Clip1
entrez
56430
canonical
uniprot
Q922J3
canonical
ensembl
ENSMUSG00000049550
resolver
ensp
ENSMUSP00000031382
resolver
ensp
ENSMUSP00000068241
resolver
ensp
ENSMUSP00000107186
resolver
ensp
ENSMUSP00000107190
resolver
ensp
ENSMUSP00000107192
resolver
ensp
ENSMUSP00000121425
resolver
ensp
ENSMUSP00000264252
resolver
ensp
ENSMUSP00000264253
resolver
ensp
ENSMUSP00000264254
resolver
ensp
ENSMUSP00000264255
resolver
ensp
ENSMUSP00000264256
resolver
ensp
ENSMUSP00000264263
resolver
ensp
ENSMUSP00000264264
resolver
ensp
ENSMUSP00000264265
resolver
ensp
ENSMUSP00000264267
resolver
ensp
ENSMUSP00000264310
resolver
ensp
ENSMUSP00000264311
resolver
ensp
ENSMUSP00000264316
resolver
ensp
ENSMUSP00000264319
resolver
ensp
ENSMUSP00000264320
resolver
ensp
ENSMUSP00000264338
resolver
ensp
ENSMUSP00000339727
resolver
enst
ENSMUST00000031382
resolver
enst
ENSMUST00000063905
resolver
enst
ENSMUST00000111561
resolver
genesymbol
Clip1
resolver
genesymbol_syn
Kiaa4046
resolver
genesymbol_syn
Rsn
resolver
uniprot
D3Z2Z1
resolver
uniprot
D3Z3M7
resolver
uniprot
F8WIA1
resolver
uniprot
Q571L7
resolver
uniprot_entry
CLIP1_MOUSE
resolver
uniprot_entry
D3Z2Z1_MOUSE
resolver
uniprot_entry
D3Z3M7_MOUSE
resolver
uniprot_entry
F8WIA1_MOUSE
resolver
uniprot_sec
Q571L7
resolver
amino_acid_sequence
MSMLKPSGLKAPTKILKPGSTALKTPAAAAAPVEKTIPSEKASGPPSSETQEEFVDDFRVGERVWVNGNKPGFIQFLGETQFAPGQWAGIVLDEPIGKNDGSVAGVRYFQCEPLKGIFTRPSKLTRKVQAEDEANGLQAAPGRTASPLSTAAATMVSSSPATPSNIPHKPSQSTAKEPSATPQISNLTKTASESISNLSEAGSVKKGERELKVGDRVLVGGTKAGVVRFLGETDFAKGEWCGVELDEPLGKNDGAVAGTRYFQCQPKYGLFAPVHKVTKIGFPSTTPAKAKAAAVRRVMAATPASLKRSPSASSLSSMSSVASSVSSKPSRTGLLTETSSRYARKISGTTALQEALKEKQQHIEQLLAERDLERAEVAKATSHVGEIEQELALARDGHDQHVLELEAKMDQLRTMVEAADREKVELLNQLEEEKRKVEDLQFRVEEESITKGDLEVATVSEKSRIMELEKDLALRAQEVAELRRRLESSKPPGDVDMSLSLLQEISALQEKLEAIHTDHQGEMTSLKEHFGAREEAFQKEIKALHTATEKLSKENESLRSKLDHANKENSDVIALWKSKLETAIASHQQAMEELKVSFSKGIGTDSAEFAELKTQIERLRLDYQHEIESLQSKQDSERSAHAKEMETMQAKLMKIIKEKEDSLEAVKARLDSAEDQHLVEMEDTLNKLQEAEIKVKELEVLQAKYTEQSEVIGNFTSQLSAVKEKLLDLDALRKANSEGKLELETLRQQLEGAEKQIKNLETERNAESSKANSITKELQEKELVLTGLQDSLNQVNQVKETLEKELQTLKEKFASTSEEAVSAQTRMQDTVNKLHQKEEQFNVLSSELEKLRENLTDMEAKFKEKDDREDQLVKAKEKLENDIAEIMKMSGDNSSQLTKMNDELRLKERSVEELQLKLTKANENASFLQKSIGEVTLKAEQSQQQAARKHEEEKKELEEKLLELEKKMETSYNQCQDLKAKYEKASSETKTKHEEILQNLQKMLADTEDKLKAAQEANRDLMQDMEELKTQADKAKAAQTAEDAMQIMEQMTKEKTETLASLEDTKQTNARLQNELDTLKENNLKTVEELNKSKELLSVENQKMEEFKKEIETLKQAAAQKSQQLSALQEENVKLAEELGRTRDEVTSHQKLEEERSVLNNQLLEMKKRESEFRKDADEEKASLQKSISLTSALLTEKDAELEKLRNEVTVLRGENATAKSLHSVVQTLESDKVKLELKVKNLELQLKENKRQLSSSSGNTDAQAEEDERAQESQIDFLNSVIVDLQRKNQDLKMKVEMMSEAALNGNGEDLNSYDSDDQEKQSKKKPRLFCDICDCFDLHDTEDCPTQAQMSEDPPHSTHHGSRSEERPYCEICEMFGHWATNCNDDETF
uniprot
proteins
function
FUNCTION: Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. {ECO:0000250|UniProtKB:P30622}.
uniprot
proteins
mass_dalton
155814
uniprot
proteins
post_translational_modification
PTM: Phosphorylated (PubMed:26972003). Phosphorylation induces conformational changes by increasing the affinity of the N-terminus for C-terminus, resulting in inhibition of its function thus decreasing its binding to microtubules and DCTN1. Exhibits a folded, autoinhibited conformation when phosphorylated and an open conformation when dephosphorylated with increased binding affinity to microtubules and DCTN1. Phosphorylation regulates its recruitment to tyrosinated microtubules and the recruitment of vesicular cargo to microtubules in neurons. Phosphorylation by MTOR may positively regulate CLIP1 association with microtubules (By similarity). {ECO:0000250|UniProtKB:P30622, ECO:0000250|UniProtKB:Q9JK25, ECO:0000269|PubMed:26972003}.
uniprot
proteins
pubmed
15345747
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16954346
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
18854161
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
26972003
uniprot
proteins
pubmed
35547804
uniprot
proteins
sequence_length
1391
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30622}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P30622}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, ruffle {ECO:0000250|UniProtKB:P30622}. Note=Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules (PubMed:16954346). Accumulates in plasma membrane regions with ruffling and protrusions. Associates with the membranes of intermediate macropinocytic vesicles (By similarity). {ECO:0000250|UniProtKB:P30622, ECO:0000269|PubMed:16954346}.
uniprot
proteins