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 Q8I8U2

Entry ID Method Resolution Chain Position Source
AF-Q8I8U2-F1 Predicted AlphaFoldDB

No variants for Q8I8U2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8I8U2

No associated diseases with Q8I8U2

4 regional properties for Q8I8U2

Type Name Position InterPro Accession
domain Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, C-terminal 601 - 806 IPR018969
domain Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, N-terminal 22 - 382 IPR018970
binding_site Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, thiamine diphosphate binding site 170 - 188 IPR019789
conserved_site Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, conserved site 157 - 163 IPR019790

Functions

Description
EC Number
Subcellular Localization
  • Golgi apparatus, trans-Golgi network
  • Cytoplasmic vesicle, clathrin-coated vesicle membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
AP-1 adaptor complex A heterotetrameric AP-type membrane coat adaptor complex that consists of beta1, gamma, mu1 and sigma1 subunits and links clathrin to the membrane surface of a vesicle; vesicles with AP-1-containing coats are normally found primarily in the trans-Golgi network. In at least humans, the AP-1 complex can be heterogeneric due to the existence of multiple subunit isoforms encoded by different genes (gamma1 and gamma2, mu1A and mu1B, and sigma1A, sigma1B and sigma1C).
clathrin coat of trans-Golgi network vesicle A clathrin coat found on a vesicle of the trans-Golgi network.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

3 GO annotations of molecular function

Name Definition
cargo adaptor activity Binding directly to the structural scaffolding elements of a vesicle coat (such as clathrin or COPII), and bridging the membrane, cargo receptor, and membrane deformation machinery.
clathrin adaptor activity Bringing together a cargo protein with clathrin, responsible for the formation of endocytic vesicles.
clathrin binding Binding to a clathrin heavy or light chain, the main components of the coat of coated vesicles and coated pits, and which also occurs in synaptic vesicles.

4 GO annotations of biological process

Name Definition
Golgi to endosome transport The directed movement of substances from the Golgi to early sorting endosomes. Clathrin vesicles transport substances from the trans-Golgi to endosomes.
Golgi to vacuole transport The directed movement of substances from the Golgi to the vacuole.
intracellular protein transport The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell.
receptor-mediated endocytosis An endocytosis process in which cell surface receptors ensure specificity of transport. A specific receptor on the cell surface binds tightly to the extracellular macromolecule (the ligand) that it recognizes; the plasma-membrane region containing the receptor-ligand complex then undergoes endocytosis, forming a transport vesicle containing the receptor-ligand complex and excluding most other plasma-membrane proteins. Receptor-mediated endocytosis generally occurs via clathrin-coated pits and vesicles.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSSKLRDLIK TVRSCKTAAE ERSQIAKESA LIRTAMKEED LESRQRNVAK LLYIHMLGYP
70 80 90 100 110 120
TQFGQMECLK LIVSPSYADK RIGYLGLMLL LDEKQEVLLL ATNCIRGDIM NSNQFIVGVS
130 140 150 160 170 180
LCAFGNICST AMARDISPEI EKVISHSNPY IRKKAALCAI RVLRKVPDLT ENYIPKIKAL
190 200 210 220 230 240
LSERNHAVIL TALTLIIEIC EMDSTQIIHF KKMVPQLVRI LKSLTSSGYL PEHDIGGVTD
250 260 270 280 290 300
PFLQVKILRL LRILGQNDPE ASDAMNDILA QVSTNTDSTK NVGNAILYEC VQTIMTIESE
310 320 330 340 350 360
NGLKVMAINI LGRFLLNRDN NIRYVALNTL SRVVNTDIQA VQRHRNTIVE CLKDPDVSIR
370 380 390 400 410 420
CRALDLIYSL VTESNIRVLV RELLNFLLIA DAQFKSELVA KLCIVTEKYA PNKRWQIDTI
430 440 450 460 470 480
LRVMSIAGNF IPDEVPSNLI QLISSTPELS SYAVQKLYLA LKQDITQQPL TQVGLWCIGE
490 500 510 520 530 540
YGDLLVADKS QLPKDEDGLS LNVSEQAVID IIDLIFRHAT TTQATRQYSL TSLAKLSSRF
550 560 570 580 590 600
SQSSLQRIKT MIDNYKQNIN LELQQRACEY STLFDFDKKA SILDRMPPIE KQEESPHIGN
610 620 630 640 650 660
KNIPTQTPPQ QHYQQQQQQP QQQSSQFGSI LDGLDSPTQS SANSGNNNNN NNKQGGNAMS
670 680 690 700 710 720
LLEDIFGSAP TPTSNGNMNN NNNMNNMNNN MNNNYAMGGM GMNNNNNNSM GGMMNNNNNN
730 740 750 760 770 780
NNNNNNNNNN NKSQASALLD IMGDLQLTPT PQQPQSQSQQ ALSPTNQTSV LQPVPQPLTF
790 800 810 820 830 840
LVYQKHGLNI SYECSKPQPN NLSLTNINMV ITNTGSSPIT NFSLQAAVPK YLKIQLLAPS
850 860 870 880 890
STVIPPNNSG EVTQVSKVLN SQQGQKPILL RLKLDFQING QPFSDVPDTP LPSLF