dbPTM

GELS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GELS_HUMAN
UniProt AC	P06396
Protein Name	Gelsolin
Gene Name	GSN
Organism	Homo sapiens (Human).
Sequence Length	782
Subcellular Localization	Isoform 2: Cytoplasm, cytoskeleton. Isoform 1: Secreted.
Protein Description	Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis..
Protein Sequence	MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEARPNSMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLFQVKGRRVVRATEVPVSWESFNNGDCFILDLGNNIHQWCGSNSNRYERLKATQVSKGIRDNERSGRARVHVSEEGTEPEAMLQVLGPKPALPAGTEDTAKEDAANRKLAKLYKVSNGAGTMSVSLVADENPFAQGALKSEDCFILDHGKDGKIFVWKGKQANTEERKAALKTASDFITKMDYPKQTQVSVLPEGGETPLFKQFFKNWRDPDQTDGLGLSYLSSHIANVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSREGGQTAPASTRLFQVRANSAGATRAVEVLPKAGALNSNDAFVLKTPSAAYLWVGTGASEAEKTGAQELLRVLRAQPVQVAEGSEPDGFWEALGGKAAYRTSPRLKDKKMDAHPPRLFACSNKIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPITVVKQGFEPPSFVGWFLGWDDDYWSVDPLDRAMAELAA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Acetylation	PHRPAPALLCALSLA CCCCHHHHHHHHHHH	3.82	19608861
11 (in isoform 3)	Phosphorylation	-	1.42	27251275
18	Acetylation	LCALSLALCALSLPV HHHHHHHHHHHCCHH	1.81	19608861
21	Acetylation	LSLALCALSLPVRAA HHHHHHHHCCHHHHH	5.43	19608861
31	O-linked_Glycosylation	PVRAATASRGASQAG HHHHHHHHCCHHHCC	27.22	OGP
35	O-linked_Glycosylation	ATASRGASQAGAPQG HHHHCCHHHCCCCCC	24.32	76973135
35	Phosphorylation	ATASRGASQAGAPQG HHHHCCHHHCCCCCC	24.32	28857561
51	Phosphorylation	VPEARPNSMVVEHPE CCCCCCCCEEECCHH	18.68	28270605
61	Acetylation	VEHPEFLKAGKEPGL ECCHHHHHCCCCCCC	61.49	19608861
86	Phosphorylation	VPVPTNLYGDFFTGD EECCCCCCCCCCCCC	19.40	22817900
174	Phosphorylation	YKKGGVASGFKHVVP CCCCCCCCCCCCCCC	42.21	28060719
194 (in isoform 2)	Ubiquitination	-	24.62	-
202	Ubiquitination	RRVVRATEVPVSWES EEEEEEEECCCCHHH	43.79	-
239	Ubiquitination	SNRYERLKATQVSKG CCHHHHHHHHEECCC	56.46	-
245	Acetylation	LKATQVSKGIRDNER HHHHEECCCCCCCCC	60.54	12650337
245	Ubiquitination	LKATQVSKGIRDNER HHHHEECCCCCCCCC	60.54	-
251 (in isoform 2)	Ubiquitination	-	53.14	-
259	Ubiquitination	RSGRARVHVSEEGTE CCCCCEEEECCCCCC	16.31	-
261	Phosphorylation	GRARVHVSEEGTEPE CCCEEEECCCCCCCH	18.30	29255136
265	Phosphorylation	VHVSEEGTEPEAMLQ EEECCCCCCCHHHHH	52.20	29255136
304	Phosphorylation	LAKLYKVSNGAGTMS HHHHEEECCCCCEEE	25.95	25850435
309	Phosphorylation	KVSNGAGTMSVSLVA EECCCCCEEEEEEEE	13.02	25850435
309 (in isoform 2)	Ubiquitination	-	13.02	-
311	Phosphorylation	SNGAGTMSVSLVADE CCCCCEEEEEEEECC	14.37	25850435
