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 Q5RBF2

Entry ID Method Resolution Chain Position Source
AF-Q5RBF2-F1 Predicted AlphaFoldDB

No variants for Q5RBF2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5RBF2

No associated diseases with Q5RBF2

6 regional properties for Q5RBF2

Type Name Position InterPro Accession
domain C2 domain 10 - 130 IPR000008
domain HECT domain 602 - 958 IPR000569
domain WW domain 197 - 230 IPR001202-1
domain WW domain 369 - 402 IPR001202-2
domain WW domain 481 - 514 IPR001202-3
domain WW domain 532 - 565 IPR001202-4

Functions

Description
EC Number 2.3.2.26 Aminoacyltransferases
Subcellular Localization
  • Cytoplasm
  • Golgi apparatus
  • Endosome, multivesicular body
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
multivesicular body A type of endosome in which regions of the limiting endosomal membrane invaginate to form internal vesicles; membrane proteins that enter the internal vesicles are sequestered from the cytoplasm.

1 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.

3 GO annotations of biological process

Name Definition
cell differentiation The process in which relatively unspecialized cells, e.g. embryonic or regenerative cells, acquire specialized structural and/or functional features that characterize the cells, tissues, or organs of the mature organism or some other relatively stable phase of the organism's life history. Differentiation includes the processes involved in commitment of a cell to a specific fate and its subsequent development to the mature state.
regulation of sodium ion transmembrane transport Any process that modulates the frequency, rate or extent of sodium ion transmembrane transport.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAPLSAALLP WHGVCVPVCY GESRILRVKV VSGIDLAKKD IFGASDPYVK LSLYVADENR
70 80 90 100 110 120
ELALVQTKTI KKTLNPKWNE EFYFRVNPSN HRLLFEVFDE NRLTRDDFLG QVDVPLSHLP
130 140 150 160 170 180
TEDPTMERPY TFKDFLLRPR SHKSRVKGFL RLKMAYMPKN GGQEEENSEQ RDDMEHGWEV
190 200 210 220 230 240
VDSNDSASQH QEELPPPPLP PGWEEKVDNL GRTYYVNHNN RTTQWHRPSL MDVSSESDNN
250 260 270 280 290 300
IRQINQEAAH RRFRSRRHIS EDLEPEPSEG GDVPEPWETI SEEVNIAGDS LGLALPPPPA
310 320 330 340 350 360
SPGSRTSPQE LSEELSRRLQ ITPDSNGEQF SSLIQREPSS RLRSCSVTDA VAEQGHLPPP
370 380 390 400 410 420
SVAYVHTTPG LPSGWEERKD AKGRTYYVNH NNRTTTWTRP IMQLAEDGAS GSATNSNNHL
430 440 450 460 470 480
IEPQIRRPRS LSSPTVTLSA PLEGAKDSPV RRAVKDTLSN PQSPQPSPYN SPKPQHKVTQ
490 500 510 520 530 540
SFLPPGWEMR IAPNGRPFFI DHNTKTTTWE DPRLKFPVHM RSKTSLNPND LGPLPPGWEE
550 560 570 580 590 600
RIHLDGRTFY IDHNSKITQW EDPRLQNPAI TGPAVPYSRE FKQKYDYFRK KLKKPADIPN
610 620 630 640 650 660
RFEMKLHRNN IFEESYRRIM SVKRPDVLKA RLWIEFESEK GLDYGGVARE WFFLLSKEMF
670 680 690 700 710 720
NPYYGLFEYS ATDNYTLQIN PNSGLCNEDH LSYFTFIGRV AGLAVFHGKL LDGFFIRPFY
730 740 750 760 770 780
KMMLGKQITL NDMESVDSEY YNSLKWILEN DPTELDLMFC IDEENFGQTY QVDLEPNGSE
790 800 810 820 830 840
IMVTNENKRE YIDLVIQWRF VNRVQKQMNA FLEGFTELLP IDLIKIFDEN ELELLMCGLG
850 860 870 880 890 900
DVDVNDWRQH SIYKNGYCPN HPVIQWFWKA VLLMDAEKRI RLLQFVTGTS RVPMNGFAEL
910 920 930 940 950
YGSNGPQLFT IEQWGSPEKL PRAHTCFNRL DLPPYETFED LREKLLMAVE NAQGFEGVD