SPART_HUMAN - dbPTM
SPART_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPART_HUMAN
UniProt AC Q8N0X7
Protein Name Spartin {ECO:0000305}
Gene Name SPART {ECO:0000312|HGNC:HGNC:18514}
Organism Homo sapiens (Human).
Sequence Length 666
Subcellular Localization Cytoplasm . Midbody . Transiently associated with endosomes (PubMed:19580544). Colocalized with IST1 to the ends of Flemming bodies during cytokinesis (PubMed:20719964).
Protein Description May be implicated in endosomal trafficking, or microtubule dynamics, or both. Participates in cytokinesis. [PubMed: 20719964]
Protein Sequence MEQEPQNGEPAEIKIIREAYKKAFLFVNKGLNTDELGQKEEAKNYYKQGIGHLLRGISISSKESEHTGPGWESARQMQQKMKETLQNVRTRLEILEKGLATSLQNDLQEVPKLYPEFPPKDMCEKLPEPQSFSSAPQHAEVNGNTSTPSAGAVAAPASLSLPSQSCPAEAPPAYTPQAAEGHYTVSYGTDSGEFSSVGEEFYRNHSQPPPLETLGLDADELILIPNGVQIFFVNPAGEVSAPSYPGYLRIVRFLDNSLDTVLNRPPGFLQVCDWLYPLVPDRSPVLKCTAGAYMFPDTMLQAAGCFVGVVLSSELPEDDRELFEDLLRQMSDLRLQANWNRAEEENEFQIPGRTRPSSDQLKEASGTDVKQLDQGNKDVRHKGKRGKRAKDTSSEEVNLSHIVPCEPVPEEKPKELPEWSEKVAHNILSGASWVSWGLVKGAEITGKAIQKGASKLRERIQPEEKPVEVSPAVTKGLYIAKQATGGAAKVSQFLVDGVCTVANCVGKELAPHVKKHGSKLVPESLKKDKDGKSPLDGAMVVAASSVQGFSTVWQGLECAAKCIVNNVSAETVQTVRYKYGYNAGEATHHAVDSAVNVGVTAYNINNIGIKAMVKKTATQTGHTLLEDYQIVDNSQRENQEGAANVNVRGEKDEQTKEVKEAKKKDK
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-------MEQEPQNG
-------CCCCCCCC
22814378
22AcetylationIIREAYKKAFLFVNK
HHHHHHHHHHHHHCC
26051181
29AcetylationKAFLFVNKGLNTDEL
HHHHHHCCCCCHHHH
26051181
29UbiquitinationKAFLFVNKGLNTDEL
HHHHHHCCCCCHHHH
21906983
39UbiquitinationNTDELGQKEEAKNYY
CHHHHCCHHHHHHHH
-
45PhosphorylationQKEEAKNYYKQGIGH
CHHHHHHHHHHHHHH
-
46PhosphorylationKEEAKNYYKQGIGHL
HHHHHHHHHHHHHHH
22817900
47UbiquitinationEEAKNYYKQGIGHLL
HHHHHHHHHHHHHHH
21906983
58PhosphorylationGHLLRGISISSKESE
HHHHHCCCCCCCCCC
26699800
60PhosphorylationLLRGISISSKESEHT
HHHCCCCCCCCCCCC
26699800
62UbiquitinationRGISISSKESEHTGP
HCCCCCCCCCCCCCC
21890473
82UbiquitinationRQMQQKMKETLQNVR
HHHHHHHHHHHHHHH
21906983
97UbiquitinationTRLEILEKGLATSLQ
HHHHHHHHHHHHHHH
21906983
97 (in isoform 1)Ubiquitination-22053931
101PhosphorylationILEKGLATSLQNDLQ
HHHHHHHHHHHHHHH
23403867
102PhosphorylationLEKGLATSLQNDLQE
HHHHHHHHHHHHHHH
23403867
112UbiquitinationNDLQEVPKLYPEFPP
HHHHHHHHHCCCCCC
-
114PhosphorylationLQEVPKLYPEFPPKD
HHHHHHHCCCCCCHH
25159151
287UbiquitinationPDRSPVLKCTAGAYM
CCCCCCEECCCCCCC
-
334MethylationLRQMSDLRLQANWNR
HHHHHHHHHHHCHHH
115917573
354PhosphorylationEFQIPGRTRPSSDQL
CCCCCCCCCCCHHHH
23403867
357PhosphorylationIPGRTRPSSDQLKEA
CCCCCCCCHHHHHHH
30108239
358PhosphorylationPGRTRPSSDQLKEAS
CCCCCCCHHHHHHHC
23403867
362UbiquitinationRPSSDQLKEASGTDV
CCCHHHHHHHCCCCH
21906983
362MethylationRPSSDQLKEASGTDV
CCCHHHHHHHCCCCH
-
362 (in isoform 1)Ubiquitination-22053931
365PhosphorylationSDQLKEASGTDVKQL
HHHHHHHCCCCHHHH
30108239
367PhosphorylationQLKEASGTDVKQLDQ
HHHHHCCCCHHHHHC
30108239