313	Phosphorylation	GAGTMSVSLVADENP CCCEEEEEEEECCCC	15.15	25850435
317	Ubiquitination	MSVSLVADENPFAQG EEEEEEECCCCCCCC	49.04	21890473
317	Ubiquitination	MSVSLVADENPFAQG EEEEEEECCCCCCCC	49.04	-
317 (in isoform 2)	Ubiquitination	-	49.04	21890473
322 (in isoform 2)	Ubiquitination	-	14.25	21890473
325	Ubiquitination	ENPFAQGALKSEDCF CCCCCCCCCCCCCEE	10.35	-
328	Ubiquitination	FAQGALKSEDCFILD CCCCCCCCCCEEEEE	39.25	21890473
328	Ubiquitination	FAQGALKSEDCFILD CCCCCCCCCCEEEEE	39.25	21890473
330	Ubiquitination	QGALKSEDCFILDHG CCCCCCCCEEEEECC	39.45	-
360	Ubiquitination	EERKAALKTASDFIT HHHHHHHHHHHHHHH	37.00	-
361	Phosphorylation	ERKAALKTASDFITK HHHHHHHHHHHHHHH	32.04	20068231
363	Phosphorylation	KAALKTASDFITKMD HHHHHHHHHHHHHCC	37.98	20068231
367	Phosphorylation	KTASDFITKMDYPKQ HHHHHHHHHCCCCCC	21.95	20068231
368	Malonylation	TASDFITKMDYPKQT HHHHHHHHCCCCCCC	25.59	26320211
368	Ubiquitination	TASDFITKMDYPKQT HHHHHHHHCCCCCCC	25.59	21890473
368 (in isoform 1)	Ubiquitination	-	25.59	21890473
368	Ubiquitination	TASDFITKMDYPKQT HHHHHHHHCCCCCCC	25.59	21890473
371	Phosphorylation	DFITKMDYPKQTQVS HHHHHCCCCCCCEEE	14.61	26074081
373	Ubiquitination	ITKMDYPKQTQVSVL HHHCCCCCCCEEEEC	60.80	21906983
373 (in isoform 1)	Ubiquitination	-	60.80	21890473
378	Phosphorylation	YPKQTQVSVLPEGGE CCCCCEEEECCCCCC	14.23	28857561
386	Phosphorylation	VLPEGGETPLFKQFF ECCCCCCCHHHHHHH	28.68	21815630
390	Acetylation	GGETPLFKQFFKNWR CCCCHHHHHHHHCCC	54.61	129347
397	Methylation	KQFFKNWRDPDQTDG HHHHHCCCCCCCCCC	55.78	-
402	O-linked_Glycosylation	NWRDPDQTDGLGLSY CCCCCCCCCCCCHHH	39.14	OGP
404	N-myristoyl glycine	RDPDQTDGLGLSYLS CCCCCCCCCCHHHHH	25.65	-
408	O-linked_Glycosylation	QTDGLGLSYLSSHIA CCCCCCHHHHHHHCC	23.41	OGP
408	Phosphorylation	QTDGLGLSYLSSHIA CCCCCCHHHHHHHCC	23.41	28857561
409	Phosphorylation	TDGLGLSYLSSHIAN CCCCCHHHHHHHCCC	18.69	22817900
411	O-linked_Glycosylation	GLGLSYLSSHIANVE CCCHHHHHHHCCCCC	16.19	OGP
411	Phosphorylation	GLGLSYLSSHIANVE CCCHHHHHHHCCCCC	16.19	24076635
412	O-linked_Glycosylation	LGLSYLSSHIANVER CCHHHHHHHCCCCCC	19.13	OGP
412	Phosphorylation	LGLSYLSSHIANVER CCHHHHHHHCCCCCC	19.13	24076635
426	O-linked_Glycosylation	RVPFDAATLHTSTAM CCCCCHHHCCHHHHH	22.31	OGP
426	Phosphorylation	RVPFDAATLHTSTAM CCCCCHHHCCHHHHH	22.31	28857561
429	Phosphorylation	FDAATLHTSTAMAAQ CCHHHCCHHHHHHHH	30.77	28857561
430	O-linked_Glycosylation	DAATLHTSTAMAAQH CHHHCCHHHHHHHHC	11.92	OGP
430	Phosphorylation	DAATLHTSTAMAAQH CHHHCCHHHHHHHHC	11.92	28857561
431	O-linked_Glycosylation	AATLHTSTAMAAQHG HHHCCHHHHHHHHCC	22.93	55829949
431	Phosphorylation	AATLHTSTAMAAQHG HHHCCHHHHHHHHCC	22.93	28857561
433	Sulfoxidation	TLHTSTAMAAQHGMD HCCHHHHHHHHCCCC	3.00	30846556
439	Sulfoxidation	AMAAQHGMDDDGTGQ HHHHHCCCCCCCCCC	4.85	30846556
455	Phosphorylation	QIWRIEGSNKVPVDP EEEEEECCCCCCCCH	22.23	27251275
465	Phosphorylation	VPVDPATYGQFYGGD CCCCHHHCEEEECCC	15.84	22817900
473	Phosphorylation	GQFYGGDSYIILYNY EEEECCCEEEEEEEE	22.85	-
478	Phosphorylation	GDSYIILYNYRHGGR CCEEEEEEEECCCCC	10.35	-
480	Phosphorylation	SYIILYNYRHGGRQG EEEEEEEECCCCCCE	7.16	-
533	Ubiquitination	VVQGKEPAHLMSLFG CCCCCCCHHHHHHHC	14.99	21890473
533 (in isoform 2)	Ubiquitination	-	14.99	21890473
536	Sulfoxidation	GKEPAHLMSLFGGKP CCCCHHHHHHHCCCC	2.04	30846556
537	Phosphorylation	KEPAHLMSLFGGKPM CCCHHHHHHHCCCCE	27.23	20860994
541	Ubiquitination	HLMSLFGGKPMIIYK HHHHHHCCCCEEEEE	24.45	-
544	Ubiquitination	SLFGGKPMIIYKGGT HHHCCCCEEEEECCC	3.11	21890473
544	Ubiquitination	SLFGGKPMIIYKGGT HHHCCCCEEEEECCC	3.11	21890473
544	Sulfoxidation	SLFGGKPMIIYKGGT HHHCCCCEEEEECCC	3.11	30846556
547	Phosphorylation	GGKPMIIYKGGTSRE CCCCEEEEECCCCCC	7.83	29978859
548	Malonylation	GKPMIIYKGGTSREG CCCEEEEECCCCCCC	40.22	26320211
551	Phosphorylation	MIIYKGGTSREGGQT EEEEECCCCCCCCCC	33.02	29978859
552	Phosphorylation	IIYKGGTSREGGQTA EEEECCCCCCCCCCC	31.45	29978859
558	Phosphorylation	TSREGGQTAPASTRL CCCCCCCCCCCCCEE	37.57	29978859
562	Phosphorylation	GGQTAPASTRLFQVR CCCCCCCCCEEEEEE	17.01	26437602
563	Phosphorylation	GQTAPASTRLFQVRA CCCCCCCCEEEEEEC	33.23	29978859
584	Acetylation	RAVEVLPKAGALNSN EEEEECCCCCCCCCC	56.12	-
584	Malonylation	RAVEVLPKAGALNSN EEEEECCCCCCCCCC	56.12	26320211
584	Ubiquitination	RAVEVLPKAGALNSN EEEEECCCCCCCCCC	56.12	21890473
584 (in isoform 1)	Ubiquitination	-	56.12	21890473
584	Ubiquitination	RAVEVLPKAGALNSN EEEEECCCCCCCCCC	56.12	21890473
590	Phosphorylation	PKAGALNSNDAFVLK CCCCCCCCCCEEEEE	36.62	23911959
597 (in isoform 2)	Ubiquitination	-	53.76	-
598	Phosphorylation	NDAFVLKTPSAAYLW CCEEEEECCCCEEEE	20.51	28857561
600	Phosphorylation	AFVLKTPSAAYLWVG EEEEECCCCEEEEEC	30.66	28857561
603	Phosphorylation	LKTPSAAYLWVGTGA EECCCCEEEEECCCC	10.79	28857561
605	Ubiquitination	TPSAAYLWVGTGASE CCCCEEEEECCCCCH	3.62	-
608	Phosphorylation	AAYLWVGTGASEAEK CEEEEECCCCCHHHH	21.69	24076635
611	Phosphorylation	LWVGTGASEAEKTGA EEECCCCCHHHHHCH	38.39	-
636	Phosphorylation	PVQVAEGSEPDGFWE CEEEECCCCCCCHHH	37.14	26657352
648	Acetylation	FWEALGGKAAYRTSP HHHHCCCCCCCCCCC	28.22	90247
651	Phosphorylation	ALGGKAAYRTSPRLK HCCCCCCCCCCCCCC	21.20	26699800
653	Phosphorylation	GGKAAYRTSPRLKDK CCCCCCCCCCCCCCC	30.33	26699800
