RUFY1_HUMAN - dbPTM
RUFY1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RUFY1_HUMAN
UniProt AC Q96T51
Protein Name RUN and FYVE domain-containing protein 1
Gene Name RUFY1
Organism Homo sapiens (Human).
Sequence Length 708
Subcellular Localization Cytoplasm. Early endosome membrane
Peripheral membrane protein.
Protein Description Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in early endosomal trafficking..
Protein Sequence MADREGGCAAGRGRELEPELEPGPGPGSALEPGEEFEIVDRSQLPGPGDLRSATRPRAAEGWSAPILTLARRATGNLSASCGSALRAAAGLGGGDSGDGTARAASKCQMMEERANLMHMMKLSIKVLLQSALSLGRSLDADHAPLQQFFVVMEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKHLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANLCLKGEDLDSQVGVIDFSLYLKDVQDLDGGKEHERITDVLDQKNYVEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQEEQQQLREQNELIRERSEKSVEITKQDTKVELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKAQNAESSLQQKNEAITSFEGKTNQVMSSMKQMEERLQHSERARQGAEERSHKLQQELGGRIGALQLQLSQLHEQCSSLEKELKSEKEQRQALQRELQHEKDTSSLLRMELQQVEGLKKELRELQDEKAELQKICEEQEQALQEMGLHLSQSKLKMEDIKEVNQALKGHAWLKDDEATHCRQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCSSTAS
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
12MethylationEGGCAAGRGRELEPE
CCCCCCCCCCCCCCC		35.9580700713
14MethylationGCAAGRGRELEPELE
CCCCCCCCCCCCCCC		43.929857955
42PhosphorylationEFEIVDRSQLPGPGD
CEEEECHHHCCCCCC		31.4424300666
52PhosphorylationPGPGDLRSATRPRAA
CCCCCCCCCCCCCCC		41.0922210691
54PhosphorylationPGDLRSATRPRAAEG
CCCCCCCCCCCCCCC		42.3122210691
63PhosphorylationPRAAEGWSAPILTLA
CCCCCCCCCCHHHHH		34.7228857561
63 (in isoform 2)Ubiquitination-34.7221906983
68PhosphorylationGWSAPILTLARRATG
CCCCCHHHHHHHHHC		21.0624719451
74PhosphorylationLTLARRATGNLSASC
HHHHHHHHCCCCHHH		25.4523401153
78PhosphorylationRRATGNLSASCGSAL
HHHHCCCCHHHHHHH		23.3329978859
80PhosphorylationATGNLSASCGSALRA
HHCCCCHHHHHHHHH		18.6829978859
83PhosphorylationNLSASCGSALRAAAG
CCCHHHHHHHHHHCC		28.5823684312
96PhosphorylationAGLGGGDSGDGTARA
CCCCCCCCCCCHHHH		41.9021815630
100PhosphorylationGGDSGDGTARAASKC
CCCCCCCHHHHHHHH		20.0828857561
123PhosphorylationLMHMMKLSIKVLLQS
HHHHHHHHHHHHHHH		18.16-
164UbiquitinationKHGLKVKKSFIGQNK
HHCCCCCHHHCCCCC		54.29-
165PhosphorylationHGLKVKKSFIGQNKS
HCCCCCHHHCCCCCC		19.1723401153
171 (in isoform 3)Ubiquitination-40.5321906983
171 (in isoform 1)Ubiquitination-40.5321906983
171UbiquitinationKSFIGQNKSFFGPLE
HHHCCCCCCCCCHHH		40.5321906983
172PhosphorylationSFIGQNKSFFGPLEL
HHCCCCCCCCCHHHH		33.1028857561
182UbiquitinationGPLELVEKLCPEASD
CHHHHHHHHCCCHHH		48.16-
184S-nitrosylationLELVEKLCPEASDIA
HHHHHHHCCCHHHHH		4.192212679
188PhosphorylationEKLCPEASDIATSVR
HHHCCCHHHHHHHHH		28.08-
192PhosphorylationPEASDIATSVRNLPE
CCHHHHHHHHHCCHH		28.2628857561
193PhosphorylationEASDIATSVRNLPEL
CHHHHHHHHHCCHHH		15.2828857561
200 (in isoform 2)Ubiquitination-5.8821906983
225"N6,N6-dimethyllysine"KKLADYLKVLIDNKH
HHHHHHHHHHHCCHH		28.85-
225MethylationKKLADYLKVLIDNKH
HHHHHHHHHHHCCHH		28.8523644510
282 (in isoform 2)Ubiquitination-3.5921906983
308 (in isoform 1)Ubiquitination-50.3321906983
308 (in isoform 3)Ubiquitination-50.3321906983
308UbiquitinationITDVLDQKNYVEELN
HHHHHCCCCHHHHHH		50.3321906983
310PhosphorylationDVLDQKNYVEELNRH
HHHCCCCHHHHHHHH		19.1027174698
319PhosphorylationEELNRHLSCTVGDLQ
HHHHHHCCCCHHHHH		11.1329978859
321PhosphorylationLNRHLSCTVGDLQTK
HHHHCCCCHHHHHHH		24.9329978859
338UbiquitinationGLEKTNSKLQEELSA
HHHHHCHHHHHHHHH		57.15-
344PhosphorylationSKLQEELSAATDRIC
HHHHHHHHHHHHHHH		21.09-
347PhosphorylationQEELSAATDRICSLQ
HHHHHHHHHHHHHHH		26.06-
349MethylationELSAATDRICSLQEE
HHHHHHHHHHHHHHH		27.71115492999
352PhosphorylationAATDRICSLQEEQQQ
HHHHHHHHHHHHHHH		30.62-
355 (in isoform 3)Phosphorylation-64.1721902226
371O-linked_GlycosylationNELIRERSEKSVEIT
HHHHHHHHHHHHEEE		44.6230379171
374PhosphorylationIRERSEKSVEITKQD
HHHHHHHHHEEECCC		22.4128857561
379AcetylationEKSVEITKQDTKVEL
HHHHEEECCCCCCHH		52.4120167786
389PhosphorylationTKVELETYKQTRQGL
CCCHHHHHHHHHHHH		7.5422817900
390 (in isoform 1)Ubiquitination-53.2521906983
390UbiquitinationKVELETYKQTRQGLD
CCHHHHHHHHHHHHH		53.252190698
400PhosphorylationRQGLDEMYSDVWKQL
HHHHHHHHHHHHHHH		10.3228796482
401PhosphorylationQGLDEMYSDVWKQLK
HHHHHHHHHHHHHHH		25.1128796482
445UbiquitinationLEKDTHEKQDTLVAL
HHCCCHHHHHHHHHH		45.96-
460UbiquitinationRQQLEEVKAINLQMF
HHHHHHHHHHCHHHH		46.99-
466SulfoxidationVKAINLQMFHKAQNA
HHHHCHHHHHHHHCH		4.2430846556
469UbiquitinationINLQMFHKAQNAESS
HCHHHHHHHHCHHHH		40.16-
480UbiquitinationAESSLQQKNEAITSF
HHHHHHHHHHHHHHH		43.74-
486PhosphorylationQKNEAITSFEGKTNQ
HHHHHHHHHCHHHHH		18.3925159151
490UbiquitinationAITSFEGKTNQVMSS
HHHHHCHHHHHHHHH		36.78-
491PhosphorylationITSFEGKTNQVMSSM
HHHHCHHHHHHHHHH		41.5629759185
499UbiquitinationNQVMSSMKQMEERLQ
HHHHHHHHHHHHHHH		48.73-
521UbiquitinationGAEERSHKLQQELGG
HHHHHHHHHHHHHHH		49.60-
545PhosphorylationSQLHEQCSSLEKELK
HHHHHHHHHHHHHHH		37.3426437602
546PhosphorylationQLHEQCSSLEKELKS
HHHHHHHHHHHHHHH		48.4526437602
555MethylationEKELKSEKEQRQALQ
HHHHHHHHHHHHHHH		67.2623644510
569UbiquitinationQRELQHEKDTSSLLR
HHHHHHHCCHHHHHH		65.27-
573PhosphorylationQHEKDTSSLLRMELQ
HHHCCHHHHHHHHHH		33.2524719451
618PhosphorylationQEMGLHLSQSKLKME
HHCCHHHCCCCCCHH		22.9717525332
620PhosphorylationMGLHLSQSKLKMEDI
CCHHHCCCCCCHHHH		36.2630278072
