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Protein

E3 ubiquitin-protein ligase UBR1

Gene

UBR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1098 – 1201104RING-type; atypicalAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.17.20. 2681.
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 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:16808. UBR1.

Subcellular locationi

  1. 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)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionThis 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.

See also OMIM:243800
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.

Polymorphism and mutation databases

BioMutaiUBR1.
DMDMi73622071.

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 – 211Phosphothreonine4 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

BgeeiQ8IWV7.
CleanExiHS_UBR1.
ExpressionAtlasiQ8IWV7. baseline and differential.
GenevestigatoriQ8IWV7.

Organism-specific databases

HPAiHPA038838.

Interactioni

Subunit structurei

Interacts with RECQL4.2 Publications

Protein-protein interaction databases

BioGridi128238. 59 interactions.
DIPiDIP-47033N.
IntActiQ8IWV7. 30 interactions.
MINTiMINT-1417571.
STRINGi9606.ENSP00000290650.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ8IWV7.

Family & Domainsi

Compositional bias

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

Domaini

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

Sequence similaritiesi

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

Zinc finger

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

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG310244.
GeneTreeiENSGT00530000063055.
HOVERGENiHBG080426.
InParanoidiQ8IWV7.
KOiK10625.
OMAiYDLRYVL.
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. AlignAdd to basket

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

        10         20         30         40         50
MADEEAGGTE RMEISAELPQ TPQRLASWWD QQVDFYTAFL HHLAQLVPEI
60 70 80 90 100
YFAEMDPDLE KQEESVQMSI FTPLEWYLFG EDPDICLEKL KHSGAFQLCG
110 120 130 140 150
RVFKSGETTY SCRDCAIDPT CVLCMDCFQD SVHKNHRYKM HTSTGGGFCD
160 170 180 190 200
CGDTEAWKTG PFCVNHEPGR AGTIKENSRC PLNEEVIVQA RKIFPSVIKY
210 220 230 240 250
VVEMTIWEEE KELPPELQIR EKNERYYCVL FNDEHHSYDH VIYSLQRALD
260 270 280 290 300
CELAEAQLHT TAIDKEGRRA VKAGAYAACQ EAKEDIKSHS ENVSQHPLHV
310 320 330 340 350
EVLHSEIMAH QKFALRLGSW MNKIMSYSSD FRQIFCQACL REEPDSENPC
360 370 380 390 400
LISRLMLWDA KLYKGARKIL HELIFSSFFM EMEYKKLFAM EFVKYYKQLQ
410 420 430 440 450
KEYISDDHDR SISITALSVQ MFTVPTLARH LIEEQNVISV ITETLLEVLP
460 470 480 490 500
EYLDRNNKFN FQGYSQDKLG RVYAVICDLK YILISKPTIW TERLRMQFLE
510 520 530 540 550
GFRSFLKILT CMQGMEEIRR QVGQHIEVDP DWEAAIAIQM QLKNILLMFQ
560 570 580 590 600
EWCACDEELL LVAYKECHKA VMRCSTSFIS SSKTVVQSCG HSLETKSYRV
610 620 630 640 650
SEDLVSIHLP LSRTLAGLHV RLSRLGAVSR LHEFVSFEDF QVEVLVEYPL
660 670 680 690 700
RCLVLVAQVV AEMWRRNGLS LISQVFYYQD VKCREEMYDK DIIMLQIGAS
710 720 730 740 750
LMDPNKFLLL VLQRYELAEA FNKTISTKDQ DLIKQYNTLI EEMLQVLIYI
760 770 780 790 800
VGERYVPGVG NVTKEEVTMR EIIHLLCIEP MPHSAIAKNL PENENNETGL
810 820 830 840 850
ENVINKVATF KKPGVSGHGV YELKDESLKD FNMYFYHYSK TQHSKAEHMQ
860 870 880 890 900
KKRRKQENKD EALPPPPPPE FCPAFSKVIN LLNCDIMMYI LRTVFERAID
910 920 930 940 950
TDSNLWTEGM LQMAFHILAL GLLEEKQQLQ KAPEEEVTFD FYHKASRLGS
960 970 980 990 1000
SAMNIQMLLE KLKGIPQLEG QKDMITWILQ MFDTVKRLRE KSCLIVATTS
1010 1020 1030 1040 1050
GSESIKNDEI THDKEKAERK RKAEAARLHR QKIMAQMSAL QKNFIETHKL
1060 1070 1080 1090 1100
MYDNTSEMPG KEDSIMEEES TPAVSDYSRI ALGPKRGPSV TEKEVLTCIL
1110 1120 1130 1140 1150
CQEEQEVKIE NNAMVLSACV QKSTALTQHR GKPIELSGEA LDPLFMDPDL
1160 1170 1180 1190 1200
AYGTYTGSCG HVMHAVCWQK YFEAVQLSSQ QRIHVDLFDL ESGEYLCPLC
1210 1220 1230 1240 1250
KSLCNTVIPI IPLQPQKINS ENADALAQLL TLARWIQTVL ARISGYNIRH
1260 1270 1280 1290 1300
AKGENPIPIF FNQGMGDSTL EFHSILSFGV ESSIKYSNSI KEMVILFATT
1310 1320 1330 1340 1350
IYRIGLKVPP DERDPRVPML TWSTCAFTIQ AIENLLGDEG KPLFGALQNR
1360 1370 1380 1390 1400
QHNGLKALMQ FAVAQRITCP QVLIQKHLVR LLSVVLPNIK SEDTPCLLSI
1410 1420 1430 1440 1450
DLFHVLVGAV LAFPSLYWDD PVDLQPSSVS SSYNHLYLFH LITMAHMLQI
1460 1470 1480 1490 1500
LLTVDTGLPL AQVQEDSEEA HSASSFFAEI SQYTSGSIGC DIPGWYLWVS
1510 1520 1530 1540 1550
LKNGITPYLR CAALFFHYLL GVTPPEELHT NSAEGEYSAL CSYLSLPTNL
1560 1570 1580 1590 1600
FLLFQEYWDT VRPLLQRWCA DPALLNCLKQ KNTVVRYPRK RNSLIELPDD
1610 1620 1630 1640 1650
YSCLLNQASH FRCPRSADDE RKHPVLCLFC GAILCSQNIC CQEIVNGEEV
1660 1670 1680 1690 1700
GACIFHALHC GAGVCIFLKI RECRVVLVEG KARGCAYPAP YLDEYGETDP
1710 1720 1730 1740
GLKRGNPLHL SRERYRKLHL VWQQHCIIEE IARSQETNQM LFGFNWQLL
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. Curated

