SHOT1_HUMAN - dbPTM
SHOT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHOT1_HUMAN
UniProt AC A0MZ66
Protein Name Shootin-1 {ECO:0000312|HGNC:HGNC:29319}
Gene Name SHTN1 {ECO:0000312|HGNC:HGNC:29319}
Organism Homo sapiens (Human).
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. 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. 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. Involved in the accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the growth cone of primary hippocampal neurons..
Protein Sequence MNSSDEEKQLQLITSLKEQAIGEYEDLRAENQKTKEKCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHLEIEKTCRESAEALATKLNKENKTLKRISMLYMAKLGPDVITEEINIDDEDSTTDTDGAAETCVSVQCQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMSMIRKRSHPSGSGAKKEKATQPETTEEVTDLKRQAVEEMMDRIKKGVHLRPVNQTARPKTKPESSKGCESAVDELKGILGTLNKSTSSRSLKSLDPENSETELERILRRRKVTAEADSSSPTGILATSESKSMPVLGSVSSVTKTALNKKTLEAEFNSPSPPTPEPGEGPRKLEGCTSSKVTFQPPSSIGCRKKYIDGEKQAEPVVVLDPVSTHEPQTKDQVAEKDPTQHKEDEGEIQPENKEDSIENVRETDSSNC
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MNSSDEEK
-------CCCHHHHH
11.22-
3Phosphorylation-----MNSSDEEKQL
-----CCCHHHHHHH
37.5629116813
4Phosphorylation----MNSSDEEKQLQ
----CCCHHHHHHHH
44.0029116813
14PhosphorylationEKQLQLITSLKEQAI
HHHHHHHHHHHHHHH
36.2825159151
15PhosphorylationKQLQLITSLKEQAIG
HHHHHHHHHHHHHHH
30.3725159151
17NeddylationLQLITSLKEQAIGEY
HHHHHHHHHHHHHHH
47.7732015554
17UbiquitinationLQLITSLKEQAIGEY
HHHHHHHHHHHHHHH
47.7721906983
17 (in isoform 1)Ubiquitination-47.7721906983
17 (in isoform 2)Ubiquitination-47.7721906983
17 (in isoform 3)Ubiquitination-47.7721906983
17 (in isoform 4)Ubiquitination-47.7721906983
24PhosphorylationKEQAIGEYEDLRAEN
HHHHHHHHHHHHHHH
14.9921945579
24 (in isoform 3)Phosphorylation-14.9927642862
29UbiquitinationGEYEDLRAENQKTKE
HHHHHHHHHHHHHHH
27.6532015554
35AcetylationRAENQKTKEKCDKIR
HHHHHHHHHHHHHHH
63.3119829747
37AcetylationENQKTKEKCDKIRQE
HHHHHHHHHHHHHHH
49.6519829755
41PhosphorylationTKEKCDKIRQERDEA
HHHHHHHHHHHHHHH
3.3432142685
54 (in isoform 7)Ubiquitination-64.9121906983
73 (in isoform 7)Ubiquitination-10.4621906983
82PhosphorylationIEKTCRESAEALATK
HHHHHHHHHHHHHHH
16.4428985074
89UbiquitinationSAEALATKLNKENKT
HHHHHHHHHHHHCHH
44.4432015554
99UbiquitinationKENKTLKRISMLYMA
HHCHHHHHHHHHHHH
29.3530230243
101PhosphorylationNKTLKRISMLYMAKL
CHHHHHHHHHHHHHH
13.5322617229
104PhosphorylationLKRISMLYMAKLGPD
HHHHHHHHHHHHCCC
6.0830108239
109UbiquitinationMLYMAKLGPDVITEE
HHHHHHHCCCEEEEE
18.6932015554
111UbiquitinationYMAKLGPDVITEEIN
HHHHHCCCEEEEEEC
42.5230230243
112 (in isoform 7)Ubiquitination-7.0321906983
121UbiquitinationTEEINIDDEDSTTDT
EEEECCCCCCCCCCC
58.7830230243
1582-HydroxyisobutyrylationIVSVQEEKKILAIEL
HCCHHHHHHHHHEEH
44.34-
159UbiquitinationVSVQEEKKILAIELE
CCHHHHHHHHHEEHH
46.3530230243
169UbiquitinationAIELENLKSKLVEVI
HEEHHHHHHHHHHHH
58.0630230243
170UbiquitinationIELENLKSKLVEVIE
EEHHHHHHHHHHHHH
34.0930230243
171UbiquitinationELENLKSKLVEVIEE
EHHHHHHHHHHHHHH
55.7730230243
181UbiquitinationEVIEEVNKVKQEKTV
HHHHHHHHHHHHHHH
56.8630230243
187PhosphorylationNKVKQEKTVLNSEVL
HHHHHHHHHCCHHHH
29.4929978859
189PhosphorylationVKQEKTVLNSEVLEQ
HHHHHHHCCHHHHHH
7.6532142685
191PhosphorylationQEKTVLNSEVLEQRK
HHHHHCCHHHHHHHH
25.5629978859
204 (in isoform 7)Ubiquitination-59.4621906983
211UbiquitinationNRVSMLAVEEYEEMQ
CCCEEEEHHHHHHHH
5.1729967540
214PhosphorylationSMLAVEEYEEMQVNL
EEEEHHHHHHHHHHH
12.04-
214 (in isoform 3)Phosphorylation-12.0427642862
228UbiquitinationLELEKDLRKKAESFA
HHHHHHHHHHHHHHH
48.8730230243
229UbiquitinationELEKDLRKKAESFAQ
HHHHHHHHHHHHHHH
64.7330230243
230UbiquitinationLEKDLRKKAESFAQE
HHHHHHHHHHHHHHH
51.4530230243
233PhosphorylationDLRKKAESFAQEMFI
HHHHHHHHHHHHHHH
30.6427251275
249PhosphorylationQNKLKRQSHLLLQSS
HCHHHHHHHHHHHCC
21.8225159151
249 (in isoform 2)Phosphorylation-21.82-
255PhosphorylationQSHLLLQSSIPDQQL
HHHHHHHCCCCHHHH
30.1523403867
256PhosphorylationSHLLLQSSIPDQQLL
HHHHHHCCCCHHHHH
25.7723403867
263UbiquitinationSIPDQQLLKALDENA
CCCHHHHHHHHHHHH
2.3730230243
271UbiquitinationKALDENAKLTQQLEE
HHHHHHHHHHHHHHH
64.7429967540
275UbiquitinationENAKLTQQLEEERIQ
HHHHHHHHHHHHHHH
45.6829967540
288UbiquitinationIQHQQKVKELEEQLE
HHHHHHHHHHHHHHH
64.7130230243
323UbiquitinationDKKELELKYQNSEEK
HHHHHHHHHCCHHHH
35.1030230243
324PhosphorylationKKELELKYQNSEEKA
HHHHHHHHCCHHHHH
26.0823403867
332UbiquitinationQNSEEKARNLKHSVD
CCHHHHHHHHHHHHH
61.1433845483
335UbiquitinationEEKARNLKHSVDELQ
HHHHHHHHHHHHHHH
37.0729967540
337PhosphorylationKARNLKHSVDELQKR
HHHHHHHHHHHHHHH
29.6718452278
337 (in isoform 2)Phosphorylation-29.67-
346UbiquitinationDELQKRVNQSENSVP
HHHHHHHHHCCCCCC
43.6332015554
346 (in isoform 5)Ubiquitination-43.6321906983
348PhosphorylationLQKRVNQSENSVPPP
HHHHHHHCCCCCCCC
33.2827174698
351PhosphorylationRVNQSENSVPPPPPP
HHHHCCCCCCCCCCC
31.7627174698
372PhosphorylationPPPNPIRSLMSMIRK
CCCCHHHHHHHHHHH
29.1927174698
375PhosphorylationNPIRSLMSMIRKRSH
CHHHHHHHHHHHCCC
19.1527422710
376 (in isoform 6)Ubiquitination-1.8221906983
381PhosphorylationMSMIRKRSHPSGSGA
HHHHHHCCCCCCCCC
42.6727282143
384PhosphorylationIRKRSHPSGSGAKKE
HHHCCCCCCCCCCCC
39.9226091039
386PhosphorylationKRSHPSGSGAKKEKA
HCCCCCCCCCCCCCC
39.6623312004
390UbiquitinationPSGSGAKKEKATQPE
CCCCCCCCCCCCCCC
65.0129967540
392UbiquitinationGSGAKKEKATQPETT
CCCCCCCCCCCCCCH
66.6633845483
394PhosphorylationGAKKEKATQPETTEE
CCCCCCCCCCCCHHH
56.5821815630
398PhosphorylationEKATQPETTEEVTDL
CCCCCCCCHHHHHHH
46.3120068231
398UbiquitinationEKATQPETTEEVTDL
CCCCCCCCHHHHHHH
46.3127667366
398 (in isoform 2)Phosphorylation-46.31-
399PhosphorylationKATQPETTEEVTDLK
CCCCCCCHHHHHHHH
28.6120068231