621UbiquitinationGLHLSQSKLKMEDIK
CHHHCCCCCCHHHHH		44.48-
635UbiquitinationKEVNQALKGHAWLKD
HHHHHHHCCCCCCCC		52.22-
641UbiquitinationLKGHAWLKDDEATHC
HCCCCCCCCCCCCCH		53.05-
674PhosphorylationCGHIFCNTCSSNELA
CCCEEECCCCCCCCC		18.2328857561
676PhosphorylationHIFCNTCSSNELALP
CEEECCCCCCCCCCC		33.8728857561
677PhosphorylationIFCNTCSSNELALPS
EEECCCCCCCCCCCC		36.1528857561
684PhosphorylationSNELALPSYPKPVRV
CCCCCCCCCCCCEEE		55.7224719451
694PhosphorylationKPVRVCDSCHTLLLQ
CCEEECCCCHHHHHH		11.5928857561
697PhosphorylationRVCDSCHTLLLQRCS
EECCCCHHHHHHHHH		24.3528857561
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
389YPhosphorylationKinaseBMXP51813
PhosphoELM
400YPhosphorylationKinaseBMXP51813
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RUFY1_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 RUFY1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BMX_HUMANBMXphysical
11877430
RAB4A_HUMANRAB4Aphysical
14617813
RAB5A_HUMANRAB5Aphysical
14617813
GRIK4_HUMANGRIK4physical
14617813
RABE1_HUMANRABEP1physical
14617813
TCPQ_HUMANCCT8physical
22939629
VP26A_HUMANVPS26Aphysical
22939629
KLC4_HUMANKLC4physical
22863883
PSME4_HUMANPSME4physical
22863883
SART3_HUMANSART3physical
22863883
TELO2_HUMANTELO2physical
22863883
TTI1_HUMANTTI1physical
22863883
RUFY1_HUMANRUFY1physical
25416956
TXD17_HUMANTXNDC17physical
25416956
RB39B_HUMANRAB39Bphysical
25416956
RAB3I_HUMANRAB3IPphysical
25416956
AP3B2_HUMANAP3B2physical
23144738
DYHC1_HUMANDYNC1H1physical
23144738
TBB5_HUMANTUBBphysical
23144738
TBA1A_HUMANTUBA1Aphysical
23144738
AP3D1_HUMANAP3D1physical
23144738
AP3S1_HUMANAP3S1physical
23144738
AP3M1_HUMANAP3M1physical
23144738
PKN2_HUMANPKN2physical
26496610
SRA1_HUMANSRA1physical
26496610
RUFY2_HUMANRUFY2physical
26496610
NEUL_HUMANNLNphysical
26496610
RUFY3_HUMANRUFY3physical
28514442
C43BP_HUMANCOL4A3BPphysical
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 RUFY1_HUMAN

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Related Literatures of Post-Translational Modification
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-618, AND MASSSPECTROMETRY.
"Interaction between tyrosine kinase Etk and a RUN-domain and FYVE-domain containing protein RUFY1. A possible role of Etk in regulationof vesicle trafficking.";
Yang J., Kim O., Wu J., Qiu Y.;
J. Biol. Chem. 277:30219-30226(2002).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-708 (ISOFORM 1), TISSUE SPECIFICITY,SUBCELLULAR LOCATION, INTERACTION WITH BMX, PHOSPHORYLATION AT TYR-389AND TYR-400, AND MUTAGENESIS OF TYR-389 AND TYR-400.

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