Clip1
entrez
65201
canonical
uniprot
Q9JK25
canonical
ensembl
ENSRNOG00000001247
resolver
ensembl
ENSRNOG00055014674
resolver
ensembl
ENSRNOG00060002932
resolver
ensembl
ENSRNOG00065006227
resolver
ensp
ENSRNOP00000072766
resolver
ensp
ENSRNOP00000073711
resolver
ensp
ENSRNOP00000079550
resolver
ensp
ENSRNOP00000087368
resolver
ensp
ENSRNOP00000090148
resolver
ensp
ENSRNOP00000092485
resolver
ensp
ENSRNOP00000093663
resolver
ensp
ENSRNOP00000093783
resolver
ensp
ENSRNOP00055020776
resolver
ensp
ENSRNOP00060003507
resolver
ensp
ENSRNOP00065006906
resolver
enst
ENSRNOT00000102474
resolver
enst
ENSRNOT00000105301
resolver
enst
ENSRNOT00000105680
resolver
enst
ENSRNOT00000110644
resolver
enst
ENSRNOT00055025456
resolver
enst
ENSRNOT00060004846
resolver
enst
ENSRNOT00065009597
resolver
genesymbol
Clip1
resolver
genesymbol_syn
Cyln1
resolver
genesymbol_syn
Rsn
resolver
uniprot
A0A0G2K3T3
resolver
uniprot
A0A8I5ZNR1
resolver
uniprot
A0A8I6A7M2
resolver
uniprot
A0A8I6AFK9
resolver
uniprot
A0A8I6AKB1
resolver
uniprot_entry
A0A8I5ZNR1_RAT
resolver
uniprot_entry
A0A8I6A7M2_RAT
resolver
uniprot_entry
A0A8I6AFK9_RAT
resolver
uniprot_entry
A0A8I6AKB1_RAT
resolver
uniprot_entry
CLIP1_RAT
resolver
uniprot_sec
A0A0G2K3T3
resolver
amino_acid_sequence
MSMLKPSGLKAPTKILKPGSTALKTPAAAAAPLEKTVPSEKASGPPSSETQEEFVDDFRVGERVWVNGNKPGFIQFLGETQFAPGQWAGIVLDEPIGKNDGSVAGVRYFQCEPLKGIFTRPSKLTRKVQAEDEANGLQTAHARAASPLSTAAATMVSSSPATPSNIPQKPSQPVAKETSATPQISNLTKTASESISNLSEAGSVKKGERELKIGDRVLVGGTKAGVVRFLGETDFAKGEWCGVELDEPLGKNDGAVAGTRYFQCQPKYGLFAPVHKVTKIGFPSTTPAKAKAAAVRRVMATTPASLKRSPSASSLSSMSSVASSVSSKPSRTGLLTETSSRYARKISGTTALQEALKEKQQHIEQLLAERDLERAEVAKATSHVGEIEQELALARDGHDQHVLELEAKMDQLRTMVEAADREKVELLNQLEEEKRKVEDLQFRVEEESITKGDLETQTKLEHARIKELEQSLLFEKTKADKLQRELEDTRVATVSEKSRIMELEKDLALRVQEVAELRRRLESSKPPGDVDMSLSLLQEISALQEKLEVTHTDHQNEVTSLKDHFGTREEMFQKEIKALHAATEKLSKENESLRSKLDHANKENSDVIALWKSKLETAIASHQQAMEELKVSFSKGIGTDSAEFAELKTQIERLRLDYQHEIESLQSKQDSERSAHAKEMESMKAKLMKIIKEKEDSLEAVKARLDTAEDQHLVEMEEMLSKLQEAEIKKEKFASASEEAVSTQTSMQDTVNKLHQKEEQFNMLSSELEKLRENLTDMEAKFKEKDEREDQLVKAKEKLENDIAEIMKMSGDNSSQLTKMNDELRLKERSVEELQLKLTKANENASLLQKSIGEVTLKAEQSQQEAAKKHEEEKKELENKLLELEKKMETSHYQCQDLKAKYEKASSETKIKHEEILQNFQKMLVDTEDKLKAAQEANRDLMQDMEELKSQADKAKAAQTAEDAMQIMEQMTKEKTETLASLEDTKQTNAKLQSELDTLKENNLKTVEELNKSKELLNEENQKMEEFKKEIETLKQAAAQKSQQLSALQEENVKLAEELGRTRDEVTSHQKLEEERSVLNNQLLEMKKSLPSNTLRESEYRKDADEEKASLQKSISLTSALLTEKDAELEKLRNEVTVLRGENASAKSLHSVVQTLESDKVKLELKVKNLELQLKENKRQLSSSSGNTDVQTEEDERAQESQQMIDFLNSVIVDLQRKNQDLKMKVEMMSEAALNGNGEDPNSYDSDDQEKQSKKKPRLFCDICDCFDLHDTEDCPTQAQMSEDPPHSTHHGSRSEERPYCEICEMFGHWATNCNDDETF
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
148279
uniprot
proteins
mutagenesis
MUTAGEN 309; /note="S->A: Phosphodeficient mutant which exhibits an open conformation with a high affinity for microtubules and DCTN1; when associated with A-311; A-313; A-319 and A-320."; /evidence="ECO:0000269|PubMed:20519438, ECO:0000269|PubMed:26972003"; MUTAGEN 309; /note="S->E: Phosphomimetic mutant which exhibits a closed autoinhibited conformation with a low affinity for microtubules and DCTN1; when associated with E-311; E-313; E-319 and E-320."; /evidence="ECO:0000269|PubMed:20519438, ECO:0000269|PubMed:26972003"; MUTAGEN 311; /note="S->A: Phosphodeficient mutant which exhibits an open conformation with a high affinity for microtubules and DCTN1; when associated with A-309; A-313; A-319 and A-320."; /evidence="ECO:0000269|PubMed:20519438, ECO:0000269|PubMed:26972003"; MUTAGEN 311; /note="S->E: Phosphomimetic mutant which exhibits a closed autoinhibited conformation with a low affinity for microtubules and DCTN1; when associated with E-309; E-313; E-319 and E-320."; /evidence="ECO:0000269|PubMed:20519438, ECO:0000269|PubMed:26972003"; MUTAGEN 313; /note="S->A: Phosphodeficient mutant which exhibits an open conformation with a high affinity for microtubules and DCTN1; when associated with A-309; A-311; A-319 and A-320."; /evidence="ECO:0000269|PubMed:20519438, ECO:0000269|PubMed:26972003"; MUTAGEN 313; /note="S->E: Phosphomimetic mutant which exhibits a closed autoinhibited conformation with a low affinity for microtubules and DCTN1; when associated with E-309; E-311; E-319 and E-320."; /evidence="ECO:0000269|PubMed:20519438, ECO:0000269|PubMed:26972003"; MUTAGEN 319; /note="S->A: Phosphodeficient mutant which exhibits an open conformation with a high affinity for microtubules and DCTN1; when associated with A-309; A-311; A-313 and A-320."; /evidence="ECO:0000269|PubMed:20519438, ECO:0000269|PubMed:26972003"; MUTAGEN 319; /note="S->E: Phosphomimetic mutant which exhibits a closed autoinhibited conformation with a low affinity for microtubules and DCTN1; when associated with E-30; E-311; E-313 and E-320."; /evidence="ECO:0000269|PubMed:20519438, ECO:0000269|PubMed:26972003"; MUTAGEN 320; /note="S->A: Phosphodeficient mutant which exhibits an open conformation with a high affinity for microtubules and DCTN1; when associated with A-309; A-311; A-313 and A-319."; /evidence="ECO:0000269|PubMed:20519438, ECO:0000269|PubMed:26972003"; MUTAGEN 320; /note="S->E: Phosphomimetic mutant, exhibits a closed autoinhibited conformation with a low affinity for microtubules and DCTN1; when associated with E-309; E-311; E-313 and E-319."; /evidence="ECO:0000269|PubMed:20519438, ECO:0000269|PubMed:26972003
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. 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 (PubMed:20519438, PubMed:26972003). Phosphorylation by MTOR may positively regulate CLIP1 association with microtubules (By similarity). {ECO:0000250|UniProtKB:P30622, ECO:0000269|PubMed:20519438, ECO:0000269|PubMed:26972003}.
uniprot
proteins
pubmed
11290329
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
20519438
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
26972003
uniprot
proteins
sequence_length
1320
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30622}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26972003}. 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:26972003). 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:26972003}.
uniprot
proteins