dbPTM

SHOT1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SHOT1_MOUSE
UniProt AC	Q8K2Q9
Protein Name	Shootin-1 {ECO:0000312\|MGI:MGI:1918903}
Gene Name	Shtn1 {ECO:0000312\|MGI:MGI:1918903}
Organism	Mus musculus (Mouse).
Sequence Length	631
Subcellular Localization	Perikaryon . Cell projection, axon . Cell projection, growth cone . Cytoplasm, cytoskeleton . Cell projection, filopodium . Cell projection, lamellipodium . Localizes in multiple growth cones at neurite tips before the neuronal symmetry-breaking step
Protein Description	Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth. [PubMed: 23864681 Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of CDC42, RAC1 and PAK1-dependent signaling pathway, thereby converting the F-actin retrograde flow into traction forces, concomitantly with filopodium extension and axon outgrowth. Plays a role in cytoskeletal organization by regulating the subcellular localization of phosphoinositide 3-kinase (PI3K) activity at the axonal growth cone. Plays also a role in regenerative neurite outgrowth (By similarity In the developing cortex, cooperates with KIF20B to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex]
Protein Sequence	MNSSDEEKQLQLITSLKEQAIGEYEDLRAENQKTKEKCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHLEIEKTCRESAEALATKLNKENKTLKRISMLYMAKLGPDVITEEINIDDDDPATDTDAAAETCVSVQCQKQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSMLAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQKKVKELEERLENEALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMSMIRKRSHPSGNSAKKEKTTQPETAEEVTDLKRQAVEEMMDRIKKGVHLRPVNQTARPKAKPDSLKGSESAVDELKGILGTLNKSTSSRSLKSLGPENSETELERILRRRKLTAEADSSSPTGILATSESKSMPVLGSVSSVTKSALNKKTLEAEFNNPCPLTPEPGEGPRKLEGCTNPKVTFQPPSKGGYRRKCVGSENQAEPVVVLDPVSTHEPQTKDQAAEKDPTQFEEEGGETQPEYKEDSGGKTGETDSSNC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNSSDEEK -------CCCHHHHH	11.22	17242355
1	Oxidation	-------MNSSDEEK -------CCCHHHHH	11.22	17242355
3	Phosphorylation	-----MNSSDEEKQL -----CCCHHHHHHH	37.56	21743459
4	Phosphorylation	----MNSSDEEKQLQ ----CCCHHHHHHHH	44.00	21743459
14	Phosphorylation	EKQLQLITSLKEQAI HHHHHHHHHHHHHHH	36.28	29472430
15	Phosphorylation	KQLQLITSLKEQAIG HHHHHHHHHHHHHHH	30.37	29472430
24	Phosphorylation	KEQAIGEYEDLRAEN HHHHHHHHHHHHHHH	14.99	25159016
59	Phosphorylation	LEEFQKISHMVIEEV HHHHHHHHHHHHHHH	16.74	-
89	Ubiquitination	SAEALATKLNKENKT HHHHHHHHHHHHCHH	44.44	22790023
101	Phosphorylation	NKTLKRISMLYMAKL CHHHHHHHHHHHHHH	13.53	26239621
233	Phosphorylation	DLRKKAESFAQEMFI HHHHHHHHHHHHHHH	30.64	-
244	Ubiquitination	EMFIEQNKLKRQSHL HHHHHHCHHHHHHHH	55.89	22790023
249	Phosphorylation	QNKLKRQSHLLLQSS HCHHHHHHHHHHHCC	21.82	25521595
256	Phosphorylation	SHLLLQSSLPDQQLL HHHHHHCCCCHHHHH	30.84	25367039
286	Acetylation	ERIQHQKKVKELEER HHHHHHHHHHHHHHH	52.55	23576753
288	Acetylation	IQHQKKVKELEERLE HHHHHHHHHHHHHHH	66.51	23576753
372	Phosphorylation	PPPNPIRSLMSMIRK CCCCHHHHHHHHHHH	29.19	29472430
375	Phosphorylation	NPIRSLMSMIRKRSH CHHHHHHHHHHHCCC	19.15	28725479
381	Phosphorylation	MSMIRKRSHPSGNSA HHHHHHCCCCCCCCC	42.67	-
384	Phosphorylation	IRKRSHPSGNSAKKE HHHCCCCCCCCCCCC	45.22	30635358
387	Phosphorylation	RSHPSGNSAKKEKTT CCCCCCCCCCCCCCC	45.02	30635358
