dbPTM

OCLN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	OCLN_HUMAN
UniProt AC	Q16625
Protein Name	Occludin
Gene Name	OCLN
Organism	Homo sapiens (Human).
Sequence Length	522
Subcellular Localization	Cell membrane Multi-pass membrane protein . Cell junction, tight junction .
Protein Description	May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. It is able to induce adhesion when expressed in cells lacking tight junctions..
Protein Sequence	MSSRPLESPPPYRPDEFKPNHYAPSNDIYGGEMHVRPMLSQPAYSFYPEDEILHFYKWTSPPGVIRILSMLIIVMCIAIFACVASTLAWDRGYGTSLLGGSVGYPYGGSGFGSYGSGYGYGYGYGYGYGGYTDPRAAKGFMLAMAAFCFIAALVIFVTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPTAQSSGSLYGSQIYALCNQFYTPAATGLYVDQYLYHYCVVDPQEAIAIVLGFMIIVAFALIIFFAVKTRRKMDRYDKSNILWDKEHIYDEQPPNVEEWVKNVSAGTQDVPSPPSDYVERVDSPMAYSSNGKVNDKRFYPESSYKSTPVPEVVQELPLTSPVDDFRQPRYSSGGNFETPSKRAPAKGRAGRSKRTEQDHYETDYTTGGESCDELEEDWIREYPPITSDQQRQLYKRNFDTGLQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYNRLKQVKGSADYKSKKNHCKQLKSKLSHIKKMVGDYDRQKT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSRPLESP ------CCCCCCCCC	34.75	24173317
3	Phosphorylation	-----MSSRPLESPP -----CCCCCCCCCC	36.30	24173317
8	Phosphorylation	MSSRPLESPPPYRPD CCCCCCCCCCCCCCC	50.84	25849741
18	Ubiquitination	PYRPDEFKPNHYAPS CCCCCCCCCCCCCCC	42.75	-
25	Phosphorylation	KPNHYAPSNDIYGGE CCCCCCCCCCCCCCC	38.67	25849741
29	Phosphorylation	YAPSNDIYGGEMHVR CCCCCCCCCCCCCCC	23.18	26657352
40	Phosphorylation	MHVRPMLSQPAYSFY CCCCCCCCCCCCCCC	28.06	25849741
44	Phosphorylation	PMLSQPAYSFYPEDE CCCCCCCCCCCCHHH	13.14	27259358
45	Phosphorylation	MLSQPAYSFYPEDEI CCCCCCCCCCCHHHH	22.02	27499020
158	Phosphorylation	AALVIFVTSVIRSEM HHHHHHHHHHHHHHH	13.41	25072903
159	Phosphorylation	ALVIFVTSVIRSEMS HHHHHHHHHHHHHHH	15.39	25072903
163	Phosphorylation	FVTSVIRSEMSRTRR HHHHHHHHHHHHHHH	26.91	25072903
166	Phosphorylation	SVIRSEMSRTRRYYL HHHHHHHHHHHHHHH	26.84	25072903
248 (in isoform 2)	Phosphorylation	-	2.94	24275569
274	Phosphorylation	TRRKMDRYDKSNILW HHHCCCCCCCCCCCC	24.37	23312004
276	Ubiquitination	RKMDRYDKSNILWDK HCCCCCCCCCCCCCH	36.15	21890473
277	Phosphorylation	KMDRYDKSNILWDKE CCCCCCCCCCCCCHH	26.63	27259358
283	Ubiquitination	KSNILWDKEHIYDEQ CCCCCCCHHHCCCCC	39.34	21906983
287	Phosphorylation	LWDKEHIYDEQPPNV CCCHHHCCCCCCCCH	18.48	21082442
299	Ubiquitination	PNVEEWVKNVSAGTQ CCHHHHHHHHCCCCC	53.34	21906983
302	Phosphorylation	EEWVKNVSAGTQDVP HHHHHHHCCCCCCCC	30.30	22617229
305	Phosphorylation	VKNVSAGTQDVPSPP HHHHCCCCCCCCCCC	22.70	17525332
310	Phosphorylation	AGTQDVPSPPSDYVE CCCCCCCCCCHHHHH	49.65	30631047
313	Phosphorylation	QDVPSPPSDYVERVD CCCCCCCHHHHHCCC	44.98	22617229
315	Phosphorylation	VPSPPSDYVERVDSP CCCCCHHHHHCCCCC	14.46	20007894
321	Phosphorylation	DYVERVDSPMAYSSN HHHHCCCCCCCCCCC	17.45	22617229
325	Phosphorylation	RVDSPMAYSSNGKVN CCCCCCCCCCCCCCC	13.33	30174305
326	Phosphorylation	VDSPMAYSSNGKVND CCCCCCCCCCCCCCC	14.05	25849741
327	Phosphorylation	DSPMAYSSNGKVNDK CCCCCCCCCCCCCCC	36.60	26356563
330	Ubiquitination	MAYSSNGKVNDKRFY CCCCCCCCCCCCCCC	41.96	21906983
337	Phosphorylation	KVNDKRFYPESSYKS CCCCCCCCCHHHCCC	15.32	26657352
340	Phosphorylation	DKRFYPESSYKSTPV CCCCCCHHHCCCCCC	34.17	26657352
341	Phosphorylation	KRFYPESSYKSTPVP CCCCCHHHCCCCCCC	34.61	26657352
342	Phosphorylation	RFYPESSYKSTPVPE CCCCHHHCCCCCCCH	20.45	26657352
343	Ubiquitination	FYPESSYKSTPVPEV CCCHHHCCCCCCCHH	50.21	21906983
344	Phosphorylation	YPESSYKSTPVPEVV CCHHHCCCCCCCHHH	29.70	26657352
345	Phosphorylation	PESSYKSTPVPEVVQ CHHHCCCCCCCHHHH	24.93	26657352
357	Phosphorylation	VVQELPLTSPVDDFR HHHHCCCCCCCCCCC	29.10	30278072
358	Phosphorylation	VQELPLTSPVDDFRQ HHHCCCCCCCCCCCC	30.52	28355574
368	Phosphorylation	DDFRQPRYSSGGNFE CCCCCCCCCCCCCCC	17.55	18707149
369	Phosphorylation	DFRQPRYSSGGNFET CCCCCCCCCCCCCCC	24.64	28355574
370	Phosphorylation	FRQPRYSSGGNFETP CCCCCCCCCCCCCCC	41.61	22617229
376	Phosphorylation	SSGGNFETPSKRAPA CCCCCCCCCCCCCCC	28.82	22617229
378	Phosphorylation	GGNFETPSKRAPAKG CCCCCCCCCCCCCCC	42.04	22496350
379	Ubiquitination	GNFETPSKRAPAKGR CCCCCCCCCCCCCCC	54.50	-
393	Phosphorylation	RAGRSKRTEQDHYET CCCCCCCCCCCCCCC	41.56	22817900
398	Phosphorylation	KRTEQDHYETDYTTG CCCCCCCCCCCCCCC	28.90	19017651
400	Phosphorylation	TEQDHYETDYTTGGE CCCCCCCCCCCCCCC	27.43	27422710
402	Phosphorylation	QDHYETDYTTGGESC CCCCCCCCCCCCCCH	17.39	19017651
403	Phosphorylation	DHYETDYTTGGESCD CCCCCCCCCCCCCHH	23.06	24043423
404	Phosphorylation	HYETDYTTGGESCDE CCCCCCCCCCCCHHH	36.64	22617229
408	Phosphorylation	DYTTGGESCDELEED CCCCCCCCHHHHCHH	30.09	22617229
420	Phosphorylation	EEDWIREYPPITSDQ CHHHHHHCCCCCHHH	12.40	24732914
424	Phosphorylation	IREYPPITSDQQRQL HHHCCCCCHHHHHHH	31.83	24732914
438	Phosphorylation	LYKRNFDTGLQEYKS HHHHCCCHHHHHHHH	35.34	21545357
443	Phosphorylation	FDTGLQEYKSLQSEL CCHHHHHHHHHHHHH	7.91	27259358
445	Phosphorylation	TGLQEYKSLQSELDE HHHHHHHHHHHHHHH	30.64	25849741
448	Phosphorylation	QEYKSLQSELDEINK HHHHHHHHHHHHHHH	45.48	30266825
458	Phosphorylation	DEINKELSRLDKELD HHHHHHHHHHHHHHH	31.71	29496963
467	Phosphorylation	LDKELDDYREESEEY HHHHHHHHHHHHHHH	21.42	22817900
471	Phosphorylation	LDDYREESEEYMAAA HHHHHHHHHHHHHHH	30.86	27642862
474	Phosphorylation	YREESEEYMAAADEY HHHHHHHHHHHHHHH	6.49	20152177
481	Phosphorylation	YMAAADEYNRLKQVK HHHHHHHHHHHHHHC	13.21	27259358
488	Ubiquitination	YNRLKQVKGSADYKS HHHHHHHCCCCCHHH	44.66	-
490	Phosphorylation	RLKQVKGSADYKSKK HHHHHCCCCCHHHHH	16.55	19017651

