Q9VX91

PR
Gene name
Ubr1
Protein name
E3 ubiquitin-protein ligase UBR1
Names
N-recognin, RING-type E3 ubiquitin transferase UBR1, Ubiquitin-protein ligase E3-alpha
Species
Drosophila melanogaster (Fruit fly)
KEGG Pathway
dme:Dmel_CG9086
EC number
2.3.2.27: Aminoacyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

983-1188 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9VX91

Entry ID Method Resolution Chain Position Source
AF-Q9VX91-F1 Predicted AlphaFoldDB

No variants for Q9VX91

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9VX91

No associated diseases with Q9VX91

3 regional properties for Q9VX91

Type Name Position InterPro Accession
domain Zinc finger, UBR-type 107 - 178 IPR003126
domain Adaptor protein ClpS, core 236 - 299 IPR003769
domain E3 ubiquitin-protein ligase UBR-like, C-terminal 1325 - 1798 IPR044046

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
ubiquitin ligase complex A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. The complex also contains other proteins that may confer substrate specificity on the complex.

3 GO annotations of molecular function

Name Definition
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
ubiquitin-protein transferase activity Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.
ubiquitin-dependent protein catabolic process via the N-end rule pathway The chemical reactions and pathways resulting in the breakdown of a protein or peptide covalently tagged with ubiquitin, via the N-end rule pathway. In the N-end rule pathway, destabilizing N-terminal residues (N-degrons) in substrates are recognized by E3 ligases (N-recognins), whereupon the substrates are linked to ubiquitin and then delivered to the proteasome for degradation.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P19812 UBR1 E3 ubiquitin-protein ligase UBR1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) EV
Q8IWV7 UBR1 E3 ubiquitin-protein ligase UBR1 Homo sapiens (Human) SS
Q8IWV8 UBR2 E3 ubiquitin-protein ligase UBR2 Homo sapiens (Human) SS
O70481 Ubr1 E3 ubiquitin-protein ligase UBR1 Mus musculus (Mouse) EV
Q6WKZ8 Ubr2 E3 ubiquitin-protein ligase UBR2 Mus musculus (Mouse) SS
10 20 30 40 50 60
MDRYDMEDVV VAPPAECSSP LKEWRLKRQA GTLDRSDIIE FLKRESPKYF DYQTSATVKD
70 80 90 100 110 120
TNVITLKCMF KESLAKEEII DVVVEFMLGD NPSSALEKLR LEGNTATVCG KVFKNGEPTY
130 140 150 160 170 180
SCRECGVDPT CVLCVNCFKR SAHRFHKYKM STSGGGGCCD CGDDEAWKKD QYCELHLANR
190 200 210 220 230 240
KNPLESKILT DAVLERVEIC FGAILAFCVS YLEIEPNASL QCLDGNVEGG QVDGAQYCTV
250 260 270 280 290 300
LYNDESHTFD QVIQTLTKIA KCRAKDAMEI VAAIDREGRA VVKCDTFEEC NKLKVSIENQ
310 320 330 340 350 360
MILPTSLVST ARNNQSLRTS VLHIGAVACQ QFALQLLGWF QEFLVRHYLF RKTFSELVQR
370 380 390 400 410 420
KQETFCIRHI LEYDVKLWKT ARTCWHRLLI SGMLMEYDNK MILAQEFSRR YATIVEDFIS
430 440 450 460 470 480
DDHDHAFSIV SLSVQLFTVP SIAHHLIAHE GIFDKLLHTF YHVAIEKFIR NKTLHFSKNI
490 500 510 520 530 540
ASLTFFKRAN YILYDLRYLL SLKPDVLSND LRNGFLEGCR ALMRVLNVMQ GMESMTRQTG
550 560 570 580 590 600
QHMDYEPEWE CAFNLHIKLA TTISQVIDWA SGDVKLLRKL YKMTMRALVS NSFIVGGEKV
610 620 630 640 650 660
MQPKKVADHV ANCLVYDISV QPVSIHLPLS RFFAGIYLHL GAHDLTYDGL QTETEALSIK
670 680 690 700 710 720
LTPREIIEPV LCTQAMIAQV GAGLWRRNGY TLLHQLYFYR NVRCRVEMLD RDIACLQIGA
730 740 750 760 770 780
SLMESNEFLI HVLNRFNTIP WLQENYWSLL SGNEMNDDII REASIFDEFL ELLIVIIGER
790 800 810 820 830 840
WMPGVSMVTE EDRLRKEIIQ LLCIKPYSHS ELSRALPDGN SGNSDNVFEE VINTVAVFKK
850 860 870 880 890 900
PVGADSKGVY ELKEHLLKEF NMYFYHYTKE DKSKAEELQR ERRKAKKQLV CCPPPMLPKL
910 920 930 940 950 960
TPAFTPMANI LQCPVFLNIC SLIMERALNA YSRSFTESHL QKVLHLLGYA IQEELSEHYP
970 980 990 1000 1010 1020
FLSFYERSQE YGILEKLEEL ARCPRLEAHY DFVLWTIERF KQLQAKQAPS DGRAGPSCSQ
1030 1040 1050 1060 1070 1080
QGTGGKLSLS AEEQAREERE NRARLAAERR AHIMAQMQKA QKSFISSNAE MFADTENETR
1090 1100 1110 1120 1130 1140
KESASTGPMD WEDIPPEEEQ GAVALESKVA CLGPDRKFYH GTDDTFKCIL CFENCAISRG
1150 1160 1170 1180 1190 1200
GRQLVSSAFV QTSRVIFTTP NLRNSQSALH ISCCGHVMHY SCWLEYFTNE EFKELRRPHR
1210 1220 1230 1240 1250 1260
NRAALAQAAN VEFQCPYCRT LSNAIIPVTE TLPAFSAPPS PNESYLPLDS FVEIMSTLAI
1270 1280 1290 1300 1310 1320
ELGNVKDHEL TTLPSVSNIL RLSGVVGGLA QFERSVQLIK NPPRLHADYI EGIEFLKKAL
1330 1340 1350 1360 1370 1380
LNTMKIQQSH LKDHPAIESI EMVPILWDSC SYTLQALEIY LYAVEKPLKA ELSMRHQSCA
1390 1400 1410 1420 1430 1440
RNLVRACSRS SALEWETDLP LLPPMRSQAE FSSRLLDTIF NQNDTSVLEW DCFRVLVPFQ
1450 1460 1470 1480 1490 1500
FGVLNLMVPE KGYKTIIPSG SMFDFYIMQT MFLAQLTKAV LCFDVEKEKA KRAEKAPNSE
1510 1520 1530 1540 1550 1560
LTQLDYIEQL PSRIRDNMID FYRRYNIPAR VLQKTKQKQL VEEESEENQG HGQTVVIPCE
1570 1580 1590 1600 1610 1620
SHHLALLLEY VQRQMSSFLR CSCLFYRFLT DVDFPDTFPT DQPDRFDLMC QYLGLDPMLG
1630 1640 1650 1660 1670 1680
VYFDMETVYA TMMHSFASHP HIDREVEQRC QPDARRSLQV EPCLRPLPRL KVLCDDFSDL
1690 1700 1710 1720 1730 1740
INSVSDIFCP NNEREEMKTP TMCLICGLIL CGQSYCCQPE LGKVSVGACT HHAHACGAEV
1750 1760 1770 1780 1790 1800
GIFLRIRDCQ VVYLGRGKGC FVPPPYLDEY GETDMGLRRG NPLRLSQAAY RKIYLQWLGH
1810 1820
GLHGEIARLN DNANVAAAAQ WHHM