dbPTM

AF1L2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AF1L2_HUMAN
UniProt AC	Q8N4X5
Protein Name	Actin filament-associated protein 1-like 2
Gene Name	AFAP1L2
Organism	Homo sapiens (Human).
Sequence Length	818
Subcellular Localization	Cytoplasm .
Protein Description	May play a role in a signaling cascade by enhancing the kinase activity of SRC. Contributes to SRC-regulated transcription activation..
Protein Sequence	MERYKALEQLLTELDDFLKILDQENLSSTALVKKSCLAELLRLYTKSSSSDEEYIYMNKVTINKQQNAESQGKAPEEQGLLPNGEPSQHSSAPQKSLPDLPPPKMIPERKQLAIPKTESPEGYYEEAEPYDTSLNEDGEAVSSSYESYDEEDGSKGKSAPYQWPSPEAGIELMRDARICAFLWRKKWLGQWAKQLCVIKDNRLLCYKSSKDHSPQLDVNLLGSSVIHKEKQVRKKEHKLKITPMNADVIVLGLQSKDQAEQWLRVIQEVSGLPSEGASEGNQYTPDAQRFNCQKPDIAEKYLSASEYGSSVDGHPEVPETKDVKKKCSAGLKLSNLMNLGRKKSTSLEPVERSLETSSYLNVLVNSQWKSRWCSVRDNHLHFYQDRNRSKVAQQPLSLVGCEVVPDPSPDHLYSFRILHKGEELAKLEAKSSEEMGHWLGLLLSESGSKTDPEEFTYDYVDADRVSCIVSAAKNSLLLMQRKFSEPNTYIDGLPSQDRQEELYDDVDLSELTAAVEPTEEATPVADDPNERESDRVYLDLTPVKSFLHGPSSAQAQASSPTLSCLDNATEALPADSGPGPTPDEPCIKCPENLGEQQLESLEPEDPSLRITTVKIQTEQQRISFPPSCPDAVVATPPGASPPVKDRLRVTSAEIKLGKNRTEAEVKRYTEEKERLEKKKEEIRGHLAQLRKEKRELKETLLKCTDKEVLASLEQKLKEIDEECRGEESRRVDLELSIMEVKDNLKKAEAGPVTLGTTVDTTHLENVSPRPKAVTPASAPDCTPVNSATTLKNRPLSVVVTGKGTVLQKAKEWEKKGAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	2-Hydroxyisobutyrylation	LSSTALVKKSCLAEL CCCCHHHHHHHHHHH	39.56	-
44	Phosphorylation	LAELLRLYTKSSSSD HHHHHHHHHCCCCCC	12.99	27273156
47	Phosphorylation	LLRLYTKSSSSDEEY HHHHHHCCCCCCCCE	27.87	26356563
48	Phosphorylation	LRLYTKSSSSDEEYI HHHHHCCCCCCCCEE	35.10	26356563
49	Phosphorylation	RLYTKSSSSDEEYIY HHHHCCCCCCCCEEE	49.23	26356563
50	Phosphorylation	LYTKSSSSDEEYIYM HHHCCCCCCCCEEEE	51.49	26356563
54	Phosphorylation	SSSSDEEYIYMNKVT CCCCCCCEEEEEEEE	8.70	19060924
56	Phosphorylation	SSDEEYIYMNKVTIN CCCCCEEEEEEEEEC	8.17	27273156
61	Phosphorylation	YIYMNKVTINKQQNA EEEEEEEEECCCCCH	22.05	26356563
96	Phosphorylation	HSSAPQKSLPDLPPP CCCCCCCCCCCCCCC	39.63	28348404
119	Phosphorylation	LAIPKTESPEGYYEE CCCCCCCCCCCCCCC	33.22	9449045
124	Phosphorylation	TESPEGYYEEAEPYD CCCCCCCCCCCCCCC	20.39	138541
158	Phosphorylation	EDGSKGKSAPYQWPS CCCCCCCCCCCCCCC	43.05	25106551
161	Phosphorylation	SKGKSAPYQWPSPEA CCCCCCCCCCCCHHH	23.95	25106551
165	Phosphorylation	SAPYQWPSPEAGIEL CCCCCCCCHHHHHHH	32.20	22777824
208	Phosphorylation	NRLLCYKSSKDHSPQ CEEEEEECCCCCCCC	19.02	23312004
209	Phosphorylation	RLLCYKSSKDHSPQL EEEEEECCCCCCCCC	37.64	23312004
213	Phosphorylation	YKSSKDHSPQLDVNL EECCCCCCCCCCHHH	25.19	25056879
223	Phosphorylation	LDVNLLGSSVIHKEK CCHHHHCHHHHCHHH	22.77	23312004
224	Phosphorylation	DVNLLGSSVIHKEKQ CHHHHCHHHHCHHHH	24.24	23312004
278	Phosphorylation	GLPSEGASEGNQYTP CCCCCCCCCCCCCCC	57.82	28348404
