Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  FYVE and coiled-coil domain-containing protein 1  

UniProtKB / Swiss-Prot ID :  FYCO1_HUMAN

Gene Name (Synonyms) : 
FYCO1, ZFYVE7  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasmic vesicle, autophagosome. Endosome. Lysosome. Note=Localizes to the external but not to the internal membrane of autophagosomes, and upon autophagosome/late endosome/lysosome fusion, it stays on the external surface of autolysosomes. 

Protein Function :  May mediate microtubule plus end-directed vesicle transport. 

Protein Sequence MASTNAESQLQRIIRDLQDAVTELSKEFQEAGEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDY...
Predicted Secondary Structure CCCCCHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCCHHHHHHHHHHHHHHHHCHHHHHHHCCCCCCH...
Protein Variant
LocationDescription
250R -> Q (in dbSNP:rs4683158). VAR_027006
282R -> H (in dbSNP:rs9875356). VAR_027007
321G -> A (in dbSNP:rs3733100). VAR_027008
381T -> M (in dbSNP:rs3733101). VAR_027009
447R -> C (in dbSNP:rs33910087). VAR_056882
679A -> V (in dbSNP:rs3796375). VAR_027010
994E -> K (in dbSNP:rs34801630). VAR_056883
1001N -> D (in dbSNP:rs13059238). VAR_027011
1376L -> P (in CATC2). VAR_065974
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MASTNA
---CCCCCH
36.05UniProtKB
Link-
811PhosphoserineDKVQSQLSM
HHHHHHHHH
35.76SysPTM
Link-
814PhosphoserineQSQLSMAEA
HHHHHHHHH
14.33SysPTM
Link-
878PhosphoserineQEELSQAKC
HHHHHHHHH
31.22HPRD
Link-
878PhosphoserineQEELSQAKC
HHHHHHHHH
31.22PhosphoELM
Link-
878PhosphoserineQEELSQAKC
HHHHHHHHH
31.22Phosphositeplus
Link-
878Phosphoserine.QEELSQAKC
HHHHHHHHH
31.22UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
OMIM disease
610019Cataract 18 (CTRCT18)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-878, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures