RASF5_HUMAN - dbPTM
RASF5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RASF5_HUMAN
UniProt AC Q8WWW0
Protein Name Ras association domain-containing protein 5
Gene Name RASSF5
Organism Homo sapiens (Human).
Sequence Length 418
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Isoform 2 is mainly located in the perinuclear region of unstimulated primary T-cells. Upon stimulation translocates to the leading edge and colocalizes with ITGAL/LFA-1 in the peripheral zone of the immunological
Protein Description Potential tumor suppressor. Seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. Isoform 2 stimulates lymphocyte polarization and the patch-like distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to ICAM1. Together with RAP1A may participate in regulation of microtubule growth. The association of isoform 2 with activated RAP1A is required for directional movement of endothelial cells during wound healing. May be involved in regulation of Ras apoptotic function. The RASSF5-STK4/MST1 complex may mediate HRAS and KRAS induced apoptosis..
Protein Sequence MAMASPAIGQRPYPLLLDPEPPRYLQSLSGPELPPPPPDRSSRLCVPAPLSTAPGAREGRSARRAARGNLEPPPRASRPARPLRPGLQQRLRRRPGAPRPRDVRSIFEQPQDPRVPAERGEGHCFAELVLPGGPGWCDLCGREVLRQALRCTNCKFTCHPECRSLIQLDCSQQEGLSRDRPSPESTLTVTFSQNVCKPVEETQRPPTLQEIKQKIDSYNTREKNCLGMKLSEDGTYTGFIKVHLKLRRPVTVPAGIRPQSIYDAIKEVNLAATTDKRTSFYLPLDAIKQLHISSTTTVSEVIQGLLKKFMVVDNPQKFALFKRIHKDGQVLFQKLSIADRPLYLRLLAGPDTEVLSFVLKENETGEVEWDAFSIPELQNFLTILEKEEQDKIQQVQKKYDKFRQKLEEALRESQGKPG
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
2 (in isoform 2)Phosphorylation-11.4030108239
2 (in isoform 2)Acetylation-11.4019369195
5 (in isoform 2)Phosphorylation-11.2030108239
5Phosphorylation---MAMASPAIGQRP
---CCCCCCCCCCCC		11.2025921289
6 (in isoform 2)Phosphorylation-20.5430108239
8 (in isoform 2)Phosphorylation-5.6930108239
9 (in isoform 2)Phosphorylation-21.3930108239
11 (in isoform 2)Phosphorylation-27.7530108239
13 (in isoform 2)Phosphorylation-14.5430108239
13PhosphorylationPAIGQRPYPLLLDPE
CCCCCCCCCCCCCCC		14.5419369195
41PhosphorylationPPPPPDRSSRLCVPA
CCCCCCCCCCEEEEC		27.4728787133
42PhosphorylationPPPPDRSSRLCVPAP
CCCCCCCCCEEEECC		30.1128787133
182PhosphorylationGLSRDRPSPESTLTV
CCCCCCCCCCCCEEE		42.0430576142
185PhosphorylationRDRPSPESTLTVTFS
CCCCCCCCCEEEEEE		31.9130576142
186PhosphorylationDRPSPESTLTVTFSQ
CCCCCCCCEEEEEEC		25.4530576142
188PhosphorylationPSPESTLTVTFSQNV
CCCCCCEEEEEECCE		20.0022210691
190PhosphorylationPESTLTVTFSQNVCK
CCCCEEEEEECCEEC		16.6029083192
192PhosphorylationSTLTVTFSQNVCKPV
CCEEEEEECCEECCC		16.1029083192
212UbiquitinationPPTLQEIKQKIDSYN
CCCHHHHHHHHHHCC		44.80-
214UbiquitinationTLQEIKQKIDSYNTR
CHHHHHHHHHHCCCC		43.40-
218PhosphorylationIKQKIDSYNTREKNC
HHHHHHHCCCCCCCE		19.46-
235PhosphorylationMKLSEDGTYTGFIKV
EEECCCCCEEEEEEE		30.17-
236PhosphorylationKLSEDGTYTGFIKVH
EECCCCCEEEEEEEE		15.47-
251PhosphorylationLKLRRPVTVPAGIRP
EEECCCCCCCCCCCC		24.3726552605
260PhosphorylationPAGIRPQSIYDAIKE
CCCCCCHHHHHHHHH		26.2928796482
262PhosphorylationGIRPQSIYDAIKEVN
CCCCHHHHHHHHHCC		12.4528796482
266UbiquitinationQSIYDAIKEVNLAAT
HHHHHHHHHCCEEEC		58.28-
273PhosphorylationKEVNLAATTDKRTSF
HHCCEEECCCCCCEE		29.8930576142
276UbiquitinationNLAATTDKRTSFYLP
CEEECCCCCCEEEEE		56.32-
278PhosphorylationAATTDKRTSFYLPLD
EECCCCCCEEEEEHH		29.0028450419
279PhosphorylationATTDKRTSFYLPLDA
ECCCCCCEEEEEHHH		18.8728450419
281PhosphorylationTDKRTSFYLPLDAIK
CCCCCEEEEEHHHHH		13.7428796482
308AcetylationVIQGLLKKFMVVDNP
HHHHHHHHHCCCCCH		38.3725953088
326UbiquitinationALFKRIHKDGQVLFQ
EEEEEECCCCCEEEE		62.27-
336PhosphorylationQVLFQKLSIADRPLY
CEEEEECCCCCCCCH		23.8324719451
343PhosphorylationSIADRPLYLRLLAGP
CCCCCCCHHHHHHCC		7.7728152594
352PhosphorylationRLLAGPDTEVLSFVL
HHHHCCCCCCEEEEE		31.0021082442
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
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:23538446
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RASF5_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 RASF5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RASM_HUMANMRASphysical
11857081
RASF1_HUMANRASSF1physical
11857081
RASF2_HUMANRASSF2physical
11857081
RASK_HUMANKRASphysical
11857081
RAP2A_HUMANRAP2Aphysical
11857081
RRAS_HUMANRRASphysical
11857081
RASF5_HUMANRASSF5physical
11857081
MAP1S_HUMANMAP1Sphysical
20562859
STK4_HUMANSTK4physical
20562859
MAP1B_HUMANMAP1Bphysical
20562859
STK3_HUMANSTK3physical
20562859
FLNC_HUMANFLNCphysical
20562859
ERP44_HUMANERP44physical
20562859
GDE_HUMANAGLphysical
20562859
KCD12_HUMANKCTD12physical
20562859
HIPK1_HUMANHIPK1physical
22173032
MDM2_HUMANMDM2physical
22173032
APBP2_HUMANAPPBP2physical
19060904
ITCH_HUMANITCHphysical
23538446
STK3_HUMANSTK3physical
21988832
FBW1A_HUMANBTRCphysical
25217643
KRA42_HUMANKRTAP4-2physical
25416956
K1C40_HUMANKRT40physical
25416956
MAP1B_HUMANMAP1Bphysical
24366813
MAP1S_HUMANMAP1Sphysical
24366813
STK4_HUMANSTK4physical
24366813
STK3_HUMANSTK3physical
24366813
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 RASF5_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273 AND THR-352,PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 (ISOFORM 2), 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 THR-352, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory