CARL1_MOUSE - dbPTM
CARL1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CARL1_MOUSE
UniProt AC Q6EDY6
Protein Name F-actin-uncapping protein LRRC16A {ECO:0000250|UniProtKB:Q5VZK9}
Gene Name Carmil1 {ECO:0000250|UniProtKB:Q5VZK9}
Organism Mus musculus (Mouse).
Sequence Length 1374
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Cell membrane . Cell projection, lamellipodium . Found on macropinosomes (By similarity). Colocalized with heterodimeric capping protein (CP) and F-actin in lamellipodia but not with F-actin in stress fibers (Pub
Protein Description Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments. [PubMed: 16054028 Plays a role in lamellipodial protrusion formations and cell migration]
Protein Sequence MTDESSDVPRELMESIKDVIGRKIKISVKKKVKLEVKGDRVENKVLVLTSCRAFLLSARIPSKLELTFSYLEIHGVICHKPAQMVVETEKCNMSMKMVSPEDVSEVLAHIGTCLRRIFPGLSPLRIMKKVSMEPSERLASLQALWDSQTLAEPGPCGGFSQMYACVCDWLGFSYKEEVQWDVDTIYLTQDTRELNLQDFSHLEHRDLIPIIAALEYNQWFTKLSSKDLKLSTDVCEQILRVVSRSNRLEELVLENAGLRIDFAQKLAGALAHNPNSGLHTINLAGNSLEDRGVSSLSIQFAKLPKGLKHLNLSKTSLSPKGVNSLCQSLSANPLTASTLTHLDLSGNALRGDDLSHMYNFLAQPNTIVHLDLSNTECSLEMVCSALLRGCLQCLAVLNLSRSVFSHRKGKEVPPSFKQFFSSSLALIQINLSGTKLSPEPLKALLLGLACNHSLKGVSLDLSNCELGHCLRSGGAQVLEGCIAEIHNITSLDISDNGLESDLSTLIVWLSKNRSIQHLALGKNFNNMKSKNLTPVLDNLVQMIQDEDSPLQSLSLADSKLKAEVTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLRFMPIPMYDAAQALKTNPEKTEEALQKIENYLLRNHETRKYLQEQAYRLQQGIVTSTTQQMIDRICVKVQDHLNSLRACGGDAIQEDLKAAERLMRDAKNSKTLLPNLYHVGGASWAGASGLSSSPIQETLESMAGEVTRVVDEQLKDLLESMVDAAETLCPNVMRKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDSLSSSHRKLANHFSRLNKSLPQREDLEVELVEEKPVKRAILTVEDLTEVERLEDLDTCMMTPKSKRKSIHSRMLRPVSRAFEMEFDLDKALEEVPIHIEDPPFPSVRQEKRSSGLISELPSEEGRRLEHFTKLRPKRNKKQQPTQAAVCTISILPQDGEQNGLMGRVDEGVDEFFTKKVTKMDCKRSSSRSSDAHELGEGDEKKKRDSRRSGFLNLIKSRSRSERPPTVLMTEELSSPKGAMRSPPVDTTRKEIKAAEHNGAPDRTEEIKTPEPLEEGPAEEAGRAERSDSRGSPQGGRRYVQVMGSGLLAEMKAKQERRAACAQKKLGNDVISQDPSSPVSCNTERLEGGATVPKLQPGLPEARFGSGTPEKNAKAEPRVDGGCRSRSSSSMPTSPKPLLQSPKPSPSARPSIPQKPRTASRPEDTPDSPSGPSSPKVALLPPILKKVSSDKERDGQNSSQSSPRSFSQEASRRSWGPAQEYQEQKQRSSGKDGHQGSKCSDSGEEAEKEFIFV
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
1Acetylation-------MTDESSDV
-------CCCCCCHH
-
2Phosphorylation------MTDESSDVP
------CCCCCCHHC
28576409
6Phosphorylation--MTDESSDVPRELM
--CCCCCCHHCHHHH
29895711
57PhosphorylationSCRAFLLSARIPSKL
HHHHHHHHCCCCCCC
21183079
62PhosphorylationLLSARIPSKLELTFS
HHHCCCCCCCEEEEE
21183079
122PhosphorylationRRIFPGLSPLRIMKK
HHHCCCCCHHHHHHH
26824392
308UbiquitinationAKLPKGLKHLNLSKT
CCCCCCCCCCCCCCC
-
324PhosphorylationLSPKGVNSLCQSLSA
CCHHHHHHHHHHHCC
25777480
328PhosphorylationGVNSLCQSLSANPLT
HHHHHHHHHCCCCCC
25777480
330PhosphorylationNSLCQSLSANPLTAS
HHHHHHHCCCCCCHH
25777480
335PhosphorylationSLSANPLTASTLTHL
HHCCCCCCHHHCCEE
25777480
337PhosphorylationSANPLTASTLTHLDL
CCCCCCHHHCCEEEC
25777480
338PhosphorylationANPLTASTLTHLDLS
CCCCCHHHCCEEECC
25777480
340PhosphorylationPLTASTLTHLDLSGN
CCCHHHCCEEECCCC
25777480
345PhosphorylationTLTHLDLSGNALRGD
HCCEEECCCCCCCCC
25777480
578PhosphorylationLGSNTSLTKVDISGN
CCCCCCCEEEECCCC
22807455
604UbiquitinationKALQINTKLRTVIWD
HHHHHCCCCCEEEEC
-
736PhosphorylationRDAKNSKTLLPNLYH
HHHHHCCCCCCCCEE
26239621
757PhosphorylationAGASGLSSSPIQETL
CCCCCCCCCCHHHHH
26239621
758PhosphorylationGASGLSSSPIQETLE
CCCCCCCCCHHHHHH
26239621
766PhosphorylationPIQETLESMAGEVTR
CHHHHHHHHCHHHHH
26239621
823UbiquitinationSIPRTFVKNVLLEQS
CCCHHHHHHHHHHHH
-
830PhosphorylationKNVLLEQSGIDILNK
HHHHHHHHCHHHHHH
25521595
862PhosphorylationDEILDSLSSSHRKLA
HHHHHHCCHHHHHHH
21183079
873PhosphorylationRKLANHFSRLNKSLP
HHHHHHHHHHHHCCC
21183079
878PhosphorylationHFSRLNKSLPQREDL
HHHHHHHCCCCCCCC
28973931
901PhosphorylationPVKRAILTVEDLTEV
CCCEEEEEHHHCCHH
28973931
906PhosphorylationILTVEDLTEVERLED
EEEHHHCCHHHCHHH
23140645
916PhosphorylationERLEDLDTCMMTPKS
HCHHHCCCCCCCCHH
25619855
920PhosphorylationDLDTCMMTPKSKRKS
HCCCCCCCCHHHHHC
25521595
937PhosphorylationSRMLRPVSRAFEMEF
HHCHHHHHHHHHEEE
26643407
964PhosphorylationIEDPPFPSVRQEKRS
CCCCCCCCCCHHHHH
-
971PhosphorylationSVRQEKRSSGLISEL
CCCHHHHHCCCCCCC
27087446
972PhosphorylationVRQEKRSSGLISELP
CCHHHHHCCCCCCCC
25521595
976PhosphorylationKRSSGLISELPSEEG
HHHCCCCCCCCCCCC
25619855
980PhosphorylationGLISELPSEEGRRLE
CCCCCCCCCCCCCHH
25619855
1046PhosphorylationTKMDCKRSSSRSSDA
CHHHCCCCCCCCCCH
20469934
1047PhosphorylationKMDCKRSSSRSSDAH
HHHCCCCCCCCCCHH
27841257
1048PhosphorylationMDCKRSSSRSSDAHE
HHCCCCCCCCCCHHH
29550500
1050PhosphorylationCKRSSSRSSDAHELG
CCCCCCCCCCHHHCC
27087446
1051PhosphorylationKRSSSRSSDAHELGE
CCCCCCCCCHHHCCC
29514104
1067PhosphorylationDEKKKRDSRRSGFLN
CCHHHHHHHHHHHHH
-
1070PhosphorylationKKRDSRRSGFLNLIK
HHHHHHHHHHHHHHH
26239621
1087PhosphorylationSRSERPPTVLMTEEL
CCCCCCCEEEEECCC
29514104
1095PhosphorylationVLMTEELSSPKGAMR
EEEECCCCCCCCCCC
26643407
1096PhosphorylationLMTEELSSPKGAMRS
EEECCCCCCCCCCCC
26239621
1103PhosphorylationSPKGAMRSPPVDTTR
CCCCCCCCCCCCCCH
29895711
1130PhosphorylationDRTEEIKTPEPLEEG
CCCCCCCCCCCCCCC
21149613
1148PhosphorylationEAGRAERSDSRGSPQ
HHCCCCCCCCCCCCC
27681418
1150PhosphorylationGRAERSDSRGSPQGG
CCCCCCCCCCCCCCC
23140645
1153PhosphorylationERSDSRGSPQGGRRY
CCCCCCCCCCCCHHH
25521595
1160PhosphorylationSPQGGRRYVQVMGSG
CCCCCHHHEEEECCH
29514104
1166PhosphorylationRYVQVMGSGLLAEMK
HHEEEECCHHHHHHH
29514104
1193PhosphorylationKLGNDVISQDPSSPV
HHCCCCCCCCCCCCC
26643407
1197PhosphorylationDVISQDPSSPVSCNT
CCCCCCCCCCCCCCC
25619855
1198PhosphorylationVISQDPSSPVSCNTE
CCCCCCCCCCCCCCC
25619855
1201PhosphorylationQDPSSPVSCNTERLE
CCCCCCCCCCCCCCC
25619855
1204PhosphorylationSSPVSCNTERLEGGA
CCCCCCCCCCCCCCC
25619855
1227PhosphorylationLPEARFGSGTPEKNA
CCHHHCCCCCCCCCC
27149854
1229PhosphorylationEARFGSGTPEKNAKA
HHHCCCCCCCCCCCC
26643407
1248PhosphorylationDGGCRSRSSSSMPTS
CCCCCCCCCCCCCCC
23684622
1249PhosphorylationGGCRSRSSSSMPTSP
CCCCCCCCCCCCCCC
23684622
1250PhosphorylationGCRSRSSSSMPTSPK
CCCCCCCCCCCCCCC
23684622
1251PhosphorylationCRSRSSSSMPTSPKP
CCCCCCCCCCCCCCC
26643407
1254PhosphorylationRSSSSMPTSPKPLLQ
CCCCCCCCCCCCCCC
26643407
1255PhosphorylationSSSSMPTSPKPLLQS
CCCCCCCCCCCCCCC
26643407
1262PhosphorylationSPKPLLQSPKPSPSA
CCCCCCCCCCCCCCC
26824392
1266PhosphorylationLLQSPKPSPSARPSI
CCCCCCCCCCCCCCC
26643407
1268PhosphorylationQSPKPSPSARPSIPQ
CCCCCCCCCCCCCCC
26643407
1272PhosphorylationPSPSARPSIPQKPRT
CCCCCCCCCCCCCCC
26643407
1279PhosphorylationSIPQKPRTASRPEDT
CCCCCCCCCCCCCCC
25619855
1281PhosphorylationPQKPRTASRPEDTPD
CCCCCCCCCCCCCCC
25619855
1286PhosphorylationTASRPEDTPDSPSGP
CCCCCCCCCCCCCCC
25619855
1289PhosphorylationRPEDTPDSPSGPSSP
CCCCCCCCCCCCCCC
25521595
1291PhosphorylationEDTPDSPSGPSSPKV
CCCCCCCCCCCCCCC
27087446
1294PhosphorylationPDSPSGPSSPKVALL
CCCCCCCCCCCCCCC
25521595
1295PhosphorylationDSPSGPSSPKVALLP
CCCCCCCCCCCCCCC
25521595
1319PhosphorylationKERDGQNSSQSSPRS
CCCCCCCCCCCCCCC
-
1320PhosphorylationERDGQNSSQSSPRSF
CCCCCCCCCCCCCCC
19367708
1322PhosphorylationDGQNSSQSSPRSFSQ
CCCCCCCCCCCCCCH
29899451
1323PhosphorylationGQNSSQSSPRSFSQE
CCCCCCCCCCCCCHH
26824392
1326PhosphorylationSSQSSPRSFSQEASR
CCCCCCCCCCHHHHH
26643407
1328PhosphorylationQSSPRSFSQEASRRS
CCCCCCCCHHHHHHC
26643407
1332PhosphorylationRSFSQEASRRSWGPA
CCCCHHHHHHCCCHH
26643407
1335PhosphorylationSQEASRRSWGPAQEY
CHHHHHHCCCHHHHH
25521595
1342PhosphorylationSWGPAQEYQEQKQRS
CCCHHHHHHHHHHHH
25619855
1358PhosphorylationGKDGHQGSKCSDSGE
CCCCCCCCCCCCCCC
21183079
1361PhosphorylationGHQGSKCSDSGEEAE
CCCCCCCCCCCCHHH
26824392
1363PhosphorylationQGSKCSDSGEEAEKE
CCCCCCCCCCHHHHH
16141072

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

Oops, there are no upstream regulatory protein records of CARL1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CARL1_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 CARL1_MOUSE !!

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

Oops, there are no PPI records of CARL1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CARL1_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP