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 Q9HFE5

Entry ID Method Resolution Chain Position Source
AF-Q9HFE5-F1 Predicted AlphaFoldDB

No variants for Q9HFE5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9HFE5

No associated diseases with Q9HFE5

4 regional properties for Q9HFE5

Type Name Position InterPro Accession
conserved_site Clathrin adaptor, mu subunit, conserved site 156 - 176 IPR018240-1
conserved_site Clathrin adaptor, mu subunit, conserved site 253 - 267 IPR018240-2
domain AP complex, mu/sigma subunit 2 - 133 IPR022775
domain Mu homology domain 156 - 425 IPR028565

Functions

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

11 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).
cell division site The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles.
cell tip The region at the end of the longest axis of a cylindrical or elongated cell.
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.
cytoplasmic vesicle A vesicle found in the cytoplasm of a cell.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endosome A vacuole to which materials ingested by endocytosis are delivered.
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
mitotic spindle pole body The microtubule organizing center that forms as part of the mitotic cell cycle; functionally homologous to the animal cell centrosome.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

1 GO annotations of molecular function

Name Definition
clathrin adaptor activity Bringing together a cargo protein with clathrin, responsible for the formation of endocytic vesicles.

5 GO annotations of biological process

Name Definition
endosome to plasma membrane protein transport The directed movement of proteins from the endosome to the plasma membrane in transport vesicles.
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 plasma membrane protein transport The directed movement of proteins from the Golgi to the plasma membrane in transport vesicles that move from the trans-Golgi network to the plasma membrane.
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.
vesicle-mediated transport A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MASAIFVLNL KGKVIISRDY RADIPMSVVE KFLPLKSEVE EEQGFSTPCL THEGINYIYI
70 80 90 100 110 120
HHNDVYLLAL SKMNSDAMEM LVFLRKMADV FIDYFKELQE ESIRDNFVLV YELLDEIMDF
130 140 150 160 170 180
GFPQTTETKI LQEYITQTSN TVKKHAPPPI AMTNAISWRS EGIHYRKNEV FLDVIESVNL
190 200 210 220 230 240
IAAADGTVIQ SEILGKVRLK CYLSGMPELR LGLNDKVLFE AAGRTIKGNT VEMEDVKFHQ
250 260 270 280 290 300
CVRLARFEND RTISFIPPDG EFDLMSYRMS SNVRPLIWVE CESIVHSGSR IEFMVKAKAQ
310 320 330 340 350 360
FKKRCIANNV QIIIPVPEDA DSPRFQTSNG HVQYAPEQAA MVWNIKKFAG GKEFFMRAEM
370 380 390 400 410 420
GLPSVKNEDI QVQKKRPVQL KFAIPYFTTS GIQVRYLKIT EPKLNYHAMP WVRYVTQNGT
EYSIRQ