DPYL4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DPYL4_HUMAN
• UniProt AC: O14531
• Protein Name: Dihydropyrimidinase-related protein 4
• Gene Name: DPYSL4
• Organism: Homo sapiens (Human).
• Sequence Length: 572
• Subcellular Localization: Cytoplasm.
• Protein Description: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity)..
• Protein Sequence: MSFQGKKSIPRITSDRLLIRGGRIVNDDQSFYADVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVLGMTPADDFCQGTKAALAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACCDYSLHVDITRWHESIKEELEALVKEKGVNSFLVFMAYKDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPITASLGTDGSHYWSKNWAKAAAFVTSPPVNPDPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAVGKDNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPAVVISQGRVALEDGKMFVTPGAGRFVPRKTFPDFVYKRIKARNRLAEIHGVPRGLYDGPVHEVMVPAKPGSGAPARASCPGKISVPPVRNLHQSGFSLSGSQADDHIARRTAQKIMAPPGGRSNITSLS

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
8	Phosphorylation	MSFQGKKSIPRITSD CCCCCCCCCCCCCCC	41.11	-
32	Phosphorylation	VNDDQSFYADVHVED ECCCCCEECEEEECC	13.72	-
101	Phosphorylation	KAALAGGTTMILDHV HHHHCCCCEEEECCC	16.57	-
102	Phosphorylation	AALAGGTTMILDHVF HHHCCCCEEEECCCC	12.89	-
210	Ubiquitination	DIVEEEQKRLLELGI CCCHHHHHHHHHHCC	48.57	-
258	Acetylation	YVTKVMSKGAADAIA EEEECCCCCHHHHHH	34.18	7987615
258	Succinylation	YVTKVMSKGAADAIA EEEECCCCCHHHHHH	34.18	-
268	Acetylation	ADAIAQAKRRGVVVF HHHHHHHHHCCEEEE	30.46	155361
268	Ubiquitination	ADAIAQAKRRGVVVF HHHHHHHHHCCEEEE	30.46	2190698
288	Phosphorylation	ASLGTDGSHYWSKNW EECCCCCCCCCCCCH	19.06	25627689
292	Phosphorylation	TDGSHYWSKNWAKAA CCCCCCCCCCHHHHE	14.67	-
293	Acetylation	DGSHYWSKNWAKAAA CCCCCCCCCHHHHEE	42.22	23236377
293	Ubiquitination	DGSHYWSKNWAKAAA CCCCCCCCCHHHHEE	42.22	-
322	Phosphorylation	DHLTCLLSSGDLQVT HHHEEEEECCCEEEC	21.23	22210691
323	Phosphorylation	HLTCLLSSGDLQVTG HHEEEEECCCEEECC	35.97	22210691
345	Ubiquitination	TAQKAVGKDNFALIP CCHHHHCCCCEEECC	42.79	-
431	Phosphorylation	THNLNVEYNIFEGVE CCCCCCEEEEEECCC	14.85	-
480	Acetylation	TFPDFVYKRIKARNR CCCHHHHHHHHHHHH	42.20	24884051
496	Methylation	AEIHGVPRGLYDGPV HHHHCCCCCCCCCCC	45.39	-
499	Phosphorylation	HGVPRGLYDGPVHEV HCCCCCCCCCCCEEE	22.98	-
521	Phosphorylation	SGAPARASCPGKISV CCCCCCCCCCCCCCC	18.45	-
537	Phosphorylation	PVRNLHQSGFSLSGS CCCCCEECCCCCCCC	30.93	22496350
540	Phosphorylation	NLHQSGFSLSGSQAD CCEECCCCCCCCCHH	25.75	24173317
542	Phosphorylation	HQSGFSLSGSQADDH EECCCCCCCCCHHHH	34.89	24117733
544	Phosphorylation	SGFSLSGSQADDHIA CCCCCCCCCHHHHHH	20.86	17525332
565	Asymmetric dimethylarginine	IMAPPGGRSNITSLS HHCCCCCCCCCCCCC	32.23	-
569	Phosphorylation	PGGRSNITSLS---- CCCCCCCCCCC----	28.06	27732954
570	Phosphorylation	GGRSNITSLS----- CCCCCCCCCC-----	23.87	27732954
572	Phosphorylation	RSNITSLS------- CCCCCCCC-------	37.63	23312004

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

Oops, there are no upstream regulatory protein records of DPYL4_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DPYL4_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of DPYL4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SH3G3_HUMAN	SH3GL3	physical	16169070
TBB5_BOVIN	TUBB	physical	12134159
RBPMS_HUMAN	RBPMS	physical	25416956

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-544, AND MASSSPECTROMETRY.
PubMed: 17525332