AP1S1_HUMAN - dbPTM
AP1S1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP1S1_HUMAN
UniProt AC P61966
Protein Name AP-1 complex subunit sigma-1A
Gene Name AP1S1
Organism Homo sapiens (Human).
Sequence Length 158
Subcellular Localization Golgi apparatus . Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side . Membrane, clathrin-coated pit . Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.
Protein Description Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules..
Protein Sequence MMRFMLLFSRQGKLRLQKWYLATSDKERKKMVRELMQVVLARKPKMCSFLEWRDLKVVYKRYASLYFCCAIEGQDNELITLELIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTSKKSVLKAIEQADLLQEEDESPRSVLEEMGLA
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
18 (in isoform 2)Ubiquitination-42.2621906983
18 (in isoform 1)Ubiquitination-42.2621906983
18UbiquitinationQGKLRLQKWYLATSD
CCCHHHEEEEECCCH
42.2621906983
20PhosphorylationKLRLQKWYLATSDKE
CHHHEEEEECCCHHH
8.0926074081
23PhosphorylationLQKWYLATSDKERKK
HEEEEECCCHHHHHH
34.5626074081
24PhosphorylationQKWYLATSDKERKKM
EEEEECCCHHHHHHH
40.8726074081
26UbiquitinationWYLATSDKERKKMVR
EEECCCHHHHHHHHH
60.2221906983
26 (in isoform 2)Ubiquitination-60.2221906983
26 (in isoform 1)Ubiquitination-60.2221906983
26AcetylationWYLATSDKERKKMVR
EEECCCHHHHHHHHH
60.2225953088
262-HydroxyisobutyrylationWYLATSDKERKKMVR
EEECCCHHHHHHHHH
60.22-
36SulfoxidationKKMVRELMQVVLARK
HHHHHHHHHHHHHCC
2.1430846556
56 (in isoform 1)Ubiquitination-33.6621906983
56UbiquitinationFLEWRDLKVVYKRYA
CCCCCCHHHHHHHHH
33.6621906983
56 (in isoform 2)Ubiquitination-33.6621906983
87PhosphorylationTLELIHRYVELLDKY
HHHHHHHHHHHHHHH
5.5411169837
94PhosphorylationYVELLDKYFGSVCEL
HHHHHHHHCCCCEEE
16.9111169829
128UbiquitinationGDVQDTSKKSVLKAI
CCCCCCCHHHHHHHH
51.6821906983
128 (in isoform 1)Ubiquitination-51.6821906983
133UbiquitinationTSKKSVLKAIEQADL
CCHHHHHHHHHHHHH
45.202190698
133AcetylationTSKKSVLKAIEQADL
CCHHHHHHHHHHHHH
45.2025953088
133 (in isoform 1)Ubiquitination-45.2021906983
147PhosphorylationLLQEEDESPRSVLEE
HHCCCCCCHHHHHHH
37.6230266825
150PhosphorylationEEDESPRSVLEEMGL
CCCCCHHHHHHHCCC
34.1424076635

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 AP1S1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP1S1_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 AP1S1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP1G2_HUMANAP1G2physical
9733768
AP1G1_HUMANAP1G1physical
9733768
RAB10_HUMANRAB10physical
17353931
S61A1_HUMANSEC61A1physical
17353931
ARMC6_HUMANARMC6physical
17353931
EBLN2_HUMANEBLN2physical
17353931
MOT1_HUMANSLC16A1physical
17353931
AP1G1_HUMANAP1G1physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609313Mental retardation, enteropathy, deafness, peripheral neuropathy, ichthyosis, and keratoderma (MEDNIK)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AP1S1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND MASSSPECTROMETRY.

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