RAX2_SCHPO - dbPTM
RAX2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAX2_SCHPO
UniProt AC O14239
Protein Name Polarized growth protein rax2
Gene Name rax2
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1155
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Localizes at the cell cortex of the 'old' growing cell tips.
Protein Description Controls cell polarity, through the G1 phase of mitosis, via regulation of for3 localization. Required for actin cable formation where it directs the spatial distribution of the actin cables..
Protein Sequence MAIYSSFWIRLYFTFRFFCYFLTSVVASDVSFLGDFSGFNVLSNSSANTDLSSQFFEQTNNGSLSSLIDTSYSNSQICYSSWQGDLYVIVLDSEQQTVLLQSNFTSNPTSLEIFSSQNTSFFGNISAIFCDDKFPYAYATFTFSDKPSFTSIYRWNVTNSNVTIEHFYNVKGNVDSLFFLNNDSVAISGNFTEISPFSSSNGPQIAKLAFRSNNSFSQNSLNRNLSSVSCDLTDSYSLWDPSSSGLVSIYAWAPYLIDFNRIRFYNYESSENSVAFFSAINPADGTVLPLTHYDLETGLSSTCDVNCSLQNFANYQDFYFSKGYNSYQIEIQMFGNGEATENSAFGLSSLQFFETNQNSYFDDSYNQESCGFPGLNSLSSYEGNFEASFSNASMPYWIQTIAGEQASVSFFPNITVPTNGTVQLLIPGCTYDNTCSQRGSVIANVYFAKNKQPATKLVQQASDFDQYVSLYSGYLQGFSDNFRPYVELLPYKNSRMVTHSIRFLEQSYTNVSNGLVFVNTTTDVNKLPSIIEFPAASKLRGTAISQIKSLSNGNFSLYMTGNFSDNYGNNVVYMDSLNHLHSFPNNGLNGWVSYIYVSGDSSYFGGNFTHTGDGSIKLNYIAMYSETSRNWSSLGLGTNGPVTHIGSTSLFIDGKIESFISFQGDFNEVYTSEGYAISTSGFSLWNPSSKSWVSMEKLGFYMSGYLFDIPGFNSTQRIYSGNLSAIASYSTRNIAHFSSDSLNDTFIPCYVNAFPSYIRLEDIAYPFANNSMIAILGSEEMEDKCTAAVYFANSTEPIYPKRILSANCSSKFIVLEDCLIIYSNDTDESDIVKNTFVSFNTTSNSLGNTTALSQLKGHINSVIVDDSYNNIFFGGNLSEQSSGCVGFCIFEYNSSSWRNISHNLISAEVQSILWVNETYSSMYLAGKFVWDTSDVDYLLMYNFDNNTIMSCKGSSSIPGPVLLASLKSQSKDEYSVLLYGTEVSSSDTYLNVLNSEGAINSYSLDIHLNQSTINSIDFFESNQISQIPINDSIIVLSGLIVLDDSSKASAVYCVNKSCLPLLTAFKDNGEAGIVRKVVQQKSFSSSASKMIPVTTKYDHIGQPRYVVIISLGISIGVMFLIMSGSIVVEIIHWFFSEHVETLHDYSNFLKELKTQ
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
44N-linked_GlycosylationSGFNVLSNSSANTDL
CCCEECCCCCCCCCH
35.50-
61N-linked_GlycosylationQFFEQTNNGSLSSLI
HHHHHCCCCCHHHHE
44.83-
103N-linked_GlycosylationQTVLLQSNFTSNPTS
CEEEEECCCCCCCCC
31.11-
118N-linked_GlycosylationLEIFSSQNTSFFGNI
EEEEECCCCCCCCCE
39.37-
124N-linked_GlycosylationQNTSFFGNISAIFCD
CCCCCCCCEEEEECC
21.64-
156N-linked_GlycosylationFTSIYRWNVTNSNVT
CEEEEEEEECCCCEE
23.03-
161N-linked_GlycosylationRWNVTNSNVTIEHFY
EEEECCCCEEEEEEE
36.70-
182N-linked_GlycosylationDSLFFLNNDSVAISG
CEEEEECCCEEEEEC
45.11-
190N-linked_GlycosylationDSVAISGNFTEISPF
CEEEEECCCEEEECC
33.60-
213N-linked_GlycosylationAKLAFRSNNSFSQNS
HHHHHHCCCCCCCCC
43.86-
224N-linked_GlycosylationSQNSLNRNLSSVSCD
CCCCCCCCCCEEECC
43.11-
306N-linked_GlycosylationLSSTCDVNCSLQNFA
CCCCCCCCCEECCCC
9.08-
391N-linked_GlycosylationNFEASFSNASMPYWI
CCEECCCCCCCCEEE
33.74-
413N-linked_GlycosylationASVSFFPNITVPTNG
CEEEECCCEECCCCC
37.09-
419N-linked_GlycosylationPNITVPTNGTVQLLI
CCEECCCCCEEEEEC
37.76-
510N-linked_GlycosylationFLEQSYTNVSNGLVF
HHHHCEEECCCCEEE
27.30-
519N-linked_GlycosylationSNGLVFVNTTTDVNK
CCCEEEEECCCCHHH
21.90-
554N-linked_GlycosylationIKSLSNGNFSLYMTG
EEECCCCCEEEEEEC
27.81-
562N-linked_GlycosylationFSLYMTGNFSDNYGN
EEEEEECCCCCCCCC
24.88-
607N-linked_GlycosylationDSSYFGGNFTHTGDG
CCCEECCCCEECCCC
38.74-
630N-linked_GlycosylationMYSETSRNWSSLGLG
EEECCCCCHHHCCCC
42.63-
713N-linked_GlycosylationLFDIPGFNSTQRIYS
EEECCCCCCCCEEEC
50.49-
722N-linked_GlycosylationTQRIYSGNLSAIASY
CCEEECCCHHHEEEE
25.53-
743N-linked_GlycosylationHFSSDSLNDTFIPCY
CCCCCCCCCCCEEEE
50.67-
769N-linked_GlycosylationDIAYPFANNSMIAIL
HCCCCCCCCCEEEEE
41.30-
793N-linked_GlycosylationTAAVYFANSTEPIYP
CEEEEECCCCCCCCC
39.30-
807N-linked_GlycosylationPKRILSANCSSKFIV
CHHHEECCCCCCEEE
23.87-
824N-linked_GlycosylationDCLIIYSNDTDESDI
CEEEEEECCCCHHHH
38.95-
840N-linked_GlycosylationKNTFVSFNTTSNSLG
HCEEEEEECCCCCCC
34.63-
848N-linked_GlycosylationTTSNSLGNTTALSQL
CCCCCCCCHHHHHHH
39.28-
876N-linked_GlycosylationNNIFFGGNLSEQSSG
CCEEECCCCCCCCCC
40.55-
893N-linked_GlycosylationGFCIFEYNSSSWRNI
EEEEEEECCCCCCCC
28.37-
899N-linked_GlycosylationYNSSSWRNISHNLIS
ECCCCCCCCCHHHHH
33.58-
916N-linked_GlycosylationVQSILWVNETYSSMY
HHHHHEECCCCCCCC
25.06-
945N-linked_GlycosylationLLMYNFDNNTIMSCK
EEEEECCCCEEEECC
43.33-
1009N-linked_GlycosylationYSLDIHLNQSTINSI
EEEEEEECCCCCCEE
21.42-
1030N-linked_GlycosylationQISQIPINDSIIVLS
CCCCCCCCCEEEEEE
31.46-
1055N-linked_GlycosylationASAVYCVNKSCLPLL
CCEEEEECHHHHHHH
27.28-

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 RAX2_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAX2_SCHPO !!

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 RAX2_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RAX2_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAX2_SCHPO

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Related Literatures of Post-Translational Modification

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