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 Q5RAG3

Entry ID Method Resolution Chain Position Source
AF-Q5RAG3-F1 Predicted AlphaFoldDB

No variants for Q5RAG3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5RAG3

No associated diseases with Q5RAG3

No regional properties for Q5RAG3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q5RAG3

Functions

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

1 GO annotations of cellular component

Name Definition
Cul2-RING ubiquitin ligase complex A ubiquitin ligase complex in which a cullin from the Cul2 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein.

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

2 GO annotations of biological process

Name Definition
positive regulation of proteasomal ubiquitin-dependent protein catabolic process Any process that activates or increases the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
protein quality control for misfolded or incompletely synthesized proteins The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MASDTPESLM ALCTDFCLRN LDGTLGYLLD KETLRLHPDI FLPSEICDRL VNEYVELVNA
70 80 90 100 110 120
ACNFEPHESF FSLFSDPRST RLTRIHLRED LVQDQDLEAI RKQDLVELYL TNCEKLSAKS
130 140 150 160 170 180
LQTLRSFSHT LVSLSLFGCT NIFYEEENPG GCEDEYLVNP TCQVLVKDFT FEGFSRLRFL
190 200 210 220 230 240
NLGRMIDWVP VESLLRPLNS LAALDLSGIQ TSDAAFLTQW KDSLVSLVLY NMDLSDDHIR
250 260 270 280 290 300
VIVQLHKLRH LDISRDRLSS YYKFKLTREV LSLFVQKLGN LMSLDISGHM ILENCSISKM
310 320 330 340 350 360
EEEAGQTSIE PSKSSIIPFR ALKRPLQFLG LFENSLCRLT HIPAYKVSGD KNEEQVLNAI
370 380 390 400 410 420
EAYTEHRPEI TSRAINLLFD IARIERCNQL LRALKLVITA LKCHKYDRNI QVTGSAALFY
430 440 450 460 470 480
LTNSEYRSEQ SVKLRRQVIQ VVLNGMESYQ EVTVQRNCCL TLCNFGIPEE LEFQYRRVNE
490 500 510 520 530 540
LLLSILNPTR QDESIQRIAV HLCNALVCQV DNDHKEAVGK MGFVVTMLKL IQKKLLDKIC
550 560 570 580 590 600
DQVMEFSWSA LWNITDETPD NCEMFLNFNG MKLFLDCLKE FPEKQELHRN MLGLLGNVAE
610 620 630 640 650 660
VKELRPQLMT SQFISVFSNL LESKADGIEV SYNACGVLSH IMFDGPEAWG VCEPQREEVE
670 680 690 700 710 720
ERMWAAIQSW DINSRRNINY RSFEPILRLL PQGISPVSQH WATWALYNLV SVYPDKYCPL
730 740 750 760
LIKEGGMPLL RDIIKMATAR QETKEMARKV IEHCSNFKEE NMDTSR