dbPTM

COR1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	COR1B_HUMAN
UniProt AC	Q9BR76
Protein Name	Coronin-1B
Gene Name	CORO1B
Organism	Homo sapiens (Human).
Sequence Length	489
Subcellular Localization	Cytoplasm, cytoskeleton . Localized to the leading edge in fibroblasts, as well as weakly along actin stress fibers.
Protein Description	Regulates leading edge dynamics and cell motility in fibroblasts. May be involved in cytokinesis and signal transduction (By similarity)..
Protein Sequence	MSFRKVVRQSKFRHVFGQPVKNDQCYEDIRVSRVTWDSTFCAVNPKFLAVIVEASGGGAFLVLPLSKTGRIDKAYPTVCGHTGPVLDIDWCPHNDEVIASGSEDCTVMVWQIPENGLTSPLTEPVVVLEGHTKRVGIIAWHPTARNVLLSAGCDNVVLIWNVGTAEELYRLDSLHPDLIYNVSWNHNGSLFCSACKDKSVRIIDPRRGTLVAEREKAHEGARPMRAIFLADGKVFTTGFSRMSERQLALWDPENLEEPMALQELDSSNGALLPFYDPDTSVVYVCGKGDSSIRYFEITEEPPYIHFLNTFTSKEPQRGMGSMPKRGLEVSKCEIARFYKLHERKCEPIVMTVPRKSDLFQDDLYPDTAGPEAALEAEEWVSGRDADPILISLREAYVPSKQRDLKISRRNVLSDSRPAMAPGSSHLGAPASTTTAADATPSGSLARAGEAGKLEEVMQELRALRALVKEQGDRICRLEEQLGRMENGDA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSFRKVVRQ ------CCHHHHHHH	33.48	16027158
21	Acetylation	HVFGQPVKNDQCYED HHHCCCCCCCCCCCC	62.58	26051181
21	Malonylation	HVFGQPVKNDQCYED HHHCCCCCCCCCCCC	62.58	26320211
26	Phosphorylation	PVKNDQCYEDIRVSR CCCCCCCCCCEEEEE	15.82	21253578
30	Methylation	DQCYEDIRVSRVTWD CCCCCCEEEEEEEEC	32.45	-
66	Phosphorylation	AFLVLPLSKTGRIDK EEEEEECCCCCCCCC	26.65	-
196	Acetylation	SLFCSACKDKSVRII CEEEHHHCCCCEEEE	68.83	26051181
199	Phosphorylation	CSACKDKSVRIIDPR EHHHCCCCEEEECCC	27.11	22817900
209	Phosphorylation	IIDPRRGTLVAEREK EECCCCCCEEEHHHH	19.08	22817900
233	Acetylation	AIFLADGKVFTTGFS EEEEECCCEEECCCC	34.42	130699
233	Ubiquitination	AIFLADGKVFTTGFS EEEEECCCEEECCCC	34.42	21890473
321	O-linked_Glycosylation	EPQRGMGSMPKRGLE CCCCCCCCCCCCCCC	24.02	30379171
330	O-linked_Glycosylation	PKRGLEVSKCEIARF CCCCCCCCHHHHHHH	23.39	30379171
331	Ubiquitination	KRGLEVSKCEIARFY CCCCCCCHHHHHHHH	40.85	-
339	Ubiquitination	CEIARFYKLHERKCE HHHHHHHHHHHCCCE	40.43	-
339	Acetylation	CEIARFYKLHERKCE HHHHHHHHHHHCCCE	40.43	22644347
344	Ubiquitination	FYKLHERKCEPIVMT HHHHHHCCCEEEEEE	39.71	-
345	Glutathionylation	YKLHERKCEPIVMTV HHHHHCCCEEEEEEC	10.61	22555962
350	Sulfoxidation	RKCEPIVMTVPRKSD CCCEEEEEECCCCCC	3.02	30846556
355	Ubiquitination	IVMTVPRKSDLFQDD EEEECCCCCCCCCCC	42.10	21890473
381	Phosphorylation	LEAEEWVSGRDADPI HHHHHHHCCCCCCCE	29.23	18452278
399	Phosphorylation	LREAYVPSKQRDLKI EHHHHCCCCCCCCCC	31.23	24719451
400	Ubiquitination	REAYVPSKQRDLKIS HHHHCCCCCCCCCCH	43.19	-
407	Phosphorylation	KQRDLKISRRNVLSD CCCCCCCHHHHHCCC	24.49	24719451
413	Phosphorylation	ISRRNVLSDSRPAMA CHHHHHCCCCCCCCC	29.29	20068231
415	Phosphorylation	RRNVLSDSRPAMAPG HHHHCCCCCCCCCCC	36.47	20068231
423	Phosphorylation	RPAMAPGSSHLGAPA CCCCCCCCCCCCCCC	17.33	20068231
424	Phosphorylation	PAMAPGSSHLGAPAS CCCCCCCCCCCCCCC	28.75	20068231
431	Phosphorylation	SHLGAPASTTTAADA CCCCCCCCCCCCCCC	25.81	28857561
432	Phosphorylation	HLGAPASTTTAADAT CCCCCCCCCCCCCCC	30.21	28857561
433	Phosphorylation	LGAPASTTTAADATP CCCCCCCCCCCCCCC	16.37	28857561
434	Phosphorylation	GAPASTTTAADATPS CCCCCCCCCCCCCCC	21.67	28857561
439	Phosphorylation	TTTAADATPSGSLAR CCCCCCCCCCCHHHC	20.66	29496963
441	Phosphorylation	TAADATPSGSLARAG CCCCCCCCCHHHCCC	36.34	28348404
443	Phosphorylation	ADATPSGSLARAGEA CCCCCCCHHHCCCCC	24.16	25850435
452	Acetylation	ARAGEAGKLEEVMQE HCCCCCCCHHHHHHH	60.83	26051181
457	Sulfoxidation	AGKLEEVMQELRALR CCCHHHHHHHHHHHH	2.64	30846556

