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Q8IWV7 (UBR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:UBR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1749 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.12 Ref.13 Ref.14

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with RECQL4. Ref.7

Subcellular location

Cytoplasmcytosol Ref.14.

Tissue specificity

Broadly expressed, with highest levels in skeletal muscle, kidney and pancreas. Present in acinar cells of the pancreas (at protein level). Ref.1 Ref.6 Ref.14

Developmental stage

Expressed in fetal pancreas. Ref.14

Domain

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.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Sequence similarities

Belongs to the UBR1 family.

Contains 1 RING-type zinc finger.

Contains 1 UBR-type zinc finger.

Sequence caution

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IWV7-1)

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.
Isoform 2 (identifier: Q8IWV7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     795-803: NNETGLENV → TRCIRPWSL
     804-1749: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 17491748E3 ubiquitin-protein ligase UBR1
PRO_0000056136

Regions

Zinc finger97 – 16872UBR-type
Zinc finger1098 – 1201104RING-type; atypical
Compositional bias864 – 8696Poly-Pro

Amino acid modifications

Modified residue21N-acetylalanine Ref.10
Modified residue211Phosphothreonine Ref.9 Ref.10 Ref.11
Modified residue11791Phosphoserine Ref.8

Natural variations

Alternative sequence795 – 8039NNETGLENV → TRCIRPWSL in isoform 2.
VSP_015164
Alternative sequence804 – 1749946Missing in isoform 2.
VSP_015165
Natural variant1361H → R in JBS; prevents proper folding of the UBR-type zinc finger. Ref.13 Ref.14
VAR_024741
Natural variant5961K → M.
Corresponds to variant rs34568456 [ dbSNP | Ensembl ].
VAR_034467
Natural variant8991I → V.
Corresponds to variant rs35069201 [ dbSNP | Ensembl ].
VAR_052116
Natural variant12791G → S in JBS. Ref.14
VAR_024742
Natural variant15481T → A.
Corresponds to variant rs3917223 [ dbSNP | Ensembl ].
VAR_061822

Experimental info

Sequence conflict2011V → A Ref.4
Sequence conflict9001D → N in AAC39845. Ref.6
Sequence conflict9731D → T in AAO14997. Ref.3
Sequence conflict9931C → S in AAC23677. Ref.6
Sequence conflict1710 – 171910LSRERYRKLH → FLVSGTEAP Ref.3
Sequence conflict17221W → R Ref.3

Secondary structure

............... 1749
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 3AE0E1A749884971

FASTA1,749200,211
        10         20         30         40         50         60 
MADEEAGGTE RMEISAELPQ TPQRLASWWD QQVDFYTAFL HHLAQLVPEI YFAEMDPDLE 

        70         80         90        100        110        120 
KQEESVQMSI FTPLEWYLFG EDPDICLEKL KHSGAFQLCG RVFKSGETTY SCRDCAIDPT 

       130        140        150        160        170        180 
CVLCMDCFQD SVHKNHRYKM HTSTGGGFCD CGDTEAWKTG PFCVNHEPGR AGTIKENSRC 

       190        200        210        220        230        240 
PLNEEVIVQA RKIFPSVIKY VVEMTIWEEE KELPPELQIR EKNERYYCVL FNDEHHSYDH 

       250        260        270        280        290        300 
VIYSLQRALD CELAEAQLHT TAIDKEGRRA VKAGAYAACQ EAKEDIKSHS ENVSQHPLHV 

       310        320        330        340        350        360 
EVLHSEIMAH QKFALRLGSW MNKIMSYSSD FRQIFCQACL REEPDSENPC LISRLMLWDA 

       370        380        390        400        410        420 
KLYKGARKIL HELIFSSFFM EMEYKKLFAM EFVKYYKQLQ KEYISDDHDR SISITALSVQ 

       430        440        450        460        470        480 
MFTVPTLARH LIEEQNVISV ITETLLEVLP EYLDRNNKFN FQGYSQDKLG RVYAVICDLK 

       490        500        510        520        530        540 
YILISKPTIW TERLRMQFLE GFRSFLKILT CMQGMEEIRR QVGQHIEVDP DWEAAIAIQM 

       550        560        570        580        590        600 
QLKNILLMFQ EWCACDEELL LVAYKECHKA VMRCSTSFIS SSKTVVQSCG HSLETKSYRV 

       610        620        630        640        650        660 
SEDLVSIHLP LSRTLAGLHV RLSRLGAVSR LHEFVSFEDF QVEVLVEYPL RCLVLVAQVV 

       670        680        690        700        710        720 
AEMWRRNGLS LISQVFYYQD VKCREEMYDK DIIMLQIGAS LMDPNKFLLL VLQRYELAEA 

       730        740        750        760        770        780 
FNKTISTKDQ DLIKQYNTLI EEMLQVLIYI VGERYVPGVG NVTKEEVTMR EIIHLLCIEP 

       790        800        810        820        830        840 
MPHSAIAKNL PENENNETGL ENVINKVATF KKPGVSGHGV YELKDESLKD FNMYFYHYSK 

       850        860        870        880        890        900 
TQHSKAEHMQ KKRRKQENKD EALPPPPPPE FCPAFSKVIN LLNCDIMMYI LRTVFERAID 

       910        920        930        940        950        960 
TDSNLWTEGM LQMAFHILAL GLLEEKQQLQ KAPEEEVTFD FYHKASRLGS SAMNIQMLLE 

       970        980        990       1000       1010       1020 
KLKGIPQLEG QKDMITWILQ MFDTVKRLRE KSCLIVATTS GSESIKNDEI THDKEKAERK 

      1030       1040       1050       1060       1070       1080 
RKAEAARLHR QKIMAQMSAL QKNFIETHKL MYDNTSEMPG KEDSIMEEES TPAVSDYSRI 

      1090       1100       1110       1120       1130       1140 
ALGPKRGPSV TEKEVLTCIL CQEEQEVKIE NNAMVLSACV QKSTALTQHR GKPIELSGEA 

      1150       1160       1170       1180       1190       1200 
LDPLFMDPDL AYGTYTGSCG HVMHAVCWQK YFEAVQLSSQ QRIHVDLFDL ESGEYLCPLC 

      1210       1220       1230       1240       1250       1260 
KSLCNTVIPI IPLQPQKINS ENADALAQLL TLARWIQTVL ARISGYNIRH AKGENPIPIF 

      1270       1280       1290       1300       1310       1320 
FNQGMGDSTL EFHSILSFGV ESSIKYSNSI KEMVILFATT IYRIGLKVPP DERDPRVPML 

      1330       1340       1350       1360       1370       1380 
TWSTCAFTIQ AIENLLGDEG KPLFGALQNR QHNGLKALMQ FAVAQRITCP QVLIQKHLVR 

      1390       1400       1410       1420       1430       1440 
LLSVVLPNIK SEDTPCLLSI DLFHVLVGAV LAFPSLYWDD PVDLQPSSVS SSYNHLYLFH 

      1450       1460       1470       1480       1490       1500 
LITMAHMLQI LLTVDTGLPL AQVQEDSEEA HSASSFFAEI SQYTSGSIGC DIPGWYLWVS 

      1510       1520       1530       1540       1550       1560 
LKNGITPYLR CAALFFHYLL GVTPPEELHT NSAEGEYSAL CSYLSLPTNL FLLFQEYWDT 

      1570       1580       1590       1600       1610       1620 
VRPLLQRWCA DPALLNCLKQ KNTVVRYPRK RNSLIELPDD YSCLLNQASH FRCPRSADDE 

      1630       1640       1650       1660       1670       1680 
RKHPVLCLFC GAILCSQNIC CQEIVNGEEV GACIFHALHC GAGVCIFLKI RECRVVLVEG 

      1690       1700       1710       1720       1730       1740 
KARGCAYPAP YLDEYGETDP GLKRGNPLHL SRERYRKLHL VWQQHCIIEE IARSQETNQM 


LFGFNWQLL 

« Hide

Isoform 2 [UniParc].