399 (in isoform 2)Phosphorylation-28.61-
403PhosphorylationPETTEEVTDLKRQAV
CCCHHHHHHHHHHHH
38.6027135362
404PhosphorylationETTEEVTDLKRQAVE
CCHHHHHHHHHHHHH
56.2033259812
4062-HydroxyisobutyrylationTEEVTDLKRQAVEEM
HHHHHHHHHHHHHHH
45.32-
406AcetylationTEEVTDLKRQAVEEM
HHHHHHHHHHHHHHH
45.3224430961
406MethylationTEEVTDLKRQAVEEM
HHHHHHHHHHHHHHH
45.3224430961
406UbiquitinationTEEVTDLKRQAVEEM
HHHHHHHHHHHHHHH
45.3221906983
406 (in isoform 1)Ubiquitination-45.3221906983
406 (in isoform 2)Ubiquitination-45.3221906983
406 (in isoform 3)Ubiquitination-45.3221906983
406 (in isoform 4)Ubiquitination-45.3221906983
406 (in isoform 5)Ubiquitination-45.3221906983
416MethylationAVEEMMDRIKKGVHL
HHHHHHHHHHCCCCC
25.40115916949
425UbiquitinationKKGVHLRPVNQTARP
HCCCCCCCCCCCCCC
35.4529967540
425 (in isoform 5)Ubiquitination-35.4521906983
433PhosphorylationVNQTARPKTKPESSK
CCCCCCCCCCCCCCC
64.7232142685
436 (in isoform 6)Ubiquitination-52.5121906983
439PhosphorylationPKTKPESSKGCESAV
CCCCCCCCCCHHHHH
31.2521964256
441PhosphorylationTKPESSKGCESAVDE
CCCCCCCCHHHHHHH
23.5232142685
446PhosphorylationSKGCESAVDELKGIL
CCCHHHHHHHHHHHH
9.0532142685
450UbiquitinationESAVDELKGILGTLN
HHHHHHHHHHHHHCC
41.6929967540
455PhosphorylationELKGILGTLNKSTSS
HHHHHHHHCCCCCCC
24.5823312004
455 (in isoform 6)Ubiquitination-24.5821906983
458UbiquitinationGILGTLNKSTSSRSL
HHHHHCCCCCCCCCH
59.2227667366
459PhosphorylationILGTLNKSTSSRSLK
HHHHCCCCCCCCCHH
32.2328857561
460PhosphorylationLGTLNKSTSSRSLKS
HHHCCCCCCCCCHHH
32.1223312004
461PhosphorylationGTLNKSTSSRSLKSL
HHCCCCCCCCCHHHC
30.7423312004
462PhosphorylationTLNKSTSSRSLKSLD
HCCCCCCCCCHHHCC
26.4423312004
464PhosphorylationNKSTSSRSLKSLDPE
CCCCCCCCHHHCCCC
41.9426657352
464 (in isoform 5)Ubiquitination-41.9421906983
466UbiquitinationSTSSRSLKSLDPENS
CCCCCCHHHCCCCCC
50.6621906983
466 (in isoform 1)Ubiquitination-50.6621906983
466 (in isoform 3)Ubiquitination-50.6621906983
466 (in isoform 4)Ubiquitination-50.6621906983
467PhosphorylationTSSRSLKSLDPENSE
CCCCCHHHCCCCCCH
43.2129255136
473PhosphorylationKSLDPENSETELERI
HHCCCCCCHHHHHHH
44.2125159151
475PhosphorylationLDPENSETELERILR
CCCCCCHHHHHHHHH
45.7730206219
485UbiquitinationERILRRRKVTAEADS
HHHHHHCCCCCCCCC
41.9721906983
485 (in isoform 1)Ubiquitination-41.9721906983
485 (in isoform 3)Ubiquitination-41.9721906983
485 (in isoform 4)Ubiquitination-41.9721906983
487PhosphorylationILRRRKVTAEADSSS
HHHHCCCCCCCCCCC
23.0927273156
492PhosphorylationKVTAEADSSSPTGIL
CCCCCCCCCCCCEEE
39.5030266825
493PhosphorylationVTAEADSSSPTGILA
CCCCCCCCCCCEEEE
40.6730266825
493 (in isoform 3)Phosphorylation-40.6721406692
494PhosphorylationTAEADSSSPTGILAT
CCCCCCCCCCEEEEE
30.3619664994
494 (in isoform 6)Ubiquitination-30.3621906983
496PhosphorylationEADSSSPTGILATSE
CCCCCCCCEEEEECC
38.5130266825
501PhosphorylationSPTGILATSESKSMP
CCCEEEEECCCCCCC
29.5830175587
