CLIP1_MOUSE - dbPTM
CLIP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLIP1_MOUSE
UniProt AC Q922J3
Protein Name CAP-Gly domain-containing linker protein 1
Gene Name Clip1
Organism Mus musculus (Mouse).
Sequence Length 1391
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Cell projection, ruffle . Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules (PubMed
Protein Description 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..
Protein Sequence MSMLKPSGLKAPTKILKPGSTALKTPAAAAAPVEKTIPSEKASGPPSSETQEEFVDDFRVGERVWVNGNKPGFIQFLGETQFAPGQWAGIVLDEPIGKNDGSVAGVRYFQCEPLKGIFTRPSKLTRKVQAEDEANGLQAAPGRTASPLSTAAATMVSSSPATPSNIPHKPSQSTAKEPSATPQISNLTKTASESISNLSEAGSVKKGERELKVGDRVLVGGTKAGVVRFLGETDFAKGEWCGVELDEPLGKNDGAVAGTRYFQCQPKYGLFAPVHKVTKIGFPSTTPAKAKAAAVRRVMAATPASLKRSPSASSLSSMSSVASSVSSKPSRTGLLTETSSRYARKISGTTALQEALKEKQQHIEQLLAERDLERAEVAKATSHVGEIEQELALARDGHDQHVLELEAKMDQLRTMVEAADREKVELLNQLEEEKRKVEDLQFRVEEESITKGDLEVATVSEKSRIMELEKDLALRAQEVAELRRRLESSKPPGDVDMSLSLLQEISALQEKLEAIHTDHQGEMTSLKEHFGAREEAFQKEIKALHTATEKLSKENESLRSKLDHANKENSDVIALWKSKLETAIASHQQAMEELKVSFSKGIGTDSAEFAELKTQIERLRLDYQHEIESLQSKQDSERSAHAKEMETMQAKLMKIIKEKEDSLEAVKARLDSAEDQHLVEMEDTLNKLQEAEIKVKELEVLQAKYTEQSEVIGNFTSQLSAVKEKLLDLDALRKANSEGKLELETLRQQLEGAEKQIKNLETERNAESSKANSITKELQEKELVLTGLQDSLNQVNQVKETLEKELQTLKEKFASTSEEAVSAQTRMQDTVNKLHQKEEQFNVLSSELEKLRENLTDMEAKFKEKDDREDQLVKAKEKLENDIAEIMKMSGDNSSQLTKMNDELRLKERSVEELQLKLTKANENASFLQKSIGEVTLKAEQSQQQAARKHEEEKKELEEKLLELEKKMETSYNQCQDLKAKYEKASSETKTKHEEILQNLQKMLADTEDKLKAAQEANRDLMQDMEELKTQADKAKAAQTAEDAMQIMEQMTKEKTETLASLEDTKQTNARLQNELDTLKENNLKTVEELNKSKELLSVENQKMEEFKKEIETLKQAAAQKSQQLSALQEENVKLAEELGRTRDEVTSHQKLEEERSVLNNQLLEMKKRESEFRKDADEEKASLQKSISLTSALLTEKDAELEKLRNEVTVLRGENATAKSLHSVVQTLESDKVKLELKVKNLELQLKENKRQLSSSSGNTDAQAEEDERAQESQIDFLNSVIVDLQRKNQDLKMKVEMMSEAALNGNGEDLNSYDSDDQEKQSKKKPRLFCDICDCFDLHDTEDCPTQAQMSEDPPHSTHHGSRSEERPYCEICEMFGHWATNCNDDETF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSMLKPSGL
------CCCCCCCCC
44.0929176673
20PhosphorylationTKILKPGSTALKTPA
CCCCCCCCCCCCCCH
21.0229176673
21PhosphorylationKILKPGSTALKTPAA
CCCCCCCCCCCCCHH
41.7629176673
43PhosphorylationTIPSEKASGPPSSET
CCCCHHCCCCCCCCC
64.0030635358
47PhosphorylationEKASGPPSSETQEEF
HHCCCCCCCCCHHHH
43.8925521595
48PhosphorylationKASGPPSSETQEEFV
HCCCCCCCCCHHHHH
50.8930635358
50PhosphorylationSGPPSSETQEEFVDD
CCCCCCCCHHHHHHH
43.1422942356
144PhosphorylationLQAAPGRTASPLSTA
CCCCCCCCCCCHHHH
37.0827742792
146PhosphorylationAAPGRTASPLSTAAA
CCCCCCCCCHHHHHH
26.2627742792
149PhosphorylationGRTASPLSTAAATMV
CCCCCCHHHHHHHHH
21.2725159016
150O-linked_GlycosylationRTASPLSTAAATMVS
CCCCCHHHHHHHHHC
28.1822517741
150PhosphorylationRTASPLSTAAATMVS
CCCCCHHHHHHHHHC
28.1825159016
154PhosphorylationPLSTAAATMVSSSPA
CHHHHHHHHHCCCCC
17.2425159016
157PhosphorylationTAAATMVSSSPATPS
HHHHHHHCCCCCCCC
17.8025777480
158PhosphorylationAAATMVSSSPATPSN
HHHHHHCCCCCCCCC
29.0025777480
159PhosphorylationAATMVSSSPATPSNI
HHHHHCCCCCCCCCC
15.8525777480
162PhosphorylationMVSSSPATPSNIPHK
HHCCCCCCCCCCCCC
30.5425777480
164PhosphorylationSSSPATPSNIPHKPS
CCCCCCCCCCCCCCC
42.9325777480
171PhosphorylationSNIPHKPSQSTAKEP
CCCCCCCCCCCCCCC
41.3825777480
173PhosphorylationIPHKPSQSTAKEPSA
CCCCCCCCCCCCCCC
34.3725777480
174PhosphorylationPHKPSQSTAKEPSAT
CCCCCCCCCCCCCCC
33.8325777480
179PhosphorylationQSTAKEPSATPQISN
CCCCCCCCCCCCHHH
45.9628066266
181PhosphorylationTAKEPSATPQISNLT
CCCCCCCCCCHHHHC
21.7728066266
185PhosphorylationPSATPQISNLTKTAS
CCCCCCHHHHCHHHH
22.1228066266
190PhosphorylationQISNLTKTASESISN
CHHHHCHHHHHHHHC
30.1327087446
192PhosphorylationSNLTKTASESISNLS
HHHCHHHHHHHHCHH
36.7927742792
194PhosphorylationLTKTASESISNLSEA
HCHHHHHHHHCHHHC
28.9027087446
196PhosphorylationKTASESISNLSEAGS
HHHHHHHHCHHHCCC
40.7827087446
199PhosphorylationSESISNLSEAGSVKK
HHHHHCHHHCCCCCC
29.6527087446
203PhosphorylationSNLSEAGSVKKGERE
HCHHHCCCCCCCCCE
37.5027087446
284PhosphorylationVTKIGFPSTTPAKAK
EEECCCCCCCHHHHH
42.5226745281
285PhosphorylationTKIGFPSTTPAKAKA
EECCCCCCCHHHHHH
36.7226643407
286PhosphorylationKIGFPSTTPAKAKAA
ECCCCCCCHHHHHHH
26.1126745281
302PhosphorylationVRRVMAATPASLKRS
HHHHHHCCHHHHCCC
15.1728066266
305PhosphorylationVMAATPASLKRSPSA
HHHCCHHHHCCCCCC
35.3126824392
309PhosphorylationTPASLKRSPSASSLS
CHHHHCCCCCCHHHH
22.9428725479
311PhosphorylationASLKRSPSASSLSSM
HHHCCCCCCHHHHHH
41.8727742792
313PhosphorylationLKRSPSASSLSSMSS
HCCCCCCHHHHHHHH
35.8327742792
314PhosphorylationKRSPSASSLSSMSSV
CCCCCCHHHHHHHHH
31.8027742792
316PhosphorylationSPSASSLSSMSSVAS
CCCCHHHHHHHHHHH
26.4125619855
317PhosphorylationPSASSLSSMSSVASS
CCCHHHHHHHHHHHH
28.1625619855
318OxidationSASSLSSMSSVASSV
CCHHHHHHHHHHHHC
2.8817242355
319PhosphorylationASSLSSMSSVASSVS
CHHHHHHHHHHHHCC
24.4925619855
320PhosphorylationSSLSSMSSVASSVSS
HHHHHHHHHHHHCCC
17.0425619855
323PhosphorylationSSMSSVASSVSSKPS
HHHHHHHHHCCCCCC
29.1725619855
324PhosphorylationSMSSVASSVSSKPSR
HHHHHHHHCCCCCCC
19.1125619855
326PhosphorylationSSVASSVSSKPSRTG
HHHHHHCCCCCCCCC
34.2926643407
327PhosphorylationSVASSVSSKPSRTGL
HHHHHCCCCCCCCCC
46.5626643407
330PhosphorylationSSVSSKPSRTGLLTE
HHCCCCCCCCCCCCH
46.3325619855
338PhosphorylationRTGLLTETSSRYARK
CCCCCCHHHHHHHHH
27.1129176673
339PhosphorylationTGLLTETSSRYARKI
CCCCCHHHHHHHHHH
13.4429176673
340PhosphorylationGLLTETSSRYARKIS
CCCCHHHHHHHHHHH
36.4129176673
347PhosphorylationSRYARKISGTTALQE
HHHHHHHHCHHHHHH
32.8726824392
349PhosphorylationYARKISGTTALQEAL
HHHHHHCHHHHHHHH
11.3426824392
350PhosphorylationARKISGTTALQEALK
HHHHHCHHHHHHHHH
28.9727742792
414PhosphorylationAKMDQLRTMVEAADR
HHHHHHHHHHHHHHH
33.8721183079
460PhosphorylationDLEVATVSEKSRIME
CEEEEECCCHHHHHH
34.6526026062
463PhosphorylationVATVSEKSRIMELEK
EEECCCHHHHHHHHH
24.0022942356
552PhosphorylationHTATEKLSKENESLR
HHHHHHHHHHCHHHH
49.3323737553
557PhosphorylationKLSKENESLRSKLDH
HHHHHCHHHHHHHHH
40.4423737553
586PhosphorylationKLETAIASHQQAMEE
HHHHHHHHHHHHHHH
18.7325338131
662PhosphorylationIIKEKEDSLEAVKAR
HHHHHHHHHHHHHHH
29.2429899451
672PhosphorylationAVKARLDSAEDQHLV
HHHHHHHCHHHHHHH
37.8425521595
684PhosphorylationHLVEMEDTLNKLQEA
HHHHHHHHHHHHHHH
20.9421183079
723UbiquitinationTSQLSAVKEKLLDLD
HHHHHHHHHHHCCHH
49.17-
817PhosphorylationKEKFASTSEEAVSAQ
HHHHCCCCHHHHHHH
30.8321454597
822PhosphorylationSTSEEAVSAQTRMQD
CCCHHHHHHHHHHHH
23.0021454597
825PhosphorylationEEAVSAQTRMQDTVN
HHHHHHHHHHHHHHH
28.0221454597
874AcetylationDREDQLVKAKEKLEN
CHHHHHHHHHHHHHH
63.4319852181
890PhosphorylationIAEIMKMSGDNSSQL
HHHHHHHHCCCHHHH
37.1619131326
910PhosphorylationELRLKERSVEELQLK
HHHHHHHCHHHHHHH
34.6721183079
919PhosphorylationEELQLKLTKANENAS
HHHHHHHHHHHCCHH
26.9028059163
931PhosphorylationNASFLQKSIGEVTLK
CHHHHHHHHHHHHHH
23.9021743459
1029AcetylationMQDMEELKTQADKAK
HHHHHHHHHHHHHHH
41.706566133
1052PhosphorylationMQIMEQMTKEKTETL
HHHHHHHHHHHHHHH
35.4326026062
1058PhosphorylationMTKEKTETLASLEDT
HHHHHHHHHHCHHHH
32.6229899451
1061PhosphorylationEKTETLASLEDTKQT
HHHHHHHCHHHHHHH
35.0929899451
1078PhosphorylationRLQNELDTLKENNLK
HHHHHHHHHHHCCCH
52.9719854140
1171PhosphorylationLEMKKRESEFRKDAD
HHHHHHHHHHHCCCH
46.1721454597
1183PhosphorylationDADEEKASLQKSISL
CCHHHHHHHHHHHHH
42.2620415495
1187PhosphorylationEKASLQKSISLTSAL
HHHHHHHHHHHHHHH
12.4022324799
1189PhosphorylationASLQKSISLTSALLT
HHHHHHHHHHHHHHC
32.4622324799
1191PhosphorylationLQKSISLTSALLTEK
HHHHHHHHHHHHCCC
12.7429899451
1192PhosphorylationQKSISLTSALLTEKD
HHHHHHHHHHHCCCH
23.3922324799
1196PhosphorylationSLTSALLTEKDAELE
HHHHHHHCCCHHHHH
41.6720415495
1255PhosphorylationKENKRQLSSSSGNTD
HHHHHHHHCCCCCCC
21.6025521595
1256PhosphorylationENKRQLSSSSGNTDA
HHHHHHHCCCCCCCH
36.8030635358
1257PhosphorylationNKRQLSSSSGNTDAQ
HHHHHHCCCCCCCHH
38.6030635358
1258PhosphorylationKRQLSSSSGNTDAQA
HHHHHCCCCCCCHHH
37.7030635358
1261PhosphorylationLSSSSGNTDAQAEED
HHCCCCCCCHHHHHH
35.9230635358
1314PhosphorylationGNGEDLNSYDSDDQE
CCCCCCCCCCCCHHH
37.3027087446
1315PhosphorylationNGEDLNSYDSDDQEK
CCCCCCCCCCCHHHH
20.5629899451
1317PhosphorylationEDLNSYDSDDQEKQS
CCCCCCCCCHHHHHH
34.5527087446
1324PhosphorylationSDDQEKQSKKKPRLF
CCHHHHHHHCCCCCE
58.4727742792
1383PhosphorylationEMFGHWATNCNDDET
HHHCCHHCCCCCCCC
34.80-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
311SPhosphorylationKinasePKA-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLIP1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CLIP1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CLIP1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CLIP1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-199 ANDSER-203, AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.

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