphism databases

    DMDMi73622071.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY061886 mRNA. Translation: AAL32103.1 .
    BC113505 mRNA. Translation: AAI13506.1 .
    BC113507 mRNA. Translation: AAI13508.1 .
    AF525401 mRNA. Translation: AAO14997.1 .
    AK027803 mRNA. Translation: BAB55380.1 . Different initiation.
    CR749326 mRNA. Translation: CAH18181.1 .
    AF061556 mRNA. Translation: AAC39845.1 .
    AH006181 Genomic DNA. Translation: AAC23677.1 .
    CCDSi CCDS10091.1. [Q8IWV7-1 ]
    RefSeqi NP_777576.1. NM_174916.2. [Q8IWV7-1 ]
    UniGenei Hs.591121.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3NY1 X-ray 2.08 A/B 97-168 [» ]
    ProteinModelPortali Q8IWV7.
    SMRi Q8IWV7. Positions 97-167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128238. 47 interactions.
    DIPi DIP-47033N.
    IntActi Q8IWV7. 29 interactions.
    MINTi MINT-1417571.
    STRINGi 9606.ENSP00000290650.

    PTM databases

    PhosphoSitei Q8IWV7.

    Polymorphism databases

    DMDMi 73622071.

    Proteomic databases

    MaxQBi Q8IWV7.
    PaxDbi Q8IWV7.
    PRIDEi Q8IWV7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290650 ; ENSP00000290650 ; ENSG00000159459 . [Q8IWV7-1 ]
    ENST00000569066 ; ENSP00000456327 ; ENSG00000159459 .
    GeneIDi 197131.
    KEGGi hsa:197131.
    UCSCi uc001zqq.3. human. [Q8IWV7-1 ]

    Organism-specific databases

    CTDi 197131.
    GeneCardsi GC15M043235.
    HGNCi HGNC:16808. UBR1.
    HPAi HPA038838.
    MIMi 243800. phenotype.
    605981. gene.
    neXtProti NX_Q8IWV7.
    Orphaneti 2315. Johanson-Blizzard syndrome.
    PharmGKBi PA38187.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG310244.
    HOVERGENi HBG080426.
    InParanoidi Q8IWV7.
    KOi K10625.
    OMAi ICLKEEA.
    OrthoDBi EOG7RNJZB.
    PhylomeDBi Q8IWV7.
    TreeFami TF323875.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    EvolutionaryTracei Q8IWV7.
    GeneWikii UBR1.
    GenomeRNAii 197131.
    NextBioi 89608.
    PROi Q8IWV7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IWV7.
    Bgeei Q8IWV7.
    CleanExi HS_UBR1.
    Genevestigatori Q8IWV7.

    Family and domain databases

    Gene3Di 3.30.1390.10. 1 hit.
    3.30.40.10. 2 hits.
    InterProi IPR003769. ClpS_core.
    IPR014719. Ribosomal_L7/12_C/ClpS-like.
    IPR003126. Znf_N-recognin.
    IPR013993. Znf_N-recognin_met.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF02617. ClpS. 1 hit.
    PF02207. zf-UBR. 1 hit.
    [Graphical view ]
    SMARTi SM00396. ZnF_UBR1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54736. SSF54736. 1 hit.
    PROSITEi PS51157. ZF_UBR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Regulation of protein catabolism by muscle-specific and cytokine-inducible ubiquitin ligase E3alpha-II during cancer cachexia."
      Kwak K.S., Zhou X., Solomon V., Baracos V.E., Davis J., Bannon A.W., Boyle W.J., Lacey D.L., Han H.Q.
      Cancer Res. 64:8193-8198(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION.
    2. "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: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-1727 (ISOFORM 1).
      Tissue: Erythroid cell.
    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] OF 166-1014 (ISOFORM 1).
      Tissue: Placenta.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 656-1749 (ISOFORM 2).
      Tissue: Heart.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 702-1034 (ISOFORM 1), TISSUE SPECIFICITY.
    7. "RECQL4, mutated in the Rothmund-Thomson and RAPADILINO syndromes, interacts with ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway."
      Yin J., Kwon Y.T., Varshavsky A., Wang W.
      Hum. Mol. Genet. 13:2421-2430(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RECQL4, IDENTIFICATION BY MASS SPECTROMETRY.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Role of N-end rule ubiquitin ligases UBR1 and UBR2 in regulating the leucine-mTOR signaling pathway."
      Kume K., Iizumi Y., Shimada M., Ito Y., Kishi T., Yamaguchi Y., Handa H.
      Genes Cells 15:339-349(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Structural basis of substrate recognition and specificity in the N-end rule pathway."
      Matta-Camacho E., Kozlov G., Li F.F., Gehring K.
      Nat. Struct. Mol. Biol. 17:1182-1187(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 98-167 ALONE AND IN COMPLEX WITH N-END RULE PEPTIDE, UBR-TYPE ZINC-FINGER, FUNCTION, VARIANT JB5 ARG-136.
    14. Cited for: VARIANTS JBS ARG-136 AND SER-1279, FUNCTION, DISEASE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiUBR1_HUMAN
    AccessioniPrimary (citable) accession number: Q8IWV7
    Secondary accession number(s): O60708
    , O75492, Q14D45, Q68DN9, Q8IWY6, Q96JY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 102 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 15
      Human chromosome 15: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3