ADD3
entrez
120
canonical
uniprot
Q9UEY8
canonical
ensembl
ENSG00000148700
resolver
ensp
ENSP00000277900
resolver
ensp
ENSP00000348381
resolver
ensp
ENSP00000353286
resolver
ensp
ENSP00000571386
resolver
ensp
ENSP00000571387
resolver
ensp
ENSP00000571388
resolver
ensp
ENSP00000571389
resolver
ensp
ENSP00000571390
resolver
ensp
ENSP00000571394
resolver
ensp
ENSP00000571398
resolver
ensp
ENSP00000571405
resolver
ensp
ENSP00000571406
resolver
ensp
ENSP00000571407
resolver
ensp
ENSP00000571414
resolver
ensp
ENSP00000571415
resolver
ensp
ENSP00000571419
resolver
ensp
ENSP00000592651
resolver
ensp
ENSP00000628104
resolver
ensp
ENSP00000628113
resolver
ensp
ENSP00000628119
resolver
ensp
ENSP00000628128
resolver
genesymbol
ADD3
resolver
genesymbol_syn
ADDL
resolver
hgnc
HGNC:245
resolver
uniprot
D3DRA8
resolver
uniprot
O43243
resolver
uniprot
Q53FL4
resolver
uniprot
Q59EK1
resolver
uniprot
Q5VU08
resolver
uniprot
Q5VU09
resolver
uniprot
Q92773
resolver
uniprot
Q9UEY7
resolver
uniprot_entry
ADDG_HUMAN
resolver
uniprot_entry
Q53FL4_HUMAN
resolver
uniprot_entry
Q59EK1_HUMAN
resolver
uniprot_entry
Q5VU08_HUMAN
resolver
uniprot_sec
D3DRA8
resolver
uniprot_sec
O43243
resolver
uniprot_sec
Q5VU09
resolver
uniprot_sec
Q92773
resolver
uniprot_sec
Q9UEY7
resolver
amino_acid_sequence
MSSDASQGVITTPPPPSMPHKERYFDRINENDPEYIRERNMSPDLRQDFNMMEQRKRVTQILQSPAFREDLECLIQEQMKKGHNPTGLLALQQIADYIMANSFSGFSSPPLSLGMVTPINDLPGADTSSYVKGEKLTRCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTNLKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLLLGDVAYYDYQGSLEEQEERIQLQKVLGPSCKVLVLRNHGVVALGETLEEAFHYIFNVQLACEIQVQALAGAGGVDNLHVLDFQKYKAFTYTVAASGGGGVNMGSHQKWKVGEIEFEGLMRTLDNLGYRTGYAYRHPLIREKPRHKSDVEIPATVTAFSFEDDTVPLSPLKYMAQRQQREKTRWLNSPNTYMKVNVPEESRNGETSPRTKITWMKAEDSSKVSGGTPIKIEDPNQFVPLNTNPNEVLEKRNKIREQNRYDLKTAGPQSQLLAGIVVDKPPSTMQFEDDDHGPPAPPNPFSHLTEGELEEYKRTIERKQQGLEDAEQELLSDDASSVSQIQSQTQSPQNVPEKLEENHELFSKSFISMEVPVMVVNGKDDMHDVEDELAKRVSRLSTSTTIENIEITIKSPEKIEEVLSPEGSPSKSPSKKKKKFRTPSFLKKNKKKEKVEA
uniprot
proteins
disease_involvement
DISEASE: Cerebral palsy, spastic quadriplegic 3 (CPSQ3) [MIM:617008]: A form of cerebral palsy, a group of non-progressive disorders of movement and/or posture resulting from defects in the developing central nervous system. CPSQ3 is an autosomal recessive neurodevelopmental disorder characterized by variable spasticity and cognitive impairment. {ECO:0000269|PubMed:23836506}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Plays a role in actin filament capping (PubMed:23836506). Binds to calmodulin (Probable). Involved in myogenic reactivity of the renal afferent arteriole (Af-art), renal interlobular arteries and middle cerebral artery (MCA) to increased perfusion pressure. Involved in regulation of potassium channels in the vascular smooth muscle cells (VSMCs) of the Af-art and MCA ex vivo. Involved in regulation of glomerular capillary pressure, glomerular filtration rate (GFR) and glomerular nephrin expression in response to hypertension. Involved in renal blood flow (RBF) autoregulation. Plays a role in podocyte structure and function. Regulates globular monomer actin (G-actin) and filamentous polymer actin (F-actin) ratios in the primary podocytes affecting actin cytoskeleton organization. Regulates expression of synaptopodin, RhoA, Rac1 and CDC42 in the renal cortex and the primary podocytes. Regulates expression of nephrin in the glomeruli and in the primary podocytes, expression of nephrin and podocinin in the renal cortex, and expression of focal adhesion proteins integrin alpha-3 and integrin beta-1 in the glomeruli. Involved in cell migration and cell adhesion of podocytes, and in podocyte foot process effacement. Regulates expression of profibrotics markers MMP2, MMP9, TGF beta-1, tubular tight junction protein E-cadherin, and mesenchymal markers vimentin and alpha-SMA (By similarity). Promotes the growth of neurites (By similarity). {ECO:0000250|UniProtKB:Q62847, ECO:0000250|UniProtKB:Q9QYB5, ECO:0000269|PubMed:23836506, ECO:0000305}.
uniprot
proteins
mass_dalton
79155
uniprot
proteins
post_translational_modification
PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.; PTM: Proteolytically cleaved by asparagine endopeptidase (AEP) into 2 fragments. Overexpression of the 1-357 fragment induces neuronal apoptosis, and overexpression of either 1-357 or 358-706 fragment increases the degeneration of dendritic spines. Overexpression of the 1-357 fragment impairs neurite outgrowth by down-regulating the expression of Rac2, and induces synaptic dysfunction and cognitive impairments in tau P301S transgenic mice, a mouse model for Alzheimer disease (AD). {ECO:0000250|UniProtKB:Q9QYB5}.
uniprot
proteins
protein_family
Adducin subfamily
uniprot
proteins
protein_family
Aldolase class II family
uniprot
proteins
pubmed
10581174
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15561718
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23836506
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
33992672
uniprot
proteins
pubmed
8893809
uniprot
proteins
sequence_length
706
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q62847}. Cell membrane {ECO:0000250|UniProtKB:Q62847}; Peripheral membrane protein; Cytoplasmic side. Cytoplasm {ECO:0000250|UniProtKB:Q9QYB5}. Note=Full-length protein and the cleavage fragment 358-706 localize mainly to the cytoplasm, while cleavage fragment 1-357 translocates from the cytoplasm to the nucleus. {ECO:0000250|UniProtKB:Q9QYB5}.
uniprot
proteins