283	Phosphorylation	GASEGNQYTPDAQRF CCCCCCCCCCCHHHH	25.00	27251275
284	Phosphorylation	ASEGNQYTPDAQRFN CCCCCCCCCCHHHHC	12.62	25056879
301	Phosphorylation	KPDIAEKYLSASEYG CCHHHHHHCCHHHHC	9.44	23090842
303	Phosphorylation	DIAEKYLSASEYGSS HHHHHHCCHHHHCCC	27.02	25394399
305	Phosphorylation	AEKYLSASEYGSSVD HHHHCCHHHHCCCCC	28.16	25106551
307	Phosphorylation	KYLSASEYGSSVDGH HHCCHHHHCCCCCCC	21.58	25394399
309	Phosphorylation	LSASEYGSSVDGHPE CCHHHHCCCCCCCCC	26.70	25106551
310	Phosphorylation	SASEYGSSVDGHPEV CHHHHCCCCCCCCCC	21.62	23090842
320	Phosphorylation	GHPEVPETKDVKKKC CCCCCCCCCCHHHHH	26.86	27307780
332	Methylation	KKCSAGLKLSNLMNL HHHCCCCHHHHHHHC	49.29	-
334	Phosphorylation	CSAGLKLSNLMNLGR HCCCCHHHHHHHCCC	26.74	101663561
344	Phosphorylation	MNLGRKKSTSLEPVE HHCCCCCCCCCCCCH	26.68	29255136
345	Phosphorylation	NLGRKKSTSLEPVER HCCCCCCCCCCCCHH	46.33	29255136
346	Phosphorylation	LGRKKSTSLEPVERS CCCCCCCCCCCCHHH	37.51	29255136
353	Phosphorylation	SLEPVERSLETSSYL CCCCCHHHHHCHHHH	19.63	28442448
356	Phosphorylation	PVERSLETSSYLNVL CCHHHHHCHHHHHHH	28.41	28442448
357	Phosphorylation	VERSLETSSYLNVLV CHHHHHCHHHHHHHH	13.96	28442448
358	Phosphorylation	ERSLETSSYLNVLVN HHHHHCHHHHHHHHC	40.85	24872395
359	Phosphorylation	RSLETSSYLNVLVNS HHHHCHHHHHHHHCC	11.32	27259358
383	Phosphorylation	RDNHLHFYQDRNRSK HHCCEEEEECCCCHH	9.96	21082442
397	Phosphorylation	KVAQQPLSLVGCEVV HHCCCCHHHCCCEEC	27.91	26356563
408	Phosphorylation	CEVVPDPSPDHLYSF CEECCCCCCCCEEEE	50.79	29255136
413	Phosphorylation	DPSPDHLYSFRILHK CCCCCCEEEEEEEEC	11.44	29255136
414	Phosphorylation	PSPDHLYSFRILHKG CCCCCEEEEEEEECC	17.89	29255136
431	Phosphorylation	LAKLEAKSSEEMGHW HHHHCCCCHHHHHHH	50.45	50563843
432	Phosphorylation	AKLEAKSSEEMGHWL HHHCCCCHHHHHHHH	36.55	50563851
456	Phosphorylation	KTDPEEFTYDYVDAD CCCHHHHCCCEECHH	20.82	30814731
457	Phosphorylation	TDPEEFTYDYVDADR CCHHHHCCCEECHHH	15.59	25106551
459	Phosphorylation	PEEFTYDYVDADRVS HHHHCCCEECHHHHH	6.99	25348954
466	Phosphorylation	YVDADRVSCIVSAAK EECHHHHHHHHHHHH	10.06	30835091
470	Phosphorylation	DRVSCIVSAAKNSLL HHHHHHHHHHHHHHH	11.55	25348954
484	Phosphorylation	LLMQRKFSEPNTYID HHHHHHCCCCCCCCC	56.00	28355574
488	Phosphorylation	RKFSEPNTYIDGLPS HHCCCCCCCCCCCCC	32.35	30108239
489	Phosphorylation	KFSEPNTYIDGLPSQ HCCCCCCCCCCCCCH	12.03	30108239
537	Phosphorylation	ERESDRVYLDLTPVK CCCCCCEEEECCCCH	8.73	25394399
541	Phosphorylation	DRVYLDLTPVKSFLH CCEEEECCCCHHHHC	26.21	19664994
545	Phosphorylation	LDLTPVKSFLHGPSS EECCCCHHHHCCCCC	33.02	30206219
551	Phosphorylation	KSFLHGPSSAQAQAS HHHHCCCCCHHHHCC	42.79	28387310
552	Phosphorylation	SFLHGPSSAQAQASS HHHCCCCCHHHHCCC	27.77	30206219
558	Phosphorylation	SSAQAQASSPTLSCL CCHHHHCCCCCCHHH	25.44	28857561
559	Phosphorylation	SAQAQASSPTLSCLD CHHHHCCCCCCHHHH	25.56	28857561
