Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P31254

Entry ID Method Resolution Chain Position Source
AF-P31254-F1 Predicted AlphaFoldDB

22 variants for P31254

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3410012458 17 S>* No EVA
rs3412849130 18 S>I No EVA
rs3411898240 18 S>L No EVA
rs48064925 60 V>A No EVA
rs51995337 127 A>S No EVA
rs3412777684 132 P>L No EVA
rs3412610382 191 R>L No EVA
rs3412785610 279 T>A No EVA
rs3411436716 287 R>S No EVA
rs3412577417 338 F>C No EVA
rs3412849182 340 T>A No EVA
rs3410012550 341 Q>E No EVA
rs3412281750 342 H>Y No EVA
rs3412665474 343 S>R No EVA
rs51133250 355 E>D No EVA
rs3411436744 364 V>E No EVA
rs3410012460 478 I>N No EVA
rs3412665531 481 E>D No EVA
rs3412578736 487 A>T No EVA
rs3412578682 521 W>C No EVA
rs3412577379 536 R>C No EVA
rs3412610339 881 H>R No EVA

No associated diseases with P31254

8 regional properties for P31254

Type Name Position InterPro Accession
domain THIF-type NAD/FAD binding fold 54 - 444 IPR000594-1
domain THIF-type NAD/FAD binding fold 450 - 945 IPR000594-2
conserved_site Ubiquitin-activating enzyme E1, conserved site 410 - 418 IPR018074
domain Ubiquitin-activating enzyme E1, C-terminal 922 - 1053 IPR018965
domain Ubiquitin-activating enzyme, SCCH domain 637 - 884 IPR019572
domain Ubiquitin-activating enzyme E1, FCCH domain 226 - 295 IPR032418
domain Ubiquitin-activating enzyme E1, four-helix bundle 297 - 365 IPR032420
active_site Ubiquitin-activating enzyme E1, Cys active site 629 - 637 IPR033127

Functions

Description
EC Number 6.2.1.45 Acid--thiol ligases
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.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ubiquitin activating enzyme activity Catalysis of the reaction: E1 + ubiquitin + ATP--> E1-ubiquitin + AMP + PPi, where the E1-ubiquitin linkage is a thioester bond between the C-terminal glycine of Ub and a sulfhydryl side group of an E1 cysteine residue. This is the first step in a cascade of reactions in which ubiquitin is ultimately added to a protein substrate.

4 GO annotations of biological process

Name Definition
cellular response to DNA damage stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
protein modification by small protein conjugation A protein modification process in which one or more groups of a small protein, such as ubiquitin or a ubiquitin-like protein, are covalently attached to a target protein.
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.
ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P22314 UBA1 Ubiquitin-like modifier-activating enzyme 1 Homo sapiens (Human) PR
Q02053 Uba1 Ubiquitin-like modifier-activating enzyme 1 Mus musculus (Mouse) PR
Q8VE47 Uba5 Ubiquitin-like modifier-activating enzyme 5 Mus musculus (Mouse) PR
Q9Z1F9 Uba2 SUMO-activating enzyme subunit 2 Mus musculus (Mouse) PR
Q8C878 Uba3 NEDD8-activating enzyme E1 catalytic subunit Mus musculus (Mouse) PR
Q5U300 Uba1 Ubiquitin-like modifier-activating enzyme 1 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MSSSVLSKKR KVSGPDSSLD SSWSPTYSVM FGVPPGPTNE MSKNKEMDID ESLYSRQLYV
70 80 90 100 110 120
LGHEAMKHLQ ASSVLISGLQ GLGVEIAKNI ILGGVKAVTL HDQGIAQWAD LSSQFCLREE
130 140 150 160 170 180
DIGKNRAEIS QPRLAELNSY VPVFAYTGPL IEEFLSGFQV VVLTNTPLEY QLQVGEFCHS
190 200 210 220 230 240
HGIKLVVADT RGLVGQLFCD FGEEMILTDS NGEQPLSAMV SMITKENPGI VTCLEDSRHG
250 260 270 280 290 300
FESGDFISFT EVQGMSELNG IGPIEIKVLG PYTFSICDTS SFSEYIRGGI VSQVKVPRKI
310 320 330 340 350 360
NFKPLLASLA EPEFVVTDFA KCCHPAQLHI GFQALHQFCT QHSRPPRPHN EEDAEELVTL
370 380 390 400 410 420
AQSVNAQALP AVQQDCLDID LIRKLAYVAA GDLAPMNAFF GGLAAQEVMK ACSGKFMPIR
430 440 450 460 470 480
QWLYFDALEC LPEHRVAFME DKCLPHQNRY DGQVAVFGSD LQEKLGKQKY FLVGAGAIGC
490 500 510 520 530 540
ELLKNFAMIG LGCGEDGEIT VTDMDTIEKS NLNRQFLFRP WDITKLKSET AAAAVRDINP
550 560 570 580 590 600
HIRIFSHQNR VGPETEHVYD DDFFQKLDGV ANALDNVDAR LYVDRRCVYY RKPLLESGTL
610 620 630 640 650 660
GTKGNVQVVV PFLTESYSSS QDPPEKSIPI CTLKNFPNAI EHTVQWARDE FEGLFKQSAE
670 680 690 700 710 720
NVNQYLTDPK FMERTLQLAG TQPLEVLEAI HCSLVLQRPQ TWADCVTWAY QHWHTQYSHN
730 740 750 760 770 780
IQQLLHNFPP AQLTSSGALF WSGPKRCPHP LTFDINNPLH LDYVMAAANL FAQTYGLGGS
790 800 810 820 830 840
QDCAVVAKLL QSLPVPKFAP KSGIRIHVSE QELQSTSATT IDDSHLEELK TALPTPDKLL
850 860 870 880 890 900
GFKMYPIDFE KDDDSNFHMD FIVAASNLRA ENYGISPADR HKSKLIAGKI IPAIATTTSA
910 920 930 940 950 960
IVGLVCLELY KVVQGHQQLE SYKNSFINLA LPLFSFSAPL APECHQYYDQ EWTLWDRFDV
970 980 990 1000 1010 1020
QGLQPSGEEM TLKQFLDYFK TEHKLEVIML SQGVSMLYSV FMPASKLKER LDQPMTEIVS
1030 1040 1050
CVSKQKLGHH VKSLVFELCC NSDSGDDIEV PYVRYIIR