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
340	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
340	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
398	Y	Phosphorylation	Kinase	SRC	P12931	PSP
400	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
402	Y	Phosphorylation	Kinase	SRC	P12931	PSP
403	T	Phosphorylation	Kinase	PRKCZ	Q05513	GPS
403	T	Phosphorylation	Kinase	PRKCH	P24723	Uniprot
403	T	Phosphorylation	Kinase	PRKCE	Q02156	GPS
404	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
404	T	Phosphorylation	Kinase	PRKCE	Q02156	GPS
404	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
404	T	Phosphorylation	Kinase	PRKCH	P24723	Uniprot
404	T	Phosphorylation	Kinase	PRKCZ	Q05513	GPS
404	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
408	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
408	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
408	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
424	T	Phosphorylation	Kinase	PRKCZ	Q05513	GPS
438	T	Phosphorylation	Kinase	PRKCZ	Q05513	GPS
471	S	Phosphorylation	Kinase	PLK3	Q9H4B4	PSP
471	S	Phosphorylation	Kinase	GRK6	P43250	PSP
471	S	Phosphorylation	Kinase	GRK7	Q8WTQ7	PSP
471	S	Phosphorylation	Kinase	CAMK2B	Q13554	PSP
471	S	Phosphorylation	Kinase	CAMK2D	Q13557	PSP
471	S	Phosphorylation	Kinase	CAMK2G	Q13555	PSP
490	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:15605377
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4L	Q96PU5	PMID:20504882

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
490	S	Phosphorylation		19125584
Phosphorylation at Ser-490 also attenuates the interaction with TJP1.

