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Q8IWV8 (UBR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase UBR2

EC=6.3.2.-
Alternative name(s):
N-recognin-2
Ubiquitin-protein ligase E3-alpha-2
Ubiquitin-protein ligase E3-alpha-II
Gene names
Name:UBR2
Synonyms:C6orf133, KIAA0349
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1755 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. Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth. Ref.1 Ref.10 Ref.14

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with UBE2B; promotes the UBE2B-H2A interaction and the ubiquitination of histone H2A by UBE2B and UBR2 By similarity. Interacts with RECQL4. Ref.6

Subcellular location

Nucleus By similarity. Note: Associated with chromatin during meiosis.

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.7

Developmental stage

Expressed in fetal pancreas. Ref.7

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.

Sequence similarities

Belongs to the UBR1 family.

Contains 1 RING-type zinc finger.

Contains 1 UBR-type zinc finger.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to leucine

Inferred from direct assay Ref.10. Source: UniProtKB

chromatin silencing

Inferred from sequence or structural similarity. Source: UniProtKB

histone H2A ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

male meiosis I

Inferred from electronic annotation. Source: Ensembl

negative regulation of TOR signaling

Inferred from mutant phenotype Ref.10. Source: UniProtKB

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchromatin

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

ubiquitin ligase complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionleucine binding

Inferred from direct assay Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 22190034. Source: IntAct

ubiquitin-protein transferase activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

vifP125043EBI-1237260,EBI-779991From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IWV8-1)

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: Q8IWV8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     397-439: QQLQRDFMED...MLITEENLMS → ERLQSDYVTD...ISAGRSGSPL
     440-1755: Missing.
Isoform 3 (identifier: Q8IWV8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-496: Missing.
     497-514: RQKFLEGFDAFLELLKCM → MYAGNIPIYKTESRSRNE
     1022-1071: SSRDKDKAER...ELFQQTLELD → HNFRVQGTKT...MKTKNSFSRH
     1072-1755: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q8IWV8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     397-426: QQLQRDFMEDDHERAVSVTALSVQFFTAPT → ERLQSDYVTDDHDREFSVADLSVQIFTVPS
Note: Derived from mouse cDNA data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 17551754E3 ubiquitin-protein ligase UBR2
PRO_0000056140

Regions

Zinc finger97 – 16872UBR-type
Zinc finger1108 – 1214107RING-type; atypical
Coiled coil1019 – 105436 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.12 Ref.13

Natural variations

Alternative sequence1 – 496496Missing in isoform 3.
VSP_015166
Alternative sequence397 – 43943QQLQR…ENLMS → ERLQSDYVTDDHDREFSVAD LSVQIFTVPSLFSISAGRSG SPL in isoform 2.
VSP_015167
Alternative sequence397 – 42630QQLQR…FTAPT → ERLQSDYVTDDHDREFSVAD LSVQIFTVPS in isoform 4.
VSP_017130
Alternative sequence440 – 17551316Missing in isoform 2.
VSP_015168
Alternative sequence497 – 51418RQKFL…LLKCM → MYAGNIPIYKTESRSRNE in isoform 3.
VSP_015169
Alternative sequence1022 – 107150SSRDK…TLELD → HNFRVQGTKTKLRGREKQRL PDCAEKRSWLRCLKCSGILL MKTKNSFSRH in isoform 3.
VSP_015170
Alternative sequence1072 – 1755684Missing in isoform 3.
VSP_015171
Natural variant1721E → D.
Corresponds to variant rs6905054 [ dbSNP | Ensembl ].
VAR_052117
Natural variant10951A → P.
Corresponds to variant rs6917033 [ dbSNP | Ensembl ].
VAR_059816
Natural variant10951A → S.
Corresponds to variant rs6917033 [ dbSNP | Ensembl ].
VAR_059817
Natural variant10951A → T. Ref.5
Corresponds to variant rs6917033 [ dbSNP | Ensembl ].
VAR_023283

Experimental info

Sequence conflict8641K → R in BAC86295. Ref.2

Secondary structure

................ 1755
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2003. Version 1.
Checksum: 04B14FCB13E21808

FASTA1,755200,538
        10         20         30         40         50         60 
MASELEPEVQ AIDRSLLECS AEEIAGKWLQ ATDLTREVYQ HLAHYVPKIY CRGPNPFPQK 

        70         80         90        100        110        120 
EDMLAQHVLL GPMEWYLCGE DPAFGFPKLE QANKPSHLCG RVFKVGEPTY SCRDCAVDPT 

       130        140        150        160        170        180 
CVLCMECFLG SIHRDHRYRM TTSGGGGFCD CGDTEAWKEG PYCQKHELNT SEIEEEEDPL 

       190        200        210        220        230        240 
VHLSEDVIAR TYNIFAITFR YAVEILTWEK ESELPADLEM VEKSDTYYCM LFNDEVHTYE 

       250        260        270        280        290        300 
QVIYTLQKAV NCTQKEAIGF ATTVDRDGRR SVRYGDFQYC EQAKSVIVRN TSRQTKPLKV 

       310        320        330        340        350        360 
QVMHSSIVAH QNFGLKLLSW LGSIIGYSDG LRRILCQVGL QEGPDGENSS LVDRLMLSDS 

       370        380        390        400        410        420 
KLWKGARSVY HQLFMSSLLM DLKYKKLFAV RFAKNYQQLQ RDFMEDDHER AVSVTALSVQ 

       430        440        450        460        470        480 
FFTAPTLARM LITEENLMSI IIKTFMDHLR HRDAQGRFQF ERYTALQAFK FRRVQSLILD 

       490        500        510        520        530        540 
LKYVLISKPT EWSDELRQKF LEGFDAFLEL LKCMQGMDPI TRQVGQHIEM EPEWEAAFTL 

       550        560        570        580        590        600 
QMKLTHVISM MQDWCASDEK VLIEAYKKCL AVLMQCHGGY TDGEQPITLS ICGHSVETIR 

       610        620        630        640        650        660 
YCVSQEKVSI HLPVSRLLAG LHVLLSKSEV AYKFPELLPL SELSPPMLIE HPLRCLVLCA 

       670        680        690        700        710        720 
QVHAGMWRRN GFSLVNQIYY YHNVKCRREM FDKDVVMLQT GVSMMDPNHF LMIMLSRFEL 

       730        740        750        760        770        780 
YQIFSTPDYG KRFSSEITHK DVVQQNNTLI EEMLYLIIML VGERFSPGVG QVNATDEIKR 

       790        800        810        820        830        840 
EIIHQLSIKP MAHSELVKSL PEDENKETGM ESVIEAVAHF KKPGLTGRGM YELKPECAKE 

       850        860        870        880        890        900 
FNLYFYHFSR AEQSKAEEAQ RKLKRQNRED TALPPPVLPP FCPLFASLVN ILQSDVMLCI 

       910        920        930        940        950        960 
MGTILQWAVE HNGYAWSESM LQRVLHLIGM ALQEEKQHLE NVTEEHVVTF TFTQKISKPG 

       970        980        990       1000       1010       1020 
EAPKNSPSIL AMLETLQNAP YLEVHKDMIR WILKTFNAVK KMRESSPTSP VAETEGTIME 

      1030       1040       1050       1060       1070       1080 
ESSRDKDKAE RKRKAEIARL RREKIMAQMS EMQRHFIDEN KELFQQTLEL DASTSAVLDH 

      1090       1100       1110       1120       1130       1140 
SPVASDMTLT ALGPAQTQVP EQRQFVTCIL CQEEQEVKVE SRAMVLAAFV QRSTVLSKNR 

      1150       1160       1170       1180       1190       1200 
SKFIQDPEKY DPLFMHPDLS CGTHTSSCGH IMHAHCWQRY FDSVQAKEQR RQQRLRLHTS 

      1210       1220       1230       1240       1250       1260 
YDVENGEFLC PLCECLSNTV IPLLLPPRNI FNNRLNFSDQ PNLTQWIRTI SQQIKALQFL 

      1270       1280       1290       1300       1310       1320 
RKEESTPNNA STKNSENVDE LQLPEGFRPD FRPKIPYSES IKEMLTTFGT ATYKVGLKVH 

      1330       1340       1350       1360       1370       1380 
PNEEDPRVPI MCWGSCAYTI QSIERILSDE DKPLFGPLPC RLDDCLRSLT RFAAAHWTVA 

      1390       1400       1410       1420       1430       1440 
SVSVVQGHFC KLFASLVPND SHEELPCILD IDMFHLLVGL VLAFPALQCQ DFSGISLGTG 

      1450       1460       1470       1480       1490       1500 
DLHIFHLVTM AHIIQILLTS CTEENGMDQE NPPCEEESAV LALYKTLHQY TGSALKEIPS 

      1510       1520       1530       1540       1550       1560 
GWHLWRSVRA GIMPFLKCSA LFFHYLNGVP SPPDIQVPGT SHFEHLCSYL SLPNNLICLF 

      1570       1580       1590       1600       1610       1620 
QENSEIMNSL IESWCRNSEV KRYLEGERDA IRYPRESNKL INLPEDYSSL INQASNFSCP 

      1630       1640       1650       1660       1670       1680 
KSGGDKSRAP TLCLVCGSLL CSQSYCCQTE LEGEDVGACT AHTYSCGSGV GIFLRVRECQ 

      1690       1700       1710       1720       1730       1740 
VLFLAGKTKG CFYSPPYLDD YGETDQGLRR GNPLHLCKER FKKIQKLWHQ HSVTEEIGHA 

      1750 
QEANQTLVGI DWQHL 

« Hide

Isoform 2 [UniParc].

Checksum: D1A9B29DF254AE1F
Show »

FASTA43949,978
Isoform 3 [UniParc].

Checksum: EC2722AF55B26BD3
Show »

FASTA57566,052
Isoform 4 [UniParc].

Checksum: 6FE8C7C600C162EE
Show »

FASTA1,755200,540

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]"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] (ISOFORM 3).
Tissue: Testis.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORM 2).
Tissue: Ovary.
[5]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 481-1755 (ISOFORMS 1/4), VARIANT THR-1095.
Tissue: Brain.
[6]"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.
[7]"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: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"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.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY061884 mRNA. Translation: AAL32101.1.
AK125795 mRNA. Translation: BAC86295.1.
AL049843, AL136223, AL391814 Genomic DNA. Translation: CAI20399.1.
AL049843, AL136223, AL391814 Genomic DNA. Translation: CAI95685.1.
AL136223, AL391814 Genomic DNA. Translation: CAI19919.1.
AL136223, AL049843, AL391814 Genomic DNA. Translation: CAI19920.1.
AL136223, AL049843, AL391814 Genomic DNA. Translation: CAI95666.1.
AL391814, AL136223 Genomic DNA. Translation: CAI14737.1.
AL391814, AL136223, AL049843 Genomic DNA. Translation: CAI14738.1.
AL391814, AL049843, AL136223 Genomic DNA. Translation: CAI95298.1.
BC024217 mRNA. Translation: AAH24217.1.
BC064512 mRNA. Translation: AAH64512.1.
AB002347 mRNA. Translation: BAA20806.1.
CCDSCCDS4870.1. [Q8IWV8-1]
CCDS55001.1. [Q8IWV8-2]
RefSeqNP_001171730.1. NM_001184801.1. [Q8IWV8-2]
NP_056070.1. NM_015255.2. [Q8IWV8-1]
XP_005249022.1. XM_005248965.2. [Q8IWV8-4]
UniGeneHs.529925.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3NY2X-ray2.61A/B/C/D/E/F/G/H98-167[»]
3NY3X-ray1.60A98-167[»]
ProteinModelPortalQ8IWV8.
SMRQ8IWV8. Positions 98-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116896. 15 interactions.
DIPDIP-38165N.
IntActQ8IWV8. 7 interactions.
STRING9606.ENSP00000361990.

PTM databases

PhosphoSiteQ8IWV8.

Polymorphism databases

DMDM73622073.

Proteomic databases

MaxQBQ8IWV8.
PaxDbQ8IWV8.
PRIDEQ8IWV8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372883; ENSP00000361974; ENSG00000024048. [Q8IWV8-3]
ENST00000372899; ENSP00000361990; ENSG00000024048. [Q8IWV8-1]
ENST00000372901; ENSP00000361992; ENSG00000024048. [Q8IWV8-4]
ENST00000372903; ENSP00000361994; ENSG00000024048. [Q8IWV8-2]
GeneID23304.
KEGGhsa:23304.
UCSCuc003osf.3. human. [Q8IWV8-2]
uc011dur.2. human. [Q8IWV8-1]
uc011dus.2. human. [Q8IWV8-4]

Organism-specific databases

CTD23304.
GeneCardsGC06P042531.
HGNCHGNC:21289. UBR2.
HPAHPA027869.
HPA027880.
MIM609134. gene.
neXtProtNX_Q8IWV8.
PharmGKBPA128394621.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG310244.
HOGENOMHOG000231769.
HOVERGENHBG080426.
KOK10626.
OMASHEELPC.
OrthoDBEOG7RNJZB.
PhylomeDBQ8IWV8.
TreeFamTF323875.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ8IWV8.
BgeeQ8IWV8.
CleanExHS_UBR2.
GenevestigatorQ8IWV8.

Family and domain databases

Gene3D3.30.1390.10. 1 hit.
InterProIPR003769. ClpS_core.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR003126. Znf_N-recognin.
IPR013993. Znf_N-recognin_met.
IPR001841. Znf_RING.
[Graphical view]
PfamPF02617. ClpS. 1 hit.
PF02207. zf-UBR. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
SM00396. ZnF_UBR1. 1 hit.
[Graphical view]
SUPFAMSSF54736. SSF54736. 1 hit.
PROSITEPS51157. ZF_UBR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8IWV8.
GeneWikiUBR2.
GenomeRNAi23304.
NextBio45149.
PROQ8IWV8.
SOURCESearch...

Entry information

Entry nameUBR2_HUMAN
AccessionPrimary (citable) accession number: Q8IWV8
Secondary accession number(s): O15057 expand/collapse secondary AC list , Q4VXK2, Q5TFH6, Q6P2I2, Q6ZUD0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 110 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 6

Human chromosome 6: entries, gene names and cross-references to MIM