UN13A_HUMAN - dbPTM
UN13A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UN13A_HUMAN
UniProt AC Q9UPW8
Protein Name Protein unc-13 homolog A
Gene Name UNC13A
Organism Homo sapiens (Human).
Sequence Length 1703
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein. Cell junction, synapse, presynaptic cell membrane
Peripheral membrane protein. Localized to the active zone of presynaptic density. Translocated to the plasma membrane as response to phorbol est
Protein Description Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in most excitatory/glutamatergic but not inhibitory/GABA-mediated synapses (By similarity). Also involved in secretory granule priming in insulin secretion (By similarity). Interacts with FBXO45 (via SRY domain); leading to the degradation of UNC13A by the proteasome (By similarity). Plays a role in dendrite formation by melanocytes. [PubMed: 23999003]
Protein Sequence MSLLCVGVKKAKFDGAQEKFNTYVTLKVQNVKSTTIAVRGSQPSWEQDFMFEINRLDLGLTVEVWNKGLIWDTMVGTVWIPLRTIRQSNEEGPGEWLTLDSQVIMADSEICGTKDPTFHRILLDTRFELPLDIPEEEARYWAKKLEQLNAMRDQDEYSFQDEQDKPLPVPSNQCCNWNYFGWGEQHNDDPDSAVDDRDSDYRSETSNSIPPPYYTTSQPNASVHQYSVRPPPLGSRESYSDSMHSYEEFSEPQALSPTGSSRYASSGELSQGSSQLSEDFDPDEHSLQGSDMEDERDRDSYHSCHSSVSYHKDSPRWDQDEEELEEDLEDFLEEEELPEDEEELEEEEEEVPDDLGSYAQREDVAVAEPKDFKRISLPPAAPGKEDKAPVAPTEAPDMAKVAPKPATPDKVPAAEQIPEAEPPKDEESFRPREDEEGQEGQDSMSRAKANWLRAFNKVRMQLQEARGEGEMSKSLWFKGGPGGGLIIIDSMPDIRKRKPIPLVSDLAMSLVQSRKAGITSALASSTLNNEELKNHVYKKTLQALIYPISCTTPHNFEVWTATTPTYCYECEGLLWGIARQGMRCTECGVKCHEKCQDLLNADCLQRAAEKSSKHGAEDRTQNIIMVLKDRMKIRERNKPEIFELIQEIFAVTKTAHTQQMKAVKQSVLDGTSKWSAKISITVVCAQGLQAKDKTGSSDPYVTVQVGKTKKRTKTIYGNLNPVWEENFHFECHNSSDRIKVRVWDEDDDIKSRVKQRFKRESDDFLGQTIIEVRTLSGEMDVWYNLDKRTDKSAVSGAIRLHISVEIKGEEKVAPYHVQYTCLHENLFHFVTDVQNNGVVKIPDAKGDDAWKVYYDETAQEIVDEFAMRYGVESIYQAMTHFACLSSKYMCPGVPAVMSTLLANINAYYAHTTASTNVSASDRFAASNFGKERFVKLLDQLHNSLRIDLSMYRNNFPASSPERLQDLKSTVDLLTSITFFRMKVQELQSPPRASQVVKDCVKACLNSTYEYIFNNCHELYSREYQTDPAKKGEVLPEEQGPSIKNLDFWSKLITLIVSIIEEDKNSYTPCLNQFPQELNVGKISAEVMWNLFAQDMKYAMEEHDKHRLCKSADYMNLHFKVKWLYNEYVTELPAFKDRVPEYPAWFEPFVIQWLDENEEVSRDFLHGALERDKKDGFQQTSEHALFSCSVVDVFSQLNQSFEIIKKLECPDPQIVGHYMRRFAKTISNVLLQYADIISKDFASYCSKEKEKVPCILMNNTQQLRVQLEKMFEAMGGKELDAEASDILKELQVKLNNVLDELSRVFATSFQPHIEECVKQMGDILSQVKGTGNVPASACSSVAQDADNVLQPIMDLLDSNLTLFAKICEKTVLKRVLKELWKLVMNTMEKTIVLPPLTDQTMIGNLLRKHGKGLEKGRVKLPSHSDGTQMIFNAAKELGQLSKLKDHMVREEAKSLTPKQCAVVELALDTIKQYFHAGGVGLKKTFLEKSPDLQSLRYALSLYTQATDLLIKTFVQTQSAQGLGVEDPVGEVSVHVELFTHPGTGEHKVTVKVVAANDLKWQTSGIFRPFIEVNIIGPQLSDKKRKFATKSKNNSWAPKYNESFQFTLSADAGPECYELQVCVKDYCFAREDRTVGLAVLQLRELAQRGSAACWLPLGRRIHMDDTGLTVLRILSQRSNDEVAKEFVKLKSDTRSAEEGGAAPAP
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
88PhosphorylationPLRTIRQSNEEGPGE
EHHHHHCCCCCCCCC
36.0428270605
98PhosphorylationEGPGEWLTLDSQVIM
CCCCCEEEECCEEEE
29.5928270605
222PhosphorylationTTSQPNASVHQYSVR
CCCCCCCEEEEEECC
27.11-
240PhosphorylationLGSRESYSDSMHSYE
CCCCCCCCCCCCCCC
32.2721601212
242PhosphorylationSRESYSDSMHSYEEF
CCCCCCCCCCCCCCC
16.68-
245PhosphorylationSYSDSMHSYEEFSEP
CCCCCCCCCCCCCCC
26.12-
256PhosphorylationFSEPQALSPTGSSRY
CCCCCCCCCCCCCCC
24.3518510355
260PhosphorylationQALSPTGSSRYASSG
CCCCCCCCCCCCCCC
17.7025307156
376PhosphorylationPKDFKRISLPPAAPG
CCCCCCCCCCCCCCC
38.5722985185
443PhosphorylationEGQEGQDSMSRAKAN
CCCCCCCHHHHHHHH
15.6929978859
445PhosphorylationQEGQDSMSRAKANWL
CCCCCHHHHHHHHHH
32.7929978859
504PhosphorylationRKPIPLVSDLAMSLV
CCCCCHHHHHHHHHH
34.2927251275
694PhosphorylationGLQAKDKTGSSDPYV
CCCCCCCCCCCCCCE
53.0529083192
696PhosphorylationQAKDKTGSSDPYVTV
CCCCCCCCCCCCEEE
36.4829083192
697PhosphorylationAKDKTGSSDPYVTVQ
CCCCCCCCCCCEEEE
43.9029083192
700PhosphorylationKTGSSDPYVTVQVGK
CCCCCCCCEEEEECC
17.4718083107
702PhosphorylationGSSDPYVTVQVGKTK
CCCCCCEEEEECCCC
10.2029083192
708PhosphorylationVTVQVGKTKKRTKTI
EEEEECCCCCEEEEE
35.5529083192
734PhosphorylationFHFECHNSSDRIKVR
CEEECCCCCCCEEEE
15.2220873877
735PhosphorylationHFECHNSSDRIKVRV
EEECCCCCCCEEEEE
35.9020873877
750UbiquitinationWDEDDDIKSRVKQRF
CCCCCCHHHHHHHHH
38.92-
869PhosphorylationVDEFAMRYGVESIYQ
HHHHHHHHCHHHHHH
16.67-
879PhosphorylationESIYQAMTHFACLSS
HHHHHHHHHHHHHCC
19.5028985074
885PhosphorylationMTHFACLSSKYMCPG
HHHHHHHCCCCCCCC
25.3528985074
888PhosphorylationFACLSSKYMCPGVPA
HHHHCCCCCCCCHHH
13.09-
943PhosphorylationLLDQLHNSLRIDLSM
HHHHHHHHHCCCHHH
14.3128857561
968PhosphorylationERLQDLKSTVDLLTS
HHHHHHHHHHHHHHH
40.7430622161
969PhosphorylationRLQDLKSTVDLLTSI
HHHHHHHHHHHHHHH
19.2230622161
974PhosphorylationKSTVDLLTSITFFRM
HHHHHHHHHHHHHHH
25.9430622161
975PhosphorylationSTVDLLTSITFFRMK
HHHHHHHHHHHHHHH
21.4330622161
977PhosphorylationVDLLTSITFFRMKVQ
HHHHHHHHHHHHHHH
19.2530622161
988PhosphorylationMKVQELQSPPRASQV
HHHHHHCCCCCHHHH
49.8825159151
993PhosphorylationLQSPPRASQVVKDCV
HCCCCCHHHHHHHHH
25.4525627689
1020PhosphorylationNNCHELYSREYQTDP
CCHHHHHCCCCCCCH
31.1224719451
1245PhosphorylationKDFASYCSKEKEKVP
HHHHHHHCCCCCCCC
35.30-
1483PhosphorylationGGVGLKKTFLEKSPD
CCCCCCHHHHHHCCC
31.6826074081
1488PhosphorylationKKTFLEKSPDLQSLR
CHHHHHHCCCHHHHH
17.8026074081
1493PhosphorylationEKSPDLQSLRYALSL
HHCCCHHHHHHHHHH
23.3126074081
1581AcetylationIGPQLSDKKRKFATK
ECCCCCHHHCCCCCC
51.6119829187
1582AcetylationGPQLSDKKRKFATKS
CCCCCHHHCCCCCCC
66.8519829197
1587PhosphorylationDKKRKFATKSKNNSW
HHHCCCCCCCCCCCC
38.70-
1593PhosphorylationATKSKNNSWAPKYNE
CCCCCCCCCCCCCCC
33.7322985185
1673PhosphorylationLTVLRILSQRSNDEV
HHHHHHHHHCCCHHH
22.6024719451
1689PhosphorylationKEFVKLKSDTRSAEE
HHHHHHHCCCCCHHC
55.4329083192
1691PhosphorylationFVKLKSDTRSAEEGG
HHHHHCCCCCHHCCC
33.3529083192
1693PhosphorylationKLKSDTRSAEEGGAA
HHHCCCCCHHCCCCC
41.9729083192

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
-KUbiquitinationE3 ubiquitin ligaseFBXO44Q9H4M3
PMID:24658274

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UN13A_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 UN13A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBSP1_MOUSEFbxo45physical
19996097
UBX10_HUMANUBXN10physical
26389662

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 UN13A_HUMAN

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Related Literatures of Post-Translational Modification

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