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 B2W244

Entry ID Method Resolution Chain Position Source
AF-B2W244-F1 Predicted AlphaFoldDB

No variants for B2W244

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2W244

No associated diseases with B2W244

2 regional properties for B2W244

Type Name Position InterPro Accession
domain GB1/RHD3-type guanine nucleotide-binding (G) domain 48 - 298 IPR030386
domain Sey1/RHD3-like, three-helix bundle domain 361 - 800 IPR046758

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
  • Enriched in the cortical ER
  • Concentrated in punctae along the ER tubules
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

2 GO annotations of molecular function

Name Definition
GTP binding Binding to GTP, guanosine triphosphate.
GTPase activity Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.

1 GO annotations of biological process

Name Definition
endoplasmic reticulum organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MMNAHFAGVG DNADNAAYEH GIQVIDEDKM FNGNVSTYLN IEKVIPAGFN YHLISVFGSQ
70 80 90 100 110 120
STGKSTLLNH LFGTQFGVMS EQERRQTTKG IWMSKNKRES GGSSMAENIL VMDVEGTDGR
130 140 150 160 170 180
ERGEDQDFER KSALFALATS EVLIVNIWEH QVGLYQGANM GLLKTVFEVN LQLFVKDSQS
190 200 210 220 230 240
TPRSLLFFVI RDHLGTTPLK NLQNTLVQDL SKLWSTISKP AGLENSRIED YFDFAFVALP
250 260 270 280 290 300
HKILQPEKFD EAVTQLSTRF KEGYNDPRKS GLIDEATAPI FLPQYHRRIP ADGFSAYAEG
310 320 330 340 350 360
VWDQIVNNKD LDLPTQQELL AQFRCDEISR EVQVAFDETI TPLEDKQAED ARAGTHSLIP
370 380 390 400 410 420
DLGPKMNAAR QKVLKDFDVN ASRYHKGVYK RKQAELEGKV DTRLKALFQK QLTAAHKSGI
430 440 450 460 470 480
EGFTEAVSAA VKNGQKKNAS YDFAQIVDSE KKKALTKFEE DATAMAIEGA AWSSHENELK
490 500 510 520 530 540
IYKKELDDVS GRLRKEEMRR LATRIERWVR TRLDESIGLE FNKLGSGRGG SGAPEHGDRP
550 560 570 580 590 600
PTEKDLWDRV WTIFTDTVKM AEKRFTDRAS SFDASADEVE VGLWRLRRKS WGVLRAKIDE
610 620 630 640 650 660
EVMEGNILLK LRENFEDKFR YDDLGVPRIW RPTDDIDGLY TKARESTITV IPLLAHFKLA
670 680 690 700 710 720
KTSKPPPLDA WIGEAPASVS PADEEDLSPI GGVDDDEDKT LEDEMTILSD GKQADLLVRF
730 740 750 760 770 780
KKTADGVYVE AKRGAIGGLS QIPFWLYPAM LALGWNEIVA VLRNPIYFIF LILLAVAAYV
790 800 810 820 830 840
TYTLNLWGPI MRVANAASQQ GLEVGKERLR AFLENSDAGR QAMAMSGSGD SNSTRRYEDV
850 860
KMDRLNGDGK KSKSMEEDLD DI