Checksum: 8E6D0EAA152D2906
Show »

FASTA80393,184

References

« Hide 'large scale' references
[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]"Congenital dyserythropoietic anemia type I is caused by mutations in codanin-1."
Dgany O., Avidan N., Delaunay J., Krasnov T., Shalmon L., Shalev H., Eidelitz-Markus T., Kapelushnik J., Cattan D., Pariente A., Tulliez M., Cretien A., Schischmanoff P.-O., Iolascon A., Fibach E., Koren A., Roessler J., Le Merrer M. expand/collapse author list , Yaniv I., Zaizov R., Ben-Asher E., Olender T., Lancet D., Beckmann J.S., Tamary H.
Am. J. Hum. Genet. 71:1467-1474(2002) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 656-1749 (ISOFORM 2).
Tissue: Heart.
[6]"The mouse and human genes encoding the recognition component of the N-end rule pathway."
Kwon Y.T., Reiss Y., Fried V.A., Hershko A., Yoon J.K., Gonda D.K., Sangan P., Copeland N.G., Jenkins N.A., Varshavsky A.
Proc. Natl. Acad. Sci. U.S.A. 95:7898-7903(1998) [PubMed] [Europe PMC] [Abstract]
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway, causes pancreatic dysfunction, malformations and mental retardation (Johanson-Blizzard syndrome)."
Zenker M., Mayerle J., Lerch M.M., Tagariello A., Zerres K., Durie P.R., Beier M., Hulskamp G., Guzman C., Rehder H., Beemer F.A., Hamel B.C.J., Vanlieferinghen P., Gershoni-Baruch R., Vieira M.W., Dumic M., Auslender R., Gil-da-Silva-Lopes V.L. expand/collapse author list , Steinlicht S., Rauh M., Shalev S.A., Thiel C., Winterpacht A., Kwon Y.T., Varshavsky A., Reis A.
Nat. Genet. 37:1345-1350(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS JBS ARG-136 AND SER-1279, FUNCTION, DISEASE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10091.1. [Q8IWV7-1]
RefSeqNP_777576.1. NM_174916.2. [Q8IWV7-1]
UniGeneHs.591121.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3NY1X-ray2.08A/B97-168[»]
ProteinModelPortalQ8IWV7.
SMRQ8IWV7. Positions 97-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128238. 45 interactions.
DIPDIP-47033N.
IntActQ8IWV7. 29 interactions.
MINTMINT-1417571.
STRING9606.ENSP00000290650.

PTM databases

PhosphoSiteQ8IWV7.

Polymorphism databases

DMDM73622071.

Proteomic databases

MaxQBQ8IWV7.
PaxDbQ8IWV7.
PRIDEQ8IWV7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290650; ENSP00000290650; ENSG00000159459. [Q8IWV7-1]
ENST00000382177; ENSP00000371612; ENSG00000159459. [Q8IWV7-2]
ENST00000569066; ENSP00000456327; ENSG00000159459.
GeneID197131.
KEGGhsa:197131.
UCSCuc001zqq.3. human. [Q8IWV7-1]

Organism-specific databases

CTD197131.
GeneCardsGC15M043235.
HGNCHGNC:16808. UBR1.
HPAHPA038838.
MIM243800. phenotype.
605981. gene.
neXtProtNX_Q8IWV7.
Orphanet2315. Johanson-Blizzard syndrome.
PharmGKBPA38187.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG310244.
HOVERGENHBG080426.
InParanoidQ8IWV7.
KOK10625.
OMAICLKEEA.
OrthoDBEOG7RNJZB.
PhylomeDBQ8IWV7.
TreeFamTF323875.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ8IWV7.
BgeeQ8IWV7.
CleanExHS_UBR1.
GenevestigatorQ8IWV7.

Family and domain databases

Gene3D3.30.1390.10. 1 hit.
3.30.40.10. 2 hits.
InterProIPR003769. 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]
PfamPF02617. ClpS. 1 hit.
PF02207. zf-UBR. 1 hit.
[Graphical view]
SMARTSM00396. ZnF_UBR1. 1 hit.
[Graphical view]
SUPFAMSSF54736. SSF54736. 1 hit.
PROSITEPS51157. ZF_UBR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8IWV7.
GeneWikiUBR1.
GenomeRNAi197131.
NextBio89608.
PROQ8IWV7.
SOURCESearch...

Entry information

Entry nameUBR1_HUMAN
AccessionPrimary (citable) accession number: Q8IWV7
Secondary accession number(s): O60708 expand/collapse secondary AC list , O75492, Q14D45, Q68DN9, Q8IWY6, Q96JY4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM