RCY1_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RCY1_YEAST
• UniProt AC: P39531
• Protein Name: Recyclin-1
• Gene Name: RCY1
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 840
• Subcellular Localization: Cytoplasm . Bud neck . Cell tip . In unpolarized G1 cells this protein is found in patches in the cytoplasm, while after bud emergence it is concentrated in nascent buds and at the mother-bud neck. Accumulates at the shmoo tips of cells treated with
• Protein Description: Involved in recycling plasma membrane proteins internalized by endocytosis. Required for recycling of the v-SNARE SNC1..
• Protein Sequence: MDDLLKVPEIVTNIASYLSTVDYLSFQQVNKRVYAIINGKNDSKYWSLKLTRMGLQQVHSNEEEEITLLDENDNQNSLRIFEIYKSFTAQNSKKIFVKFYRCYNSYARKLYNNNLANFFPTSYSNDPLKQTRILNFIKKYNFSNKNDIETFTRIETNFNILREIFINSVLKESELNYQSNNLAAVARFMKILLISNEESNAIEFFKSKADLPPSLTVLPSNDELFWAEQPREEDSGGSTVIFNSKNLDTFLNQLRDFLNEKIKLADILFKDEFPVILQFIESFIQDILLDILNNILLSYSEFLKENGKDSKANYECVPELYFTFIKKFDTELNDSVNAGANFRKVVRDLLNLYLEPFVVNYMNQTTRVFESLINSQLANYDTQVQDKQREQNAKIYNTLKDQTDASSASNNELPNDLSIITETSKTVPEADSKPSTIHQSVHSTDISNDKLDFLSSFTKIFKFSNNENQRLKQQLQLAYNLNLISNNLQNIKSLISLDLCYKILQETSEKTDQIYKFHTIESLLPLIKLRCQEIFKILITQLNKNHVKPAFEKAILLLQKYNPNEIEQIEIKFNSLSPANTQVEPLVQFTELINIGDIILQMISIFYKNELIPKKIIDKNKDFLNDVIQLKKNFETSIDDFVAEGLNIGINKLMDEISFVFKTLQLPDDYNPPPPSRNSPIRDIKPTKCAIRVVELLSNHCFLLTGATDKGTIDVYQQEIGERFFNEIVKHLKKCFISTEGAIWLICDLNYFYDFIANKLKQKNVVPYFVGLKSIGQLYIISGKDSKELGKLISDLGKFNGIFTQEEIYEFVQRRSDWVRVRKDVEKVMYGLGIRDCCIM

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
98	Acetylation	NSKKIFVKFYRCYNS CCCEEEEEHHHHHHH	26.40	24489116
138	Acetylation	TRILNFIKKYNFSNK HHHHHHHHHHCCCCC	45.10	24489116
403	Phosphorylation	YNTLKDQTDASSASN HHHHHHHCCCCCCCC	43.60	21440633
406	Phosphorylation	LKDQTDASSASNNEL HHHHCCCCCCCCCCC	29.28	21440633
407	Phosphorylation	KDQTDASSASNNELP HHHCCCCCCCCCCCC	37.12	21082442
409	Phosphorylation	QTDASSASNNELPND HCCCCCCCCCCCCCC	41.98	21440633
507	Phosphorylation	CYKILQETSEKTDQI HHHHHHHHHHCCCCE	29.26	21551504
508	Phosphorylation	YKILQETSEKTDQIY HHHHHHHHHCCCCEE	36.02	21551504
515	Phosphorylation	SEKTDQIYKFHTIES HHCCCCEEEHHHHHH	11.28	21440633
631	Acetylation	LNDVIQLKKNFETSI HHHHHHHHHHHCCCH	29.33	22865919

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RCY1_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RCY1_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RCY1_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SKP1_YEAST	SKP1	physical	11287615
YPT32_YEAST	YPT32	physical	15537705
YPT31_YEAST	YPT31	physical	15537705
SNC1_YEAST	SNC1	physical	15537705
GYP2_YEAST	MDR1	genetic	12807768
CDC50_YEAST	CDC50	physical	17093059
ATC3_YEAST	DRS2	physical	17093059
ATC5_YEAST	DNF1	physical	17093059
ATC4_YEAST	DNF2	physical	17093059
SRS2_YEAST	SRS2	genetic	21459050
SNC1_YEAST	SNC1	physical	21686101
SKP1_YEAST	SKP1	physical	21686101
RCY1_YEAST	RCY1	physical	14747994
ATC3_YEAST	DRS2	physical	24272750
CENPA_YEAST	CSE4	physical	26975376
PSH1_YEAST	PSH1	genetic	26975376
YMP0_YEAST	YMR010W	genetic	28057802
KES1_YEAST	KES1	genetic	28057802

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND MASSSPECTROMETRY.
PubMed: 18407956

"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND MASSSPECTROMETRY.
PubMed: 17563356