dbPTM

PAR6A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PAR6A_HUMAN	Jmol._Canvas2D (Jmol) "myJmol"[x]
UniProt AC	Q9NPB6
Protein Name	Partitioning defective 6 homolog alpha
Gene Name	PARD6A
Organism	Homo sapiens (Human).
Sequence Length	346
Subcellular Localization	Cytoplasm. Cell membrane. Cell projection, ruffle. Cell junction, tight junction. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Colocali
Protein Description	Adapter protein involved in asymmetrical cell division and cell polarization processes. Probably involved in the formation of epithelial tight junctions. Association with PARD3 may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. [PubMed: 10873802 Regulates centrosome organization and function. Essential for the centrosomal recruitment of key proteins that control centrosomal microtubule organization]
Protein Sequence	MARPQRTPARSPDSIVEVKSKFDAEFRRFALPRASVSGFQEFSRLLRAVHQIPGLDVLLGYTDAHGDLLPLTNDDSLHRALASGPPPLRLLVQKRAEADSSGLAFASNSLQRRKKGLLLRPVAPLRTRPPLLISLPQDFRQVSSVIDVDLLPETHRRVRLHKHGSDRPLGFYIRDGMSVRVAPQGLERVPGIFISRLVRGGLAESTGLLAVSDEILEVNGIEVAGKTLDQVTDMMVANSHNLIVTVKPANQRNNVVRGASGRLTGPPSAGPGPAEPDSDDDSSDLVIENRQPPSSNGLSQGPPCWDLHPGCRHPGTRSSLPSLDDQEQASSGWGSRIRGDGSGFSL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	PQRTPARSPDSIVEV CCCCCCCCCCCEEEE	34.85	21815630
14	Phosphorylation	TPARSPDSIVEVKSK CCCCCCCCEEEEHHH	31.73	24719451
19	Ubiquitination	PDSIVEVKSKFDAEF CCCEEEEHHHCCHHH	34.13	29967540
37	Phosphorylation	ALPRASVSGFQEFSR CCCCHHCCCHHHHHH	31.25	24972180
61	Phosphorylation	GLDVLLGYTDAHGDL CCCCEEEEECCCCCE	11.04	22210691
62	Phosphorylation	LDVLLGYTDAHGDLL CCCEEEEECCCCCEE	25.55	22210691
100	Phosphorylation	QKRAEADSSGLAFAS HHHHHHCCCCCHHHC	33.10	21712546
101	Phosphorylation	KRAEADSSGLAFASN HHHHHCCCCCHHHCH	38.07	21712546
106 (in isoform 2)	Phosphorylation	-	11.38	22210691
107	Phosphorylation	SSGLAFASNSLQRRK CCCCHHHCHHHHHHH	22.09	25850435
108 (in isoform 2)	Phosphorylation	-	43.22	22210691
109	Phosphorylation	GLAFASNSLQRRKKG CCHHHCHHHHHHHCC	24.31	21815630
143	Phosphorylation	PQDFRQVSSVIDVDL CCCHHHHHCCCCHHC	15.56	22210691
144	Phosphorylation	QDFRQVSSVIDVDLL CCHHHHHCCCCHHCC	25.00	22210691
154	Phosphorylation	DVDLLPETHRRVRLH CHHCCCCCCCCEEEC	20.81	28348404
165	Phosphorylation	VRLHKHGSDRPLGFY EEECCCCCCCCCEEE	30.11	20873877
264	Phosphorylation	RGASGRLTGPPSAGP ECCCCCCCCCCCCCC	46.40	28111955
268	Phosphorylation	GRLTGPPSAGPGPAE CCCCCCCCCCCCCCC	49.33	28111955
277	Phosphorylation	GPGPAEPDSDDDSSD CCCCCCCCCCCCCCC	57.09	33259812
278	Phosphorylation	PGPAEPDSDDDSSDL CCCCCCCCCCCCCCC	54.37	30278072
282	Phosphorylation	EPDSDDDSSDLVIEN CCCCCCCCCCCEECC	32.52	30278072
283	Phosphorylation	PDSDDDSSDLVIENR CCCCCCCCCCEECCC	41.79	30576142
318	Phosphorylation	CRHPGTRSSLPSLDD CCCCCCCCCCCCCCC	35.74	22617229
319	Phosphorylation	RHPGTRSSLPSLDDQ CCCCCCCCCCCCCCH	40.80	28985074
322	Phosphorylation	GTRSSLPSLDDQEQA CCCCCCCCCCCHHHH	50.12	23186163
345	Phosphorylation	RGDGSGFSL------ CCCCCCCCC------	36.37	27134283

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
345	S	Phosphorylation	Kinase	PRKCI	P41743	GPS
345	S	Phosphorylation	Kinase	PKCZ	Q05513	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO31	Q5XUX0	PMID:24658274

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PAR6A_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 PAR6A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ECT2_HUMAN	ECT2	physical	15254234
KPCZ_HUMAN	PRKCZ	physical	15254234
CDC42_HUMAN	CDC42	physical	10934474
RHOQ_HUMAN	RHOQ	physical	10934474
RAC1_HUMAN	RAC1	physical	10873802
CDC42_HUMAN	CDC42	physical	10873802
MPP5_HUMAN	MPP5	physical	12545177
KPCZ_HUMAN	PRKCZ	physical	11260256
RAC1_HUMAN	RAC1	physical	11260256
CDC42_HUMAN	CDC42	physical	11260256
MARK2_HUMAN	MARK2	physical	14676191
MARK4_HUMAN	MARK4	physical	14676191
KPCI_HUMAN	PRKCI	physical	14676191
CDC42_HUMAN	CDC42	physical	14676191
L2GL1_HUMAN	LLGL1	physical	14676191
RPAP3_HUMAN	RPAP3	physical	14676191
PAR6B_HUMAN	PARD6B	physical	14676191
PDRG1_HUMAN	PDRG1	physical	14676191
KPCZ_HUMAN	PRKCZ	physical	14676191
L2GL2_HUMAN	LLGL2	physical	14676191
PIHD1_HUMAN	PIH1D1	physical	14676191
WDR92_HUMAN	WDR92	physical	14676191
SGT1_HUMAN	SUGT1	physical	14676191
PARD3_HUMAN	PARD3	physical	14676191
SMUF1_HUMAN	SMURF1	physical	15761148
KPCI_HUMAN	PRKCI	physical	11257119
PARD3_HUMAN	PARD3	physical	11257119
ZO1_HUMAN	TJP1	physical	11257119
VHL_HUMAN	VHL	physical	17101696
KPCI_HUMAN	PRKCI	physical	12813044
KPCZ_HUMAN	PRKCZ	physical	12813044
MP2K5_HUMAN	MAP2K5	physical	12813044
FBX31_HUMAN	FBXO31	physical	23469015
TBG1_HUMAN	TUBG1	physical	23469015
WDR83_HUMAN	WDR83	physical	23439680
RICTR_HUMAN	RICTOR	physical	20978191
GRB2_HUMAN	GRB2	physical	25814554
P55G_HUMAN	PIK3R3	physical	25814554
TGFR1_HUMAN	TGFBR1	physical	15761148
KPCI_HUMAN	PRKCI	physical	21516116
EPHB4_HUMAN	EPHB4	physical	26496610
DHE3_HUMAN	GLUD1	physical	26496610
L2GL2_HUMAN	LLGL2	physical	26496610
L2GL1_HUMAN	LLGL1	physical	26496610
ORC2_HUMAN	ORC2	physical	26496610
PMS2_HUMAN	PMS2	physical	26496610
KPCI_HUMAN	PRKCI	physical	26496610
SMCA4_HUMAN	SMARCA4	physical	26496610
ASPP2_HUMAN	TP53BP2	physical	26496610
TTC3_HUMAN	TTC3	physical	26496610
PRDX3_HUMAN	PRDX3	physical	26496610
RASF8_HUMAN	RASSF8	physical	26496610
KIF1B_HUMAN	KIF1B	physical	26496610
PI3R4_HUMAN	PIK3R4	physical	26496610
SIR6_HUMAN	SIRT6	physical	26496610
M3K20_HUMAN	ZAK	physical	26496610
NOL8_HUMAN	NOL8	physical	26496610
ELP3_HUMAN	ELP3	physical	26496610
PLXA3_HUMAN	PLXNA3	physical	26496610
ASH1L_HUMAN	ASH1L	physical	26496610
PARD3_HUMAN	PARD3	physical	26496610
ARI5B_HUMAN	ARID5B	physical	26496610
T126A_HUMAN	TMEM126A	physical	26496610
PAR6B_HUMAN	PARD6B	physical	26496610
LRCH3_HUMAN	LRCH3	physical	26496610
DPP9_HUMAN	DPP9	physical	26496610
KPCZ_HUMAN	PRKCZ	physical	27143478

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 PAR6A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-278, AND MASSSPECTROMETRY.	18691976 [Abstract]