Experimental Info

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

Natural variant

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

Alternative sequence

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
GeneIDi197131.
KEGGihsa:197131.
UCSCiuc001zqq.3. human. [Q8IWV7-1]

Polymorphism and mutation databases

BioMutaiUBR1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi128238. 59 interactions.
DIPiDIP-47033N.
IntActiQ8IWV7. 30 interactions.
MINTiMINT-1417571.
STRINGi9606.ENSP00000290650.

PTM databases

PhosphoSiteiQ8IWV7.

Polymorphism and mutation databases

BioMutaiUBR1.
DMDMi73622071.

Proteomic databases

MaxQBiQ8IWV7.
PaxDbiQ8IWV7.
PRIDEiQ8IWV7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi197131.
GeneCardsiGC15M043235.
HGNCiHGNC:16808. UBR1.
HPAiHPA038838.
MIMi243800. phenotype.
605981. gene.
neXtProtiNX_Q8IWV7.
Orphaneti2315. Johanson-Blizzard syndrome.
PharmGKBiPA38187.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG310244.
GeneTreeiENSGT00530000063055.
HOVERGENiHBG080426.
InParanoidiQ8IWV7.
KOiK10625.
OMAiYDLRYVL.
OrthoDBiEOG7RNJZB.
PhylomeDBiQ8IWV7.
TreeFamiTF323875.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi3.4.17.20. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiQ8IWV7.
GeneWikiiUBR1.
GenomeRNAii197131.
NextBioi89608.
PROiQ8IWV7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IWV7.
CleanExiHS_UBR1.
ExpressionAtlasiQ8IWV7. baseline and differential.
GenevestigatoriQ8IWV7.

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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  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, VARIANT JB5 ARG-136.
  15. 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: April 29, 2015
This is version 108 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.