370 (in isoform 1)Ubiquitination-22053931
370UbiquitinationEASGTDVKQLDQGNK
HHCCCCHHHHHCCCC
21906983
370MethylationEASGTDVKQLDQGNK
HHCCCCHHHHHCCCC
-
377UbiquitinationKQLDQGNKDVRHKGK
HHHHCCCCCCCCCCC
21906983
382MethylationGNKDVRHKGKRGKRA
CCCCCCCCCCCCCCC
-
390UbiquitinationGKRGKRAKDTSSEEV
CCCCCCCCCCCCCCC
-
392PhosphorylationRGKRAKDTSSEEVNL
CCCCCCCCCCCCCCH
23403867
393PhosphorylationGKRAKDTSSEEVNLS
CCCCCCCCCCCCCHH
23401153
394PhosphorylationKRAKDTSSEEVNLSH
CCCCCCCCCCCCHHH
23403867
400PhosphorylationSSEEVNLSHIVPCEP
CCCCCCHHHEEECCC
23403867
412UbiquitinationCEPVPEEKPKELPEW
CCCCCCCCCCCCCHH
-
414UbiquitinationPVPEEKPKELPEWSE
CCCCCCCCCCCHHHH
-
422UbiquitinationELPEWSEKVAHNILS
CCCHHHHHHHHHHHC
-
440UbiquitinationWVSWGLVKGAEITGK
CCCHHCCCCCCHHHH
21906983
447AcetylationKGAEITGKAIQKGAS
CCCCHHHHHHHHHHH
25953088
447UbiquitinationKGAEITGKAIQKGAS
CCCCHHHHHHHHHHH
21906983
451UbiquitinationITGKAIQKGASKLRE
HHHHHHHHHHHHHHH
-
455UbiquitinationAIQKGASKLRERIQP
HHHHHHHHHHHHCCC
-
465AcetylationERIQPEEKPVEVSPA
HHCCCCCCCCCCCHH
26051181
465UbiquitinationERIQPEEKPVEVSPA
HHCCCCCCCCCCCHH
21906983
470PhosphorylationEEKPVEVSPAVTKGL
CCCCCCCCHHHHCCE
29255136
474PhosphorylationVEVSPAVTKGLYIAK
CCCCHHHHCCEEEEH
29255136
474O-linked_GlycosylationVEVSPAVTKGLYIAK
CCCCHHHHCCEEEEH
30059200
475UbiquitinationEVSPAVTKGLYIAKQ
CCCHHHHCCEEEEHH
21906983
481UbiquitinationTKGLYIAKQATGGAA
HCCEEEEHHHCCCCC
-
489AcetylationQATGGAAKVSQFLVD
HHCCCCCHHHHHHHC
7712387
489UbiquitinationQATGGAAKVSQFLVD
HHCCCCCHHHHHHHC
-
499S-nitrosocysteineQFLVDGVCTVANCVG
HHHHCCCCHHHHHCC
-
504S-nitrosocysteineGVCTVANCVGKELAP
CCCHHHHHCCHHHHH
-
507UbiquitinationTVANCVGKELAPHVK
HHHHHCCHHHHHHHH
21906983
514UbiquitinationKELAPHVKKHGSKLV
HHHHHHHHHHCCCCC
-
515UbiquitinationELAPHVKKHGSKLVP
HHHHHHHHHCCCCCC
-
518PhosphorylationPHVKKHGSKLVPESL
HHHHHHCCCCCCHHH
28857561
519UbiquitinationHVKKHGSKLVPESLK
HHHHHCCCCCCHHHC
-
524PhosphorylationGSKLVPESLKKDKDG
CCCCCCHHHCCCCCC
25159151
526UbiquitinationKLVPESLKKDKDGKS
CCCCHHHCCCCCCCC
-
527UbiquitinationLVPESLKKDKDGKSP
CCCHHHCCCCCCCCC
-
529UbiquitinationPESLKKDKDGKSPLD
CHHHCCCCCCCCCCC
-
532UbiquitinationLKKDKDGKSPLDGAM
HCCCCCCCCCCCCCE
-
578UbiquitinationTVQTVRYKYGYNAGE
HEEEEHHHHCCCCCH
21906983
578SumoylationTVQTVRYKYGYNAGE
HEEEEHHHHCCCCCH
-
578 (in isoform 1)Ubiquitination-22053931
602PhosphorylationVNVGVTAYNINNIGI
CCCCCEEEEECCCCH
27642862
610UbiquitinationNINNIGIKAMVKKTA
EECCCCHHHHEEECC
-
615 (in isoform 1)Ubiquitination-22053931
615UbiquitinationGIKAMVKKTATQTGH
CHHHHEEECCCCCCC
21906983
616PhosphorylationIKAMVKKTATQTGHT
HHHHEEECCCCCCCC
27642862
618PhosphorylationAMVKKTATQTGHTLL
HHEEECCCCCCCCHH
27642862
620PhosphorylationVKKTATQTGHTLLED
EEECCCCCCCCHHEE
28555341
628PhosphorylationGHTLLEDYQIVDNSQ
CCCHHEEEEECCCCH
25884760
651UbiquitinationNVNVRGEKDEQTKEV
CCCCCCCCHHHHHHH
-
655PhosphorylationRGEKDEQTKEVKEAK
CCCCHHHHHHHHHHH
23025827
656UbiquitinationGEKDEQTKEVKEAKK
CCCHHHