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Q8IWV8

- UBR2_HUMAN

UniProt

Q8IWV8 - UBR2_HUMAN

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Protein
E3 ubiquitin-protein ligase UBR2
Gene
UBR2, C6orf133, KIAA0349
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. 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.3 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri97 – 16872UBR-type
Add
BLAST
Zinc fingeri1108 – 1214107RING-type; atypical
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. cellular response to leucine Source: UniProtKB
  2. chromatin silencing Source: UniProtKB
  3. histone H2A ubiquitination Source: UniProtKB
  4. male meiosis I Source: Ensembl
  5. negative regulation of TOR signaling Source: UniProtKB
  6. spermatogenesis Source: Ensembl
  7. ubiquitin-dependent protein catabolic process Source: Ensembl
Complete GO annotation...

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 UBR2 (EC:6.3.2.-)
Alternative name(s):
N-recognin-2
Ubiquitin-protein ligase E3-alpha-2
Ubiquitin-protein ligase E3-alpha-II
Gene namesi
Name:UBR2
Synonyms:C6orf133, KIAA0349
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:21289. UBR2.

Subcellular locationi

Nucleus By similarity
Note: Associated with chromatin during meiosis.

GO - Cellular componenti

  1. chromatin Source: Ensembl
  2. nucleus Source: HPA
  3. plasma membrane Source: HPA
  4. ubiquitin ligase complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394621.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 17551754E3 ubiquitin-protein ligase UBR2
PRO_0000056140Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8IWV8.
PaxDbiQ8IWV8.
PRIDEiQ8IWV8.

PTM databases

PhosphoSiteiQ8IWV8.

Expressioni

Tissue specificityi

Broadly expressed, with highest levels in skeletal muscle, kidney and pancreas. Present in acinar cells of the pancreas (at protein level).2 Publications

Developmental stagei

Expressed in fetal pancreas.1 Publication

Gene expression databases

ArrayExpressiQ8IWV8.
BgeeiQ8IWV8.
CleanExiHS_UBR2.
GenevestigatoriQ8IWV8.

Organism-specific databases

HPAiHPA027869.
HPA027880.

Interactioni

Subunit structurei

Interacts with UBE2B; promotes the UBE2B-H2A interaction and the ubiquitination of histone H2A by UBE2B and UBR2 By similarity. Interacts with RECQL4.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
vifP125043EBI-1237260,EBI-779991From a different organism.

Protein-protein interaction databases

BioGridi116896. 15 interactions.
DIPiDIP-38165N.
IntActiQ8IWV8. 7 interactions.
STRINGi9606.ENSP00000361990.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi108 – 1125
Turni113 – 1153
Beta strandi116 – 1183
Helixi125 – 1295
Helixi132 – 1354
Beta strandi138 – 1425
Turni154 – 1563
Beta strandi157 – 1593
Turni164 – 1663

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NY2X-ray2.61A/B/C/D/E/F/G/H98-167[»]
3NY3X-ray1.60A98-167[»]
ProteinModelPortaliQ8IWV8.
SMRiQ8IWV8. Positions 98-167.

Miscellaneous databases

EvolutionaryTraceiQ8IWV8.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1019 – 105436 Reviewed prediction
Add
BLAST

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.

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG310244.
HOGENOMiHOG000231769.
HOVERGENiHBG080426.
KOiK10626.
OMAiSHEELPC.
OrthoDBiEOG7RNJZB.
PhylomeDBiQ8IWV8.
TreeFamiTF323875.

Family and domain databases

Gene3Di3.30.1390.10. 1 hit.
InterProiIPR003769. ClpS_core.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR003126. Znf_N-recognin.
IPR013993. Znf_N-recognin_met.
IPR001841. Znf_RING.
[Graphical view]
PfamiPF02617. ClpS. 1 hit.
PF02207. zf-UBR. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00396. ZnF_UBR1. 1 hit.
[Graphical view]
SUPFAMiSSF54736. SSF54736. 1 hit.
PROSITEiPS51157. ZF_UBR. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8IWV8-1) [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

MASELEPEVQ AIDRSLLECS AEEIAGKWLQ ATDLTREVYQ HLAHYVPKIY     50
CRGPNPFPQK EDMLAQHVLL GPMEWYLCGE DPAFGFPKLE QANKPSHLCG 100
RVFKVGEPTY SCRDCAVDPT CVLCMECFLG SIHRDHRYRM TTSGGGGFCD 150
CGDTEAWKEG PYCQKHELNT SEIEEEEDPL VHLSEDVIAR TYNIFAITFR 200
YAVEILTWEK ESELPADLEM VEKSDTYYCM LFNDEVHTYE QVIYTLQKAV 250
NCTQKEAIGF ATTVDRDGRR SVRYGDFQYC EQAKSVIVRN TSRQTKPLKV 300
QVMHSSIVAH QNFGLKLLSW LGSIIGYSDG LRRILCQVGL QEGPDGENSS 350
LVDRLMLSDS KLWKGARSVY HQLFMSSLLM DLKYKKLFAV RFAKNYQQLQ 400
RDFMEDDHER AVSVTALSVQ FFTAPTLARM LITEENLMSI IIKTFMDHLR 450
HRDAQGRFQF ERYTALQAFK FRRVQSLILD LKYVLISKPT EWSDELRQKF 500
LEGFDAFLEL LKCMQGMDPI TRQVGQHIEM EPEWEAAFTL QMKLTHVISM 550
MQDWCASDEK VLIEAYKKCL AVLMQCHGGY TDGEQPITLS ICGHSVETIR 600
YCVSQEKVSI HLPVSRLLAG LHVLLSKSEV AYKFPELLPL SELSPPMLIE 650
HPLRCLVLCA QVHAGMWRRN GFSLVNQIYY YHNVKCRREM FDKDVVMLQT 700
GVSMMDPNHF LMIMLSRFEL YQIFSTPDYG KRFSSEITHK DVVQQNNTLI 750
EEMLYLIIML VGERFSPGVG QVNATDEIKR EIIHQLSIKP MAHSELVKSL 800
PEDENKETGM ESVIEAVAHF KKPGLTGRGM YELKPECAKE FNLYFYHFSR 850
AEQSKAEEAQ RKLKRQNRED TALPPPVLPP FCPLFASLVN ILQSDVMLCI 900
MGTILQWAVE HNGYAWSESM LQRVLHLIGM ALQEEKQHLE NVTEEHVVTF 950
TFTQKISKPG EAPKNSPSIL AMLETLQNAP YLEVHKDMIR WILKTFNAVK 1000
KMRESSPTSP VAETEGTIME ESSRDKDKAE RKRKAEIARL RREKIMAQMS 1050
EMQRHFIDEN KELFQQTLEL DASTSAVLDH SPVASDMTLT ALGPAQTQVP 1100
EQRQFVTCIL CQEEQEVKVE SRAMVLAAFV QRSTVLSKNR SKFIQDPEKY 1150
DPLFMHPDLS CGTHTSSCGH IMHAHCWQRY FDSVQAKEQR RQQRLRLHTS 1200
YDVENGEFLC PLCECLSNTV IPLLLPPRNI FNNRLNFSDQ PNLTQWIRTI 1250
SQQIKALQFL RKEESTPNNA STKNSENVDE LQLPEGFRPD FRPKIPYSES 1300
IKEMLTTFGT ATYKVGLKVH PNEEDPRVPI MCWGSCAYTI QSIERILSDE 1350
DKPLFGPLPC RLDDCLRSLT RFAAAHWTVA SVSVVQGHFC KLFASLVPND 1400
SHEELPCILD IDMFHLLVGL VLAFPALQCQ DFSGISLGTG DLHIFHLVTM 1450
AHIIQILLTS CTEENGMDQE NPPCEEESAV LALYKTLHQY TGSALKEIPS 1500
GWHLWRSVRA GIMPFLKCSA LFFHYLNGVP SPPDIQVPGT SHFEHLCSYL 1550
SLPNNLICLF QENSEIMNSL IESWCRNSEV KRYLEGERDA IRYPRESNKL 1600
INLPEDYSSL INQASNFSCP KSGGDKSRAP TLCLVCGSLL CSQSYCCQTE 1650
LEGEDVGACT AHTYSCGSGV GIFLRVRECQ VLFLAGKTKG CFYSPPYLDD 1700
YGETDQGLRR GNPLHLCKER FKKIQKLWHQ HSVTEEIGHA QEANQTLVGI 1750
DWQHL 1755
Length:1,755
Mass (Da):200,538
Last modified:March 1, 2003 - v1
Checksum:i04B14FCB13E21808
GO
Isoform 2 (identifier: Q8IWV8-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:439
Mass (Da):49,978
Checksum:iD1A9B29DF254AE1F
GO
Isoform 3 (identifier: Q8IWV8-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:575
Mass (Da):66,052
Checksum:iEC2722AF55B26BD3
GO
Isoform 4 (identifier: Q8IWV8-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,755
Mass (Da):200,540
Checksum:i6FE8C7C600C162EE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti172 – 1721E → D.
Corresponds to variant rs6905054 [ dbSNP | Ensembl ].
VAR_052117
Natural varianti1095 – 10951A → P.
Corresponds to variant rs6917033 [ dbSNP | Ensembl ].
VAR_059816
Natural varianti1095 – 10951A → S.
Corresponds to variant rs6917033 [ dbSNP | Ensembl ].
VAR_059817
Natural varianti1095 – 10951A → T.1 Publication
Corresponds to variant rs6917033 [ dbSNP | Ensembl ].
VAR_023283

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 496496Missing in isoform 3.
VSP_015166Add
BLAST
Alternative sequencei397 – 43943QQLQR…ENLMS → ERLQSDYVTDDHDREFSVAD LSVQIFTVPSLFSISAGRSG SPL in isoform 2.
VSP_015167Add
BLAST
Alternative sequencei397 – 42630QQLQR…FTAPT → ERLQSDYVTDDHDREFSVAD LSVQIFTVPS in isoform 4.
VSP_017130Add
BLAST
Alternative sequencei440 – 17551316Missing in isoform 2.
VSP_015168Add
BLAST
Alternative sequencei497 – 51418RQKFL…LLKCM → MYAGNIPIYKTESRSRNE in isoform 3.
VSP_015169Add
BLAST
Alternative sequencei1022 – 107150SSRDK…TLELD → HNFRVQGTKTKLRGREKQRL PDCAEKRSWLRCLKCSGILL MKTKNSFSRH in isoform 3.
VSP_015170Add
BLAST
Alternative sequencei1072 – 1755684Missing in isoform 3.
VSP_015171Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti864 – 8641K → R in BAC86295. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4870.1. [Q8IWV8-1]
CCDS55001.1. [Q8IWV8-2]
RefSeqiNP_001171730.1. NM_001184801.1. [Q8IWV8-2]
NP_056070.1. NM_015255.2. [Q8IWV8-1]
XP_005249022.1. XM_005248965.2. [Q8IWV8-4]
UniGeneiHs.529925.

Genome annotation databases

EnsembliENST00000372883; ENSP00000361974; ENSG00000024048. [Q8IWV8-3]
ENST00000372899; ENSP00000361990; ENSG00000024048. [Q8IWV8-1]
ENST00000372901; ENSP00000361992; ENSG00000024048. [Q8IWV8-4]
ENST00000372903; ENSP00000361994; ENSG00000024048. [Q8IWV8-2]
GeneIDi23304.
KEGGihsa:23304.
UCSCiuc003osf.3. human. [Q8IWV8-2]
uc011dur.2. human. [Q8IWV8-1]
uc011dus.2. human. [Q8IWV8-4]

Polymorphism databases

DMDMi73622073.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4870.1. [Q8IWV8-1 ]
CCDS55001.1. [Q8IWV8-2 ]
RefSeqi NP_001171730.1. NM_001184801.1. [Q8IWV8-2 ]
NP_056070.1. NM_015255.2. [Q8IWV8-1 ]
XP_005249022.1. XM_005248965.2. [Q8IWV8-4 ]
UniGenei Hs.529925.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3NY2 X-ray 2.61 A/B/C/D/E/F/G/H 98-167 [» ]
3NY3 X-ray 1.60 A 98-167 [» ]
ProteinModelPortali Q8IWV8.
SMRi Q8IWV8. Positions 98-167.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116896. 15 interactions.
DIPi DIP-38165N.
IntActi Q8IWV8. 7 interactions.
STRINGi 9606.ENSP00000361990.

PTM databases

PhosphoSitei Q8IWV8.

Polymorphism databases

DMDMi 73622073.

Proteomic databases

MaxQBi Q8IWV8.
PaxDbi Q8IWV8.
PRIDEi Q8IWV8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000372883 ; ENSP00000361974 ; ENSG00000024048 . [Q8IWV8-3 ]
ENST00000372899 ; ENSP00000361990 ; ENSG00000024048 . [Q8IWV8-1 ]
ENST00000372901 ; ENSP00000361992 ; ENSG00000024048 . [Q8IWV8-4 ]
ENST00000372903 ; ENSP00000361994 ; ENSG00000024048 . [Q8IWV8-2 ]
GeneIDi 23304.
KEGGi hsa:23304.
UCSCi uc003osf.3. human. [Q8IWV8-2 ]
uc011dur.2. human. [Q8IWV8-1 ]
uc011dus.2. human. [Q8IWV8-4 ]

Organism-specific databases

CTDi 23304.
GeneCardsi GC06P042531.
HGNCi HGNC:21289. UBR2.
HPAi HPA027869.
HPA027880.
MIMi 609134. gene.
neXtProti NX_Q8IWV8.
PharmGKBi PA128394621.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG310244.
HOGENOMi HOG000231769.
HOVERGENi HBG080426.
KOi K10626.
OMAi SHEELPC.
OrthoDBi EOG7RNJZB.
PhylomeDBi Q8IWV8.
TreeFami TF323875.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTracei Q8IWV8.
GeneWikii UBR2.
GenomeRNAii 23304.
NextBioi 45149.
PROi Q8IWV8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8IWV8.
Bgeei Q8IWV8.
CleanExi HS_UBR2.
Genevestigatori Q8IWV8.

Family and domain databases

Gene3Di 3.30.1390.10. 1 hit.
InterProi IPR003769. ClpS_core.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR003126. Znf_N-recognin.
IPR013993. Znf_N-recognin_met.
IPR001841. Znf_RING.
[Graphical view ]
Pfami PF02617. ClpS. 1 hit.
PF02207. zf-UBR. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
SM00396. ZnF_UBR1. 1 hit.
[Graphical view ]
SUPFAMi SSF54736. SSF54736. 1 hit.
PROSITEi PS51157. ZF_UBR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  8. 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. 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. 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.

Entry informationi

Entry nameiUBR2_HUMAN
AccessioniPrimary (citable) accession number: Q8IWV8
Secondary accession number(s): O15057
, Q4VXK2, Q5TFH6, Q6P2I2, Q6ZUD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 111 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 6
    Human chromosome 6: 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

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