654	Phosphorylation	GKAAYRTSPRLKDKK CCCCCCCCCCCCCCC	10.06	26699800
673	Phosphorylation	PPRLFACSNKIGRFV CCCEEEECCCCCCEE	37.41	28857561
677 (in isoform 2)	Ubiquitination	-	20.70	21890473
685	Ubiquitination	RFVIEEVPGELMQED CEEEEECCCHHHHHH	33.54	-
715	Phosphorylation	FVWVGKDSQEEEKTE EEEECCCCCHHHHHH	42.87	23312004
721	Phosphorylation	DSQEEEKTEALTSAK CCCHHHHHHHHHHHH	29.75	23312004
725	Phosphorylation	EEKTEALTSAKRYIE HHHHHHHHHHHHHHH	33.42	23312004
726	Phosphorylation	EKTEALTSAKRYIET HHHHHHHHHHHHHHC	32.42	23312004
728	Acetylation	TEALTSAKRYIETDP HHHHHHHHHHHHCCC	45.56	7672103
728	Ubiquitination	TEALTSAKRYIETDP HHHHHHHHHHHHCCC	45.56	2190698
728 (in isoform 1)	Ubiquitination	-	45.56	21890473
742	Phosphorylation	PANRDRRTPITVVKQ CCCCCCCCCEEEEEC	21.67	2176481

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
35	Y	Phosphorylation	Kinase	SRC	P12931	GPS
86	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
358	Y	Phosphorylation	Kinase	SRC	P12931	GPS
409	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
414	Y	Phosphorylation	Kinase	SRC	P12931	GPS
465	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
465	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
552	Y	Phosphorylation	Kinase	SRC	P12931	GPS
600	Y	Phosphorylation	Kinase	SRC	P12931	GPS
603	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
651	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANDR_HUMAN	AR	physical	12941811
FAK2_HUMAN	PTK2B	physical	12578912
TM1L1_HUMAN	TOM1L1	physical	16169070
ACTS_HUMAN	ACTA1	physical	10583954
VDAC1_HUMAN	VDAC1	physical	11039896
FINC_HUMAN	FN1	physical	6092370
PK3CA_HUMAN	PIK3CA	physical	11577104
FAK1_HUMAN	PTK2	physical	11577104
VINC_HUMAN	VCL	physical	11577104
PAXI_HUMAN	PXN	physical	11577104
SRC_HUMAN	SRC	physical	11577104
PTN12_HUMAN	PTPN12	physical	11577104
A4_HUMAN	APP	physical	10329371
ACTN4_HUMAN	ACTN4	physical	11733011
ACTS_HUMAN	ACTA1	physical	8395021
CFLAR_HUMAN	CFLAR	physical	25246592
ITCH_HUMAN	ITCH	physical	25246592

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
105120	Amyloidosis 5 (AMYL5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GELS_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Identification of Tyr438 as the major in vitro c-Src phosphorylationsite in human gelsolin: a mass spectrometric approach."; De Corte V., Demol H., Goethals M., Van Damme J., Gettemans J.,Vandekerckhove J.; Protein Sci. 8:234-241(1999). Cited for: PHOSPHORYLATION AT TYR-86; TYR-409; TYR-465; TYR-603 AND TYR-651.	10210201 [Abstract]