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 Q04183

Entry ID Method Resolution Chain Position Source
7E2C EM 418 A J 1-1289 PDB
7E2D EM 371 A J 1-1289 PDB
7E8S EM 436 A J/U 1-1289 PDB
7E8T EM 380 A J 1-1289 PDB
7E93 EM 654 A J/U 1-1289 PDB
7E94 EM 467 A J/U 1-1289 PDB
7EA3 EM 431 A J/W 1-1289 PDB
7U05 EM 370 A A/a 1-1289 PDB
7U06 EM 420 A A/a 1-1289 PDB
AF-Q04183-F1 Predicted AlphaFoldDB

18 variants for Q04183

Variant ID(s) Position Change Description Diseaes Association Provenance
s04-1287834 33 N>D No SGRP
s04-1287540 131 T>A No SGRP
s04-1286554 459 E>D No SGRP
s04-1286221 570 S>R No SGRP
s04-1286207 575 N>S No SGRP
s04-1286063 623 L>S No SGRP
s04-1285817 705 V>A No SGRP
s04-1285422 837 G>R No SGRP
s04-1285232 900 M>T No SGRP
s04-1285220 904 D>G No SGRP
s04-1285131 934 L>V No SGRP
s04-1284975 986 P>S No SGRP
s04-1284867 1022 V>L No SGRP
s04-1284765 1056 V>L No SGRP
s04-1284710 1074 S>L No SGRP
s04-1284288 1215 I>V No SGRP
s04-1284107 1275 G>E No SGRP
s04-1284102 1277 I>F No SGRP

No associated diseases with Q04183

No regional properties for Q04183

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q04183

Functions

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

4 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.
early endosome A membrane-bounded organelle that receives incoming material from primary endocytic vesicles that have been generated by clathrin-dependent and clathrin-independent endocytosis; vesicles fuse with the early endosome to deliver cargo for sorting into recycling or degradation pathways.
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

4 GO annotations of biological process

Name Definition
early endosome to Golgi transport The directed movement of substances from early endosomes to the Golgi.
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).
regulation of GTPase activity Any process that modulates the rate of GTP hydrolysis by a GTPase.
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
MNILKHFPSY VGPSKIRTLV IPIGHWTRKE FNNAVQKLSE FNEIHLSDVT PIDSPIFTPQ
70 80 90 100 110 120
GFPHGKLFFD FLTIDHDDAL ELFLYDFEPF RKTFVIIGLV NDYSDPLTNL NFMKEKYPTL
130 140 150 160 170 180
ISPNLVYASS TPTKELEQTI DTMENVFASS PDMQKNIETI MCDIARNFLT ALNSYYSSYK
190 200 210 220 230 240
HVTLRSPGAI GGNAVLKTTL IRQNSYTSSS SSTPMSAVQS SVSSSSKAGS VTTASKRLSS
250 260 270 280 290 300
FEMTTNSLKR SASLKLATTL STSENRSQQK SLGRQMKILG NFQLLAGRYV DALNSFVDAI
310 320 330 340 350 360
TTLYKVRDYL WLGSALDGIS ICFLLLSYLG LSYQIPQIVS LICPVEKLNF ESSSTGISPV
370 380 390 400 410 420
DSNSKATAST TASSTPRNSI SIAAMQSPRN SIMSLSAPAL NIDVENINLP LLIKCISDKV
430 440 450 460 470 480
LYYYDLSLMH NSEYAPQVVY CEFLLKTLTF MTSCYKSSEF SKDVLDNIVK NQHRALSDIP
490 500 510 520 530 540
NSPMFPRFEV YFYSNKLFEL QLKEMQVEAQ IKIYSTMAEV YRLLGYKRKQ LFVLRLLMVA
550 560 570 580 590 600
LLATPNKIAW HPDYRTLIDT IIELLNINES EAKINVDDPS QSTWLILQKK ILQLCIKVSR
610 620 630 640 650 660
KINDFEYVAK FSSILITKYT HLLNQSEQDA LFKEYIQPSI TNESITSYWD PFILREVVIN
670 680 690 700 710 720
RILDSDPTSN EIPLESDVSS LESLENRQKT QDINPQEVFN PFKRVQPTSF VSNNSTKVPI
730 740 750 760 770 780
LVFLVGDKAE FTCRVQNPFK FDFTINDIQL DEEISEFCEI DRKAVSYSGP YNVKAESIRS
790 800 810 820 830 840
ITLPLIIKKP TYKKIYEISC LKISILKLPL QKFDIINDSR RSNPVEEEAE YSKCIYGKLK
850 860 870 880 890 900
IKILPEQPQL ELLSTSKMTR NSWMMLDGTK TDFHITVRNK SLSCAINHIK IIPMNNIEQM
910 920 930 940 950 960
LKPDYWKKMP PDDLYIMEKQ LDWLSKSCVR IIKLPTVIKP NETITFDLEL DNTAVPFNFT
970 980 990 1000 1010 1020
GFDLLIEYGM SATDESCIYL KKLSIPYEVT LRRTIEVPSM DIIPLNELFS SQVENVDWIE
1030 1040 1050 1060 1070 1080
YVMSKIRAES NLHSRDFILL LLDFRNSWID GIKLNVQFED FTSNEYHVEA SHTSRIIVPI
1090 1100 1110 1120 1130 1140
KKIDYKKYNF ENTPIPRIYP GRQFIQSGLN EEQTIEMRQK FWCREHIISK LKCNWKLTTD
1150 1160 1170 1180 1190 1200
QSVTGSVDFN KFIEKFDHKM VYTIYPGRLF YGVQLLLDEP KVKVGEIINL KIITEPTSTC
1210 1220 1230 1240 1250 1260
RRKQNSTVNF LDIVIFDSKT SKILPRSNRR ILYNGSLTKP ISTTKVSEIN LEIIPIEKGR
1270 1280
YEFSVCISKS NNQDGIIQFD SENVILSVI