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 Q8VD37

Entry ID Method Resolution Chain Position Source
AF-Q8VD37-F1 Predicted AlphaFoldDB

28 variants for Q8VD37

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388685014 172 E>A No EVA
rs3388694542 177 R>T No EVA
rs3388697588 178 R>H No EVA
rs3388694554 197 L>P No EVA
rs3388683457 199 P>S No EVA
rs3388697821 288 I>M No EVA
rs3388701772 305 A>T No EVA
rs3388697522 337 P>S No EVA
rs32662586 355 T>P No EVA
rs3388696653 377 E>* No EVA
rs3388688953 392 Y>* No EVA
rs3388698414 405 G>* No EVA
rs3388692567 409 T>I No EVA
rs3388696698 447 T>N No EVA
rs3388688946 476 V>A No EVA
rs3388688946 476 V>G No EVA
rs3388676796 516 A>T No EVA
rs3388683529 563 K>E No EVA
rs3388697820 576 I>T No EVA
rs3410377145 583 N>T No EVA
rs3388676823 586 P>R No EVA
rs3388701806 603 L>M No EVA
rs3388697566 624 W>C No EVA
rs3388694667 635 K>Q No EVA
rs3388694636 647 Y>* No EVA
rs3388694576 675 E>K No EVA
rs3388694689 678 S>N No EVA
rs3388702654 793 I>F No EVA

No associated diseases with Q8VD37

2 regional properties for Q8VD37

Type Name Position InterPro Accession
domain Protein kinase domain 338 - 613 IPR000719
domain Leucine-rich repeat-containing N-terminal, plant-type 24 - 61 IPR013210

Functions

Description
EC Number
Subcellular Localization
  • Membrane, clathrin-coated pit ; Peripheral membrane protein ; Cytoplasmic side
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
AP-2 adaptor complex A heterotetrameric AP-type membrane coat adaptor complex that consists of alpha, beta2, mu2 and sigma2 subunits, and links clathrin to the membrane surface of a vesicle, and the cargo receptors during receptor/clathrin mediated endocytosis. Vesicles with AP-2-containing coats are normally found primarily near the plasma membrane, on endocytic vesicles. In at least humans, the AP-2 complex can be heterogeneric due to the existence of multiple subunit isoforms encoded by different alpha genes (alphaA and alphaC).
clathrin-coated pit A part of the endomembrane system in the form of an invagination of a membrane upon which a clathrin coat forms, and that can be converted by vesicle budding into a clathrin-coated vesicle. Coated pits form on the plasma membrane, where they are involved in receptor-mediated selective transport of many proteins and other macromolecules across the cell membrane, in the trans-Golgi network, and on some endosomes.
clathrin-coated vesicle A vesicle with a coat formed of clathrin connected to the membrane via one of the clathrin adaptor complexes.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
presynapse The part of a synapse that is part of the presynaptic cell.

4 GO annotations of molecular function

Name Definition
microtubule binding Binding to a microtubule, a filament composed of tubulin monomers.
phospholipid binding Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.
SH3 domain binding Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.
tubulin binding Binding to monomeric or multimeric forms of tubulin, including microtubules.

8 GO annotations of biological process

Name Definition
clathrin coat assembly The process that results in the assembly of clathrin triskelia into the ordered structure known as a clathrin cage.
clathrin-dependent endocytosis An endocytosis process that begins when material is taken up into clathrin-coated pits, which then pinch off to form clathrin-coated endocytic vesicles.
energy homeostasis Any process involved in the balance between food intake (energy input) and energy expenditure.
positive regulation of eating behavior Any process that activates or increases the frequency, rate or extent of eating behavior.
positive regulation of feeding behavior Any process that activates or increases the frequency, rate or extent of feeding behavior.
positive regulation of multicellular organism growth Any process that activates or increases the frequency, rate or extent of growth of an organism to reach its usual body size.
positive regulation of receptor-mediated endocytosis Any process that activates or increases the frequency, rate or extent of receptor mediated endocytosis, the uptake of external materials by cells, utilizing receptors to ensure specificity of transport.
response to dietary excess The physiological process in which dietary excess is sensed by the central nervous system, resulting in a reduction in food intake and increased energy expenditure.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q05080 HOF1 Cytokinesis protein 2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q9H939 PSTPIP2 Proline-serine-threonine phosphatase-interacting protein 2 Homo sapiens (Human) PR
O60861 GAS7 Growth arrest-specific protein 7 Homo sapiens (Human) PR
Q9BQI5 SGIP1 SH3-containing GRB2-like protein 3-interacting protein 1 Homo sapiens (Human) PR
P97814 Pstpip1 Proline-serine-threonine phosphatase-interacting protein 1 Mus musculus (Mouse) PR
Q60780 Gas7 Growth arrest-specific protein 7 Mus musculus (Mouse) PR
Q99M15 Pstpip2 Proline-serine-threonine phosphatase-interacting protein 2 Mus musculus (Mouse) PR
10 20 30 40 50 60
MMEGLKKRTR KAFGIRKKEK DTDSTGSPDR DGMQPSPHEP PYHSKAECAR EGGKKASKKS
70 80 90 100 110 120
NGAPNGFYAE IDWERYNSPE LDEEGYSIRP EEPGSTKGKH FYSSSESEEE EESHKKFNIK
130 140 150 160 170 180
IKPLQSKDVL KNAATVDELK ASIGNIALSP SPVRKSPRRS PGAIKRNLSS EEVARPRRST
190 200 210 220 230 240
PTPELTSKKP LDDTLALAPL FGPPLESAFD EQKTEVLLDQ PEIWGSGQPM NPSTESPELA
250 260 270 280 290 300
RPFPTGTPPP LPPKTVPATP PRTGSPLTVA TGNDQAATEA KIEKLPSISD LDSIFGPVLS
310 320 330 340 350 360
PKSVAVNTEE KWVHFSDASP EHVTPELTPR EQVVTPPAAS DIPADSPAPA PPGPTGSAGP
370 380 390 400 410 420
PGPPGPRHVP SPLNLEEVQK KVAEQTFIKD DYLETLSSPK ECGLGQRATP PPPPPPTYRT
430 440 450 460 470 480
VVSSPGPGSG SGTGTTSGAS SPARPATPLV PCSTTPPPPP PRPPSRPKLP PGKPGVGDVS
490 500 510 520 530 540
RPFSPPIHSS SPPPIAPLAR AESTSSISST NSLSAATTPT VGSSRGPSPL TMGAQDTLPV
550 560 570 580 590 600
AAAFTETVNA YFKGADPSKC IVKITGEMVL SFPAGITRHF ANNPSPAALT FRVVNSSRLE
610 620 630 640 650 660
HVLPNPQLLC CDNTQNDANT KEFWVNMPNL MTHLKKVSEQ KPQATYYNVD MLKYQVSAQG
670 680 690 700 710 720
IQSTPLNLAV NWRCEPASTD LRIDYKYNTD AMSTAVALNN VQFLVPIDGG VTKLQAVLPP
730 740 750 760 770 780
AVWNAEQQRI LWKIPDISQK SENGGVGSLL ARFQLSEGPS KPSPLVVQFT SEGSTLSGCD
790 800
IELVGAGYRF SLIKKRFAAG KYLADN