561	Phosphorylation	QAQASSPTLSCLDNA HHHCCCCCCHHHHCH	33.00	28857561
563	Phosphorylation	QASSPTLSCLDNATE HCCCCCCHHHHCHHH	18.34	30206219
569	Phosphorylation	LSCLDNATEALPADS CHHHHCHHHCCCCCC	28.22	25002506
576	Phosphorylation	TEALPADSGPGPTPD HHCCCCCCCCCCCCC	49.33	25002506
600	Phosphorylation	LGEQQLESLEPEDPS CCHHHHHHCCCCCCC	46.77	113326983
617	Phosphorylation	ITTVKIQTEQQRISF EEEEEEEECHHCCCC	38.95	23312004
623	Phosphorylation	QTEQQRISFPPSCPD EECHHCCCCCCCCCC	33.61	23312004
627	Phosphorylation	QRISFPPSCPDAVVA HCCCCCCCCCCCEEE	38.22	28102081
635	Phosphorylation	CPDAVVATPPGASPP CCCCEEECCCCCCCC	20.57	22777824
640	Phosphorylation	VATPPGASPPVKDRL EECCCCCCCCHHHHE	35.33	29255136
650	Phosphorylation	VKDRLRVTSAEIKLG HHHHEEEEHEEEECC	18.78	27794612
651	Phosphorylation	KDRLRVTSAEIKLGK HHHEEEEHEEEECCC	22.50	54886155
668	Phosphorylation	TEAEVKRYTEEKERL CHHHHHHHHHHHHHH	16.88	72499757
669	Phosphorylation	EAEVKRYTEEKERLE HHHHHHHHHHHHHHH	41.52	72499763
697	Acetylation	RKEKRELKETLLKCT HHHHHHHHHHHHHCC	43.85	18527893
728	Phosphorylation	EECRGEESRRVDLEL HHHCCCHHHCCCEEE	22.53	29449344
736	Phosphorylation	RRVDLELSIMEVKDN HCCCEEEEEEEHHHH	15.54	24505115
753	Phosphorylation	KAEAGPVTLGTTVDT HHCCCCEEECCEEEC	23.70	23312004
756	Phosphorylation	AGPVTLGTTVDTTHL CCCEEECCEEECCCH	27.10	28348404
757	Phosphorylation	GPVTLGTTVDTTHLE CCEEECCEEECCCHH	18.00	28348404
760	Phosphorylation	TLGTTVDTTHLENVS EECCEEECCCHHCCC	16.27	28348404
761	O-linked_Glycosylation	LGTTVDTTHLENVSP ECCEEECCCHHCCCC	21.72	30379171
761	Phosphorylation	LGTTVDTTHLENVSP ECCEEECCCHHCCCC	21.72	28348404
767	Phosphorylation	TTHLENVSPRPKAVT CCCHHCCCCCCCCCC	27.12	25850435
774	Phosphorylation	SPRPKAVTPASAPDC CCCCCCCCCCCCCCC	20.28	10401181
788	Phosphorylation	CTPVNSATTLKNRPL CCCCCCCCCCCCCCC	32.27	10401193
796	Phosphorylation	TLKNRPLSVVVTGKG CCCCCCCEEEEECCC	18.62	28731282
800	Phosphorylation	RPLSVVVTGKGTVLQ CCCEEEEECCCCHHH	22.90	23312004
804	Phosphorylation	VVVTGKGTVLQKAKE EEEECCCCHHHHHHH	22.87	23312004

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
54	Y	Phosphorylation	Kinase	RET	P07949	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AF1L2_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 AF1L2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
A4_HUMAN	APP	physical	21832049

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 AF1L2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-668 AND THR-669, ANDMASS SPECTROMETRY.	17924679 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-413, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-383 AND TYR-413, ANDMASS SPECTROMETRY.	18083107 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-413, AND MASSSPECTROMETRY.	15951569 [Abstract]