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

10 structures for P32893

Entry ID Method Resolution Chain Position Source
7E2C EM 418 A K 1-559 PDB
7E2D EM 371 A K 1-560 PDB
7E8S EM 436 A K/V 1-560 PDB
7E8T EM 380 A K 1-560 PDB
7E93 EM 654 A K/V 1-560 PDB
7E94 EM 467 A K/V 1-560 PDB
7EA3 EM 431 A K/X 1-560 PDB
7U05 EM 370 A C/c 1-560 PDB
7U06 EM 420 A C/c 1-560 PDB
AF-P32893-F1 Predicted AlphaFoldDB

16 variants for P32893

Variant ID(s) Position Change Description Diseaes Association Provenance
s07-830681 54 Q>H No SGRP
s07-830695 59 L>S No SGRP
s07-830776 86 R>K No SGRP
s07-830898 127 Q>E No SGRP
s07-830926 136 K>R No SGRP
s07-830997 160 A>T No SGRP
s07-831018 167 N>D No SGRP
s07-831046 176 N>S No SGRP
s07-831135 206 Q>K No SGRP
s07-831412 298 T>I No SGRP
s07-831639 374 V>F No SGRP
s07-831703 395 G>A No SGRP
s07-831939 474 G>W No SGRP
s07-831992 491 N>K No SGRP
s07-832078 520 A>V No SGRP
s07-832156 546 N>S No SGRP

No associated diseases with P32893

No regional properties for P32893

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P32893

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Golgi apparatus, cis-Golgi network
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
trans-Golgi network The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.
TRAPPII protein complex A complex that mediates intra-Golgi traffic, Golgi exit, endosome-to-Golgi traffic, and the trafficking of autophagy proteins from Golgi to the phagophore assembly site. Binds to a component of the COPI coat. In yeast it includes the following subunits: Bet3 (as homodimer), Bet5, Tca17, Trs20, Trs23, Trs31, Trs33, Trs65, Trs120, Trs130. The whole complex is thought to dimerize with itself.

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

6 GO annotations of biological process

Name Definition
beta-glucan biosynthetic process The chemical reactions and pathways resulting in the formation of beta-glucans.
cell wall organization A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
intra-Golgi vesicle-mediated transport The directed movement of substances within the Golgi, mediated by small transport vesicles. These either fuse with the cis-Golgi or with each other to form the membrane stacks known as the cis-Golgi reticulum (network).
protein-containing complex assembly The aggregation, arrangement and bonding together of a set of macromolecules to form a protein-containing complex.
regulation of catalytic activity Any process that modulates the activity of an enzyme.
retrograde transport, endosome to Golgi The directed movement of membrane-bounded vesicles from endosomes back to the trans-Golgi network where they are recycled for further rounds of transport.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MECFVPLRCD LDGSNIEQLR QSHLSRKFII FDEQLNLWLW FQGNSQENKR FVLQNMIILI
70 80 90 100 110 120
NEAQVTRTST IDDYFTQVEN NENLWRLKND CCSKILFKSN VVMNNGYNNQ IKFVFEYKSV
130 140 150 160 170 180
DANFNNQDSL QDPQAKYTLD KYSSEEILPS FEPVYSWSSA ATKSSKNTNN HLEKNNRATH
190 200 210 220 230 240
RVSSKNSEVH EADVSRNPNT FTLKLQYPIF SLLNMRLRNI SLKSEHCILS SLDFQTSKAS
250 260 270 280 290 300
EQLTKKFIYP QEHNSFLKLN FQEISYKLID GTSQIELDPI CPLKVPLTAF SYDSISATFK
310 320 330 340 350 360
LVLLPKSTQP HRVKITLAYE LELHPNLKLP VRTSWETEVT LKRSMPISST SSQYSSNNNN
370 380 390 400 410 420
TNHSASFNGA ANNVNSGGLA NLRLGGVSSS RFSLGAASTT SLVNSKLSNV KFKFINSNIK
430 440 450 460 470 480
VIKGEKFTMR LQIINSSSSP LDLVVYYNNT INPIPSANNV RNSNGINNCG MNNGTIPNSP
490 500 510 520 530 540
LTLENQYQLH NKYRKIAEGI ILLSNDYKIP VVPPRETYFA DLRFIGIMSG YYGTLSGLKV
550
LDLNTNELIE VGNGASVLIQ