502PhosphorylationPTGILATSESKSMPV
CCEEEEECCCCCCCC
33.9823403867
504PhosphorylationGILATSESKSMPVLG
EEEEECCCCCCCCEE
29.7823403867
506PhosphorylationLATSESKSMPVLGSV
EEECCCCCCCCEECH
37.2829255136
506 (in isoform 3)Phosphorylation-37.2821406692
512PhosphorylationKSMPVLGSVSSVTKT
CCCCCEECHHHHHHH
18.0523927012
514PhosphorylationMPVLGSVSSVTKTAL
CCCEECHHHHHHHHH
22.3125159151
515PhosphorylationPVLGSVSSVTKTALN
CCEECHHHHHHHHHC
31.4823927012
517PhosphorylationLGSVSSVTKTALNKK
EECHHHHHHHHHCCC
25.3223927012
519PhosphorylationSVSSVTKTALNKKTL
CHHHHHHHHHCCCCC
27.3222210691
524UbiquitinationTKTALNKKTLEAEFN
HHHHHCCCCCEECCC
58.2121906983
524 (in isoform 1)Ubiquitination-58.2121906983
524 (in isoform 3)Ubiquitination-58.2121906983
524 (in isoform 4)Ubiquitination-58.2121906983
525PhosphorylationKTALNKKTLEAEFNS
HHHHCCCCCEECCCC
31.2921815630
532PhosphorylationTLEAEFNSPSPPTPE
CCEECCCCCCCCCCC
31.8825159151
534PhosphorylationEAEFNSPSPPTPEPG
EECCCCCCCCCCCCC
43.2530278072
537PhosphorylationFNSPSPPTPEPGEGP
CCCCCCCCCCCCCCC
43.6028355574
556PhosphorylationGCTSSKVTFQPPSSI
CCCCCCEEECCCCCC
21.9323312004
556 (in isoform 5)Ubiquitination-21.9321906983
561PhosphorylationKVTFQPPSSIGCRKK
CEEECCCCCCCCCHH
41.0725159151
562PhosphorylationVTFQPPSSIGCRKKY
EEECCCCCCCCCHHC
28.8625159151
586PhosphorylationVVVLDPVSTHEPQTK
EEEECCCCCCCCCCH
29.4528348404
586 (in isoform 6)Ubiquitination-29.4521906983
587PhosphorylationVVLDPVSTHEPQTKD
EEECCCCCCCCCCHH
30.4128348404
599AcetylationTKDQVAEKDPTQHKE
CHHHHCCCCCCCCCC
60.3126051181
616UbiquitinationGEIQPENKEDSIENV
CCCCCCCHHHHHHHH
62.332190698
616 (in isoform 1)Ubiquitination-62.3321906983
619PhosphorylationQPENKEDSIENVRET
CCCCHHHHHHHHHHH
32.6625159151
626PhosphorylationSIENVRETDSSNC--
HHHHHHHHCCCCC--
30.5329449344
628PhosphorylationENVRETDSSNC----
HHHHHHCCCCC----
30.7625627689
629PhosphorylationNVRETDSSNC-----
HHHHHCCCCC-----
45.0525627689

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
101SPhosphorylationKinasePAK1Q13153
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
101SPhosphorylation

-
101SPhosphorylation

-
249SPhosphorylation

20068231
249SPhosphorylation

20068231

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBXN1_HUMANUBXN1physical
22939629
UNK_HUMANUNKphysical
22939629
CAP1_HUMANCAP1physical
22863883
FAS_HUMANFASNphysical
22863883
ENPL_HUMANHSP90B1physical
22863883
KCD12_HUMANKCTD12physical
22863883
TPM4_HUMANTPM4physical
22863883
SHOT1_HUMANKIAA1598physical
25416956

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 SHOT1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494 AND THR-496, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-506; SER-515;SER-532 AND THR-537, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-537, AND MASSSPECTROMETRY.

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