392	Methylation	GNSAKKEKTTQPETA CCCCCCCCCCCCCCH	66.79	-
438	Phosphorylation	RPKAKPDSLKGSESA CCCCCCCCCCCCHHH	40.27	29176673
442	Phosphorylation	KPDSLKGSESAVDEL CCCCCCCCHHHHHHH	27.13	25159016
444	Phosphorylation	DSLKGSESAVDELKG CCCCCCHHHHHHHHH	34.98	25521595
455	Phosphorylation	ELKGILGTLNKSTSS HHHHHHHHCCCCCCC	24.58	29176673
459	Phosphorylation	ILGTLNKSTSSRSLK HHHHCCCCCCCCHHH	32.23	22817900
460	Phosphorylation	LGTLNKSTSSRSLKS HHHCCCCCCCCHHHH	32.12	23984901
461	Phosphorylation	GTLNKSTSSRSLKSL HHCCCCCCCCHHHHH	30.74	19060867
462	Phosphorylation	TLNKSTSSRSLKSLG HCCCCCCCCHHHHHC	26.44	17242355
464	Phosphorylation	NKSTSSRSLKSLGPE CCCCCCCHHHHHCCC	41.94	21082442
467	Phosphorylation	TSSRSLKSLGPENSE CCCCHHHHHCCCCCH	43.80	25521595
473	Phosphorylation	KSLGPENSETELERI HHHCCCCCHHHHHHH	44.21	25521595
475	Phosphorylation	LGPENSETELERILR HCCCCCHHHHHHHHH	45.77	30635358
487	Phosphorylation	ILRRRKLTAEADSSS HHHHCCCCHHCCCCC	26.03	25159016
492	Phosphorylation	KLTAEADSSSPTGIL CCCHHCCCCCCCEEE	39.50	26239621
493	Phosphorylation	LTAEADSSSPTGILA CCHHCCCCCCCEEEE	40.67	26239621
494	Phosphorylation	TAEADSSSPTGILAT CHHCCCCCCCEEEEC	30.36	27087446
496	Phosphorylation	EADSSSPTGILATSE HCCCCCCCEEEECCC	38.51	25159016
502	Phosphorylation	PTGILATSESKSMPV CCEEEECCCCCCCCC	33.98	30352176
504	Phosphorylation	GILATSESKSMPVLG EEEECCCCCCCCCEE	29.78	30352176
506	Phosphorylation	LATSESKSMPVLGSV EECCCCCCCCCEECH	37.28	25521595
507	Oxidation	ATSESKSMPVLGSVS ECCCCCCCCCEECHH	2.82	17242355
512	Phosphorylation	KSMPVLGSVSSVTKS CCCCCEECHHHHCHH	18.05	29176673
514	Phosphorylation	MPVLGSVSSVTKSAL CCCEECHHHHCHHHH	22.31	25159016
515	Phosphorylation	PVLGSVSSVTKSALN CCEECHHHHCHHHHC	31.48	25159016
517	Phosphorylation	LGSVSSVTKSALNKK EECHHHHCHHHHCCC	22.64	29176673
537	Phosphorylation	FNNPCPLTPEPGEGP CCCCCCCCCCCCCCC	15.68	26239621
550	Glutathionylation	GPRKLEGCTNPKVTF CCCCCCCCCCCCEEE	2.13	24333276
556	Phosphorylation	GCTNPKVTFQPPSKG CCCCCCEEECCCCCC	23.76	22871156
619	Phosphorylation	QPEYKEDSGGKTGET CCCEECCCCCCCCCC	51.00	20531401

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
101	S	Phosphorylation	Kinase	PAK1	O88643	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
101	S	Phosphorylation	-
Phosphorylated on Ser-101 and Ser-249 by PAK1 through a CDC42- and RAC1-dependent signaling pathway, which enhances its association with F-actin retrograde flow in filopodia and lamellipodia of axonal growth cones.
101	S	Phosphorylation	-
Phosphorylation on Ser-101 and Ser-249 is increased by netrin-1.
249	S	Phosphorylation	17242355
Phosphorylated on Ser-101 and Ser-249 by PAK1 through a CDC42- and RAC1-dependent signaling pathway, which enhances its association with F-actin retrograde flow in filopodia and lamellipodia of axonal growth cones.
249	S	Phosphorylation	17242355
Phosphorylation on Ser-101 and Ser-249 is increased by netrin-1.

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 SHOT1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SHOT1_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SHOT1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-4; SER-464 ANDSER-467, AND MASS SPECTROMETRY.	17242355 [Abstract]

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