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 O77836

Entry ID Method Resolution Chain Position Source
AF-O77836-F1 Predicted AlphaFoldDB

45 variants for O77836

Variant ID(s) Position Change Description Diseaes Association Provenance
rs444061786 9 A>S No EVA
rs718837987 12 L>V No EVA
rs525095333 15 I>V No EVA
rs473727468 25 T>I No EVA
rs464352210 30 G>R No EVA
rs478183795 33 K>T No EVA
rs464510101 34 V>A No EVA
rs464510101 34 V>G No EVA
rs461515450 34 V>M No EVA
rs447682365 36 A>V No EVA
rs478842182 38 Q>K No EVA
rs462120233 42 L>H No EVA
rs441950868 43 A>D No EVA
rs441950868 43 A>V No EVA
rs483001873 44 L>P No EVA
rs483001873 44 L>Q No EVA
rs462806875 45 K>N No EVA
rs798509569 54 R>* No EVA
rs439448027 61 E>D No EVA
rs453857937 83 V>L No EVA
rs440106496 88 D>H No EVA
rs466440878 137 I>L No EVA
rs470124123 155 T>N No EVA
rs450078363 162 N>T No EVA
rs478036771 164 Y>C No EVA
rs457975137 167 E>G No EVA
rs447609234 168 K>R No EVA
rs441810891 171 C>R No EVA
rs476391026 174 V>I No EVA
rs433142344 184 Y>* No EVA
rs479320849 298 K>E No EVA
rs442181762 304 D>H No EVA
rs483214423 320 P>T No EVA
rs439675546 326 D>A No EVA
rs470971615 326 D>E No EVA
rs439675546 326 D>V No EVA
rs453504610 344 D>H No EVA
rs436567292 347 K>R No EVA
rs474354286 351 R>Q No EVA
rs457261656 354 F>L No EVA
rs443098046 391 N>S No EVA
rs463803851 422 T>P No EVA
rs483107603 434 D>E No EVA
rs110490061 504 S>N No EVA
rs447759073 525 L>F No EVA

No associated diseases with O77836

No regional properties for O77836

Type Name Position InterPro Accession
No domain, repeats, and functional sites for O77836

Functions

Description
EC Number 2.4.1.145 Hexosyltransferases
Subcellular Localization
  • Golgi apparatus membrane ; Single-pass type II membrane protein
  • ;
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum-Golgi intermediate compartment A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport.
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
Golgi stack The set of thin, flattened membrane-bounded compartments, called cisternae, that form the central portion of the Golgi complex. The stack usually comprises cis, medial, and trans cisternae; the cis- and trans-Golgi networks are not considered part of the stack.
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.
peroxisome A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.

5 GO annotations of molecular function

Name Definition
acetylglucosaminyltransferase activity Catalysis of the transfer of an N-acetylglucosaminyl residue from UDP-N-acetyl-glucosamine to a sugar.
alanine-glyoxylate transaminase activity Catalysis of the reaction: L-alanine + glyoxylate = pyruvate + glycine.
alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,4-(N-acetyl-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R.
metal ion binding Binding to a metal ion.
protein homodimerization activity Binding to an identical protein to form a homodimer.

3 GO annotations of biological process

Name Definition
glyoxylate metabolic process The chemical reactions and pathways involving glyoxylate, the anion of glyoxylic acid, HOC-COOH.
N-glycan processing The conversion of N-linked glycan (N = nitrogen) structures from the initially transferred oligosaccharide to a mature form, by the actions of glycosidases and glycosyltransferases. The early processing steps are conserved and play roles in glycoprotein folding and trafficking.
protein N-linked glycosylation A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9UM21 MGAT4A Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A Homo sapiens (Human) PR
Q5M854 Mgat4a Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MRLRNGTVAT VLAFITSFLT LSWYTTWQNG KEKVIAYQRE FLALKERLRI AEHRISQRSS
70 80 90 100 110 120
ELSAIVQQFK RVEAETNRSK DPVNKFSDDT LKILKELTSK KSLQVPSIYY HLPHLLQNEG
130 140 150 160 170 180
SLQPAVQIGN GRTGVSIVMG IPTVKREVKS YLIETLHSLI DNLYPEEKLD CVIVVFIGET
190 200 210 220 230 240
DTDYVNGVVA NLEKEFSKEI SSGLVEIISP PESYYPDLTN LKETFGDSKE RVRWRTKQNL
250 260 270 280 290 300
DYCFLMMYAQ EKGTYYIQLE DDIIVKQNYF NTIKNFALQL SSEEWMILEF SQLGFIGKMF
310 320 330 340 350 360
QAPDLTLIVE FIFMFYKEKP IDWLLDHILW VKVCNPEKDA KHCDRQKANL RIRFRPSLFQ
370 380 390 400 410 420
HVGLHSSLTG KIQKLTDKDY MKPLLLKIHV NPPAEVSTSL KVYQGHTLEK TYMGEDFFWA
430 440 450 460 470 480
ITPVAGDYIL FKFDKPVNVE SYLFHSGNQD HPGDILLNTT VEVLPLKSEG LDISKETKDK
490 500 510 520 530
RLEDGYFRIG KFENGVAEGM VDPSLNPISA FRLSVIQNSA VWAILNEIHI KKVTN