RUFY3_HUMAN - dbPTM
RUFY3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RUFY3_HUMAN
UniProt AC Q7L099
Protein Name Protein RUFY3 {ECO:0000305}
Gene Name RUFY3 {ECO:0000312|HGNC:HGNC:30285}
Organism Homo sapiens (Human).
Sequence Length 469
Subcellular Localization Cytoplasm . Endomembrane system . Cell projection, invadopodium . Perikaryon . Cell projection . Cell projection, growth cone . Cell projection, filopodium . Cell projection, lamellipodium . Colocalizes with PAK1, F-actin, myosins and integrins in in
Protein Description Plays a role in the generation of neuronal polarity formation and axon growth (By similarity). Implicated in the formation of a single axon by developing neurons (By similarity). May inhibit the formation of additional axons by inhibition of PI3K in minor neuronal processes (By similarity). Plays a role in the formation of F-actin-enriched protrusive structures at the cell periphery. [PubMed: 25766321 Plays a role in cytoskeletal organization by regulating the subcellular localization of FSCN1 and DBN1 at axonal growth cones (By similarity Promotes gastric cancer cell migration and invasion in a PAK1-dependent manner]
Protein Sequence MSALTPPTDMPTPTTDKITQAAMETIYLCKFRVSMDGEWLCLRELDDISLTPDPEPTHEDPNYLMANERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFCMKGEDLDSQVGVIDFSMYLKDGNSSKGTEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKLIPKHH
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
2Phosphorylation------MSALTPPTD
------CCCCCCCCC		31.8029514088
4 (in isoform 2)Phosphorylation-6.0725159151
5Phosphorylation---MSALTPPTDMPT
---CCCCCCCCCCCC		27.2622199227
8PhosphorylationMSALTPPTDMPTPTT
CCCCCCCCCCCCCCC		46.2427732954
9 (in isoform 2)Phosphorylation-47.0027251275
12PhosphorylationTPPTDMPTPTTDKIT
CCCCCCCCCCCCHHH		26.9927732954
14 (in isoform 2)Phosphorylation-50.5427251275
16 (in isoform 2)Phosphorylation-42.7227251275
27PhosphorylationQAAMETIYLCKFRVS
HHHHHHHHHCEEEEC		17.29-
34PhosphorylationYLCKFRVSMDGEWLC
HHCEEEECCCCCEEE		13.6024117733
49PhosphorylationLRELDDISLTPDPEP
EEECCCCCCCCCCCC		32.9328857561
50 (in isoform 2)Phosphorylation-9.1127251275
51PhosphorylationELDDISLTPDPEPTH
ECCCCCCCCCCCCCC		20.8928857561
55 (in isoform 2)Phosphorylation-70.9325921289
57PhosphorylationLTPDPEPTHEDPNYL
CCCCCCCCCCCCCCH		35.9127732954
59 (in isoform 2)Phosphorylation-77.0925921289
81UbiquitinationNMAKLSIKGLIESAL
HHHHHHHHHHHHHHH		44.26-
91 (in isoform 2)Phosphorylation-21.3224117733
94 (in isoform 2)Phosphorylation-5.9824117733
97 (in isoform 2)Phosphorylation-43.1924117733
105 (in isoform 2)Phosphorylation-3.3530177828
106 (in isoform 2)Phosphorylation-4.1830177828
120UbiquitinationKHGLKAKKTFLGQNK
HHCHHHCCHHCCCCC		49.74-
128AcetylationTFLGQNKSFWGPLEL
HHCCCCCCCCCHHHH		33.5119608861
151UbiquitinationAEITASVKDLPGLKT
HHHHEECCCCCCCCC		51.56-
157 (in isoform 3)Ubiquitination-57.61-
157UbiquitinationVKDLPGLKTPVGRGR
CCCCCCCCCCCCHHH		57.61-
181AcetylationKKLSEYMKALINKKE
HHHHHHHHHHHCHHH		38.8619608861
241AcetylationGVIDFSMYLKDGNSS
CEEEEEEEEECCCCC		14.9219608861
264UbiquitinationITAILDQKNYVEELN
EEEEECCCCHHHHHH		50.33-
266PhosphorylationAILDQKNYVEELNRH
EEECCCCHHHHHHHH		19.1027174698
320PhosphorylationMERVKEESSYILESN
HHHHHHHHHHHHHCC		29.5428555341
322PhosphorylationRVKEESSYILESNRK
HHHHHHHHHHHCCCC		20.85-
350UbiquitinationSEARKHLKEETQLRL
HHHHHHHHHHHHHHH		53.90-
393PhosphorylationEKQDALVSLRQQLDD
HHHHHHHHHHHHHHH		20.7724719451
403 (in isoform 4)Phosphorylation-28.4127251275
405AcetylationLDDLRALKHELAFKL
HHHHHHHHHHHHHHH		33.7625953088
420UbiquitinationQSSDLGVKQKSELNS
HHCCCCCHHHHHHHH		50.65-
420AcetylationQSSDLGVKQKSELNS
HHCCCCCHHHHHHHH		50.6525953088
420 (in isoform 3)Ubiquitination-50.65-
432UbiquitinationLNSRLEEKTNQMAAT
HHHHHHHHHHHHHHH		43.32-
439PhosphorylationKTNQMAATIKQLEQS
HHHHHHHHHHHHHHH		21.1122210691
452AcetylationQSEKDLVKQAKTLNS
HHHHHHHHHHHHHHH		52.4125953088
453 (in isoform 4)Phosphorylation-40.3817081983
456 (in isoform 3)Phosphorylation-33.9027251275
459 (in isoform 4)Phosphorylation-31.6928348404
506 (in isoform 3)Phosphorylation-17081983
512 (in isoform 3)Phosphorylation-28348404
517 (in isoform 4)Phosphorylation-27251275
527 (in isoform 4)Phosphorylation-27251275
529 (in isoform 4)Phosphorylation-27251275
564 (in isoform 4)Phosphorylation-29514088
565 (in isoform 4)Phosphorylation-29514088
570 (in isoform 3)Phosphorylation-27251275
580 (in isoform 3)Phosphorylation-27251275
582 (in isoform 3)Phosphorylation-27251275
617 (in isoform 3)Phosphorylation-29514088
618 (in isoform 3)Phosphorylation-29514088
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 RUFY3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RUFY3_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 RUFY3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
U119A_HUMANUNC119physical
16169070
A4_HUMANAPPphysical
21832049
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 RUFY3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-181, AND MASS SPECTROMETRY.

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