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 OCLN_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZO2_HUMAN	TJP2	physical	14512431
ZO1_MOUSE	Tjp1	physical	7798316
YES_HUMAN	YES1	physical	11950934
ZO2_HUMAN	TJP2	physical	10575001
ZO1_HUMAN	TJP1	physical	9792688
CXB1_HUMAN	GJB1	physical	10581193
ZO1_HUMAN	TJP1	physical	12169098
ITCH_HUMAN	ITCH	physical	19478092
EPN1_HUMAN	EPN1	physical	19478092
EPS15_HUMAN	EPS15	physical	19478092
HGS_HUMAN	HGS	physical	19478092
NED4L_HUMAN	NEDD4L	physical	20504882
TGFR1_HUMAN	TGFBR1	physical	15761153
TGFR2_HUMAN	TGFBR2	physical	15761153
CLC7A_HUMAN	CLEC7A	physical	25416956
SYNE4_HUMAN	SYNE4	physical	25416956
SNW1_HUMAN	SNW1	physical	16616143
KC1E_HUMAN	CSNK1E	physical	16616143
ULK1_HUMAN	ULK1	physical	16616143
KC1A_HUMAN	CSNK1A1	physical	16616143
FATE1_HUMAN	FATE1	physical	21516116
KC1E_HUMAN	CSNK1E	physical	25241761
ZO1_HUMAN	TJP1	physical	26090670
FBLN1_HUMAN	FBLN1	physical	28514442
MFAP4_HUMAN	MFAP4	physical	28514442
CTGE5_HUMAN	CTAGE5	physical	28514442
CO4A_HUMAN	C4A	physical	28514442
KC1E_HUMAN	CSNK1E	physical	28514442
NEDD4_HUMAN	NEDD4	physical	28514442
CIA30_HUMAN	NDUFAF1	physical	28514442
ANTR1_HUMAN	ANTXR1	physical	28514442
ACAD9_HUMAN	ACAD9	physical	28514442
FBLN3_HUMAN	EFEMP1	physical	28514442
DJC13_HUMAN	DNAJC13	physical	28514442
PREB_HUMAN	PREB	physical	28514442
MA1A1_HUMAN	MAN1A1	physical	28514442
NED4L_HUMAN	NEDD4L	physical	28514442
TNFL9_HUMAN	TNFSF9	physical	28514442
CSK21_HUMAN	CSNK2A1	physical	23758859
ZO1_HUMAN	TJP1	physical	23758859
ZO2_HUMAN	TJP2	physical	23758859
OCLN_HUMAN	OCLN	physical	23758859

Drug and Disease Associations

Kegg Disease
H00840	Band-like calcification with simplified gyration and polymicrogyria (BLC-PMG); Pseudo-TORCH syndrome
OMIM Disease
251290	Band-like calcification with simplified gyration and polymicrogyria (BLCPMG)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of OCLN_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Identification and analysis of occludin phosphosites: a combined massspectrometry and bioinformatics approach."; Sundstrom J.M., Tash B.R., Murakami T., Flanagan J.M., Bewley M.C.,Stanley B.A., Gonsar K.B., Antonetti D.A.; J. Proteome Res. 8:808-817(2009). Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 416-522, AND PHOSPHORYLATIONAT SER-490.	19125584 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND MASSSPECTROMETRY.	18318008 [Abstract]
"PKC eta regulates occludin phosphorylation and epithelial tightjunction integrity."; Suzuki T., Elias B.C., Seth A., Shen L., Turner J.R., Giorgianni F.,Desiderio D., Guntaka R., Rao R.; Proc. Natl. Acad. Sci. U.S.A. 106:61-66(2009). Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-403 ANDTHR-404, AND MUTAGENESIS OF THR-404.	19114660 [Abstract]
"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 THR-305, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Phosphorylation of Tyr-398 and Tyr-402 in occludin prevents itsinteraction with ZO-1 and destabilizes its assembly at the tightjunctions."; Elias B.C., Suzuki T., Seth A., Giorgianni F., Kale G., Shen L.,Turner J.R., Naren A., Desiderio D.M., Rao R.; J. Biol. Chem. 284:1559-1569(2009). Cited for: INTERACTION WITH TJP1, PHOSPHORYLATION AT TYR-398 AND TYR-402,MUTAGENESIS OF TYR-398 AND TYR-402, AND SUBCELLULAR LOCATION.	19017651 [Abstract]

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