EMAL1_HUMAN - dbPTM
EMAL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EMAL1_HUMAN
UniProt AC O00423
Protein Name Echinoderm microtubule-associated protein-like 1
Gene Name EML1
Organism Homo sapiens (Human).
Sequence Length 815
Subcellular Localization Cytoplasm . Cytoplasm, perinuclear region . Cytoplasm, cytoskeleton . Detected in cytoplasmic punctae. Co-localizes with microtubules (PubMed:24859200). Enriched in perinuclear regions during interphase and in the region of spindle microtubules durin
Protein Description Modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. Required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. Does not affect neuron migration per se..
Protein Sequence MEDGFSSYSSLYDTSSLLQFCNDDSASAASSMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRKGPTKARPLMQTLPLRTTVNNGTVLPKKPTGSLPSPSGVRKETAVPATKSNIKRTSSSERVSPGGRRESNGDSRGNRNRTGSTSSSSSGKKNSESKPKEPVFSAEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGFFDRAVTCIAFSKSNGGTNLCAVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLNKKQGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGKGTNRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTEIPEQFGPIRTVAEGKGDVILIGTTRNFVLQGTLSGDFTPITQGHTDELWGLAIHASKSQFLTCGHDKHATLWDAVGHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTRVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVPSACKQVVSVETTRDIEWATYTCTLGFHVFGVWPEGSDGTDINAVCRAHEKKLLSTGDDFGKVHLFSYPCSQFRAPSHIYGGHSSHVTNVDFLCEDSHLISTGGKDTSIMQWRVI
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
90PhosphorylationKARPLMQTLPLRTTV
CCCCCHHCCCCEEEE
19.1723312004
100PhosphorylationLRTTVNNGTVLPKKP
CEEEEECCEECCCCC
16.4032142685
108PhosphorylationTVLPKKPTGSLPSPS
EECCCCCCCCCCCCC
48.5623403867
110PhosphorylationLPKKPTGSLPSPSGV
CCCCCCCCCCCCCCC
39.3223927012
113PhosphorylationKPTGSLPSPSGVRKE
CCCCCCCCCCCCCCC
36.6726055452
113 (in isoform 3)Phosphorylation-36.6725849741
115PhosphorylationTGSLPSPSGVRKETA
CCCCCCCCCCCCCCC
55.0130266825
127PhosphorylationETAVPATKSNIKRTS
CCCCCCCCCCCCCCC
43.5432645325
132 (in isoform 3)Phosphorylation-35.7222210691
133PhosphorylationTKSNIKRTSSSERVS
CCCCCCCCCCCCCCC
28.1420363803
134 (in isoform 3)Phosphorylation-35.5822210691
134PhosphorylationKSNIKRTSSSERVSP
CCCCCCCCCCCCCCC
35.5826699800
135PhosphorylationSNIKRTSSSERVSPG
CCCCCCCCCCCCCCC
35.2920363803
136PhosphorylationNIKRTSSSERVSPGG
CCCCCCCCCCCCCCC
29.2326699800
140PhosphorylationTSSSERVSPGGRRES
CCCCCCCCCCCCCCC
24.8520363803
144 (in isoform 3)Phosphorylation-45.1422210691
145 (in isoform 3)Phosphorylation-55.7822210691
147PhosphorylationSPGGRRESNGDSRGN
CCCCCCCCCCCCCCC
44.2830242111
151PhosphorylationRRESNGDSRGNRNRT
CCCCCCCCCCCCCCC
43.4126699800
154 (in isoform 3)Phosphorylation-36.6225849741
158PhosphorylationSRGNRNRTGSTSSSS
CCCCCCCCCCCCCCC
38.7526699800
159PhosphorylationRGNRNRTGSTSSSSS
CCCCCCCCCCCCCCC
26.2032645325
159 (in isoform 3)Phosphorylation-26.2025849741
160PhosphorylationGNRNRTGSTSSSSSG
CCCCCCCCCCCCCCC
25.2226657352
161PhosphorylationNRNRTGSTSSSSSGK
CCCCCCCCCCCCCCC
33.6926699800
162PhosphorylationRNRTGSTSSSSSGKK
CCCCCCCCCCCCCCC
29.8926699800
163PhosphorylationNRTGSTSSSSSGKKN
CCCCCCCCCCCCCCC
34.0426699800
171PhosphorylationSSSGKKNSESKPKEP
CCCCCCCCCCCCCCC
52.7229214152
173PhosphorylationSGKKNSESKPKEPVF
CCCCCCCCCCCCCCE
54.8223186163
181PhosphorylationKPKEPVFSAEEGYVK
CCCCCCEECCCCEEE
34.7023186163
186PhosphorylationVFSAEEGYVKMFLRG
CEECCCCEEEEEECC
10.5219060867
202AcetylationPVTMYMPKDQVDSYS
EEEEECCHHHCCCCE
44.2410534121
222UbiquitinationELPTKRLKLEWVYGY
ECCCCCEEEEEEEEE
48.68-
396PhosphorylationTCGKSHLYFWTLEGS
EECCCEEEEEEEECC
7.52-
448PhosphorylationILVWGKGTNRISYAV
EEEECCCCCCEEEEE
25.47-
452PhosphorylationGKGTNRISYAVQGAH
CCCCCCEEEEEECCH
12.10-
453PhosphorylationKGTNRISYAVQGAHE
CCCCCEEEEEECCHH
14.39-
473PhosphorylationLCMLRDGTLVSGGGK
EEEEECCEEECCCCC
28.42-
476PhosphorylationLRDGTLVSGGGKDRK
EECCEEECCCCCCCE
34.53-
486PhosphorylationGKDRKLISWSGNYQK
CCCCEEEECCCCHHH
26.1429083192
488PhosphorylationDRKLISWSGNYQKLR
CCEEEECCCCHHHHC
15.4629083192
491PhosphorylationLISWSGNYQKLRKTE
EEECCCCHHHHCCCC
15.5629083192
532PhosphorylationFVLQGTLSGDFTPIT
EEEECEECCCCEECC
35.8322210691
536PhosphorylationGTLSGDFTPITQGHT
CEECCCCEECCCCCC
20.6522210691
755PhosphorylationAHEKKLLSTGDDFGK
HHHHHEECCCCCCCC
40.5621712546

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 EMAL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EMAL1_HUMAN !!

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 EMAL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
I20L2_HUMANISG20L2physical
16189514
I20L2_HUMANISG20L2physical
19060904
TBA1B_HUMANTUBA1Bphysical
24706829
TBB3_HUMANTUBB3physical
24706829
EMAL1_HUMANEML1physical
25740311
TBA1A_HUMANTUBA1Aphysical
25740311
TBB3_HUMANTUBB3physical
25740311
FBX28_HUMANFBXO28physical
28514442
TBB2A_HUMANTUBB2Aphysical
28514442
EMAL4_HUMANEML4physical
28514442
TBB2B_HUMANTUBB2Bphysical
28514442
TBB5_HUMANTUBBphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EMAL1_HUMAN

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Related Literatures of Post-Translational Modification

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