SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8IWV7

- UBR1_HUMAN

UniProt

Q8IWV7 - UBR1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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-typeAdd
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
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 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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 RECQL4.1 Publication

Protein-protein interaction databases

BioGridi128238. 45 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.

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.

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.

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. VSP_015164
Alternative sequencei804 – 1749946Missing in isoform 2. VSP_015165Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011V → A1 Publication
Sequence conflicti900 – 9001D → N in AAC39845. 1 Publication
Sequence conflicti973 – 9731D → T in AAO14997. 1 Publication
Sequence conflicti993 – 9931C → S in AAC23677. 1 Publication
Sequence conflicti1710 – 171910LSRERYRKLH → FLVSGTEAP1 Publication
Sequence conflicti1722 – 17221W → R1 Publication

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]
ENST00000382177; ENSP00000371612; ENSG00000159459. [Q8IWV7-2]
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. 45 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 ]
ENST00000382177 ; ENSP00000371612 ; ENSG00000159459 . [Q8IWV7-2 ]
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

« 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. "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: September 3, 2014
This is version 101 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

Similar proteinsi