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
2	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
2	S	Phosphorylation	Kinase	PKCE	Q02156	PSP
2	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
2	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
2	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
2	S	Phosphorylation		16027158
Phosphorylation by PKC on Ser-2 regulates the interaction with the Arp2/3 complex and cell motility in fibroblasts.

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 COR1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SAFB1_HUMAN	SAFB	physical	22939629
NU107_HUMAN	NUP107	physical	22939629
TPM2_HUMAN	TPM2	physical	22939629
EPIPL_HUMAN	EPPK1	physical	22939629
VATF_HUMAN	ATP6V1F	physical	22939629
SRC8_HUMAN	CTTN	physical	22939629
TELO2_HUMAN	TELO2	physical	22939629
RPAC1_HUMAN	POLR1C	physical	21988832
IMA1_HUMAN	KPNA2	physical	21988832
ERF1_HUMAN	ETF1	physical	22863883
NUDC_HUMAN	NUDC	physical	22863883
PAPOA_HUMAN	PAPOLA	physical	22863883
PARVA_HUMAN	PARVA	physical	22863883
SWP70_HUMAN	SWAP70	physical	22863883
TBC17_HUMAN	TBC1D17	physical	22863883
ZYX_HUMAN	ZYX	physical	22863883
ACTB_HUMAN	ACTB	physical	26344197
ACTG_HUMAN	ACTG1	physical	26344197
LSM2_HUMAN	LSM2	physical	26344197
RUVB2_HUMAN	RUVBL2	physical	26344197
SPTN2_HUMAN	SPTBN2	physical	26344197
TIPRL_HUMAN	TIPRL	physical	26344197
IFT57_HUMAN	IFT57	physical	27173435

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 COR1B_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphorylation of coronin 1B by protein kinase C regulatesinteraction with Arp2/3 and cell motility."; Cai L., Holoweckyj N., Schaller M.D., Bear J.E.; J. Biol. Chem. 280:31913-31923(2005). Cited for: FUNCTION, HOMOOLIGOMERIZATION, INTERACTION WITH ACTR2; ARPC1B ANDARPC2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2, AND MUTAGENESISOF SER-2.	16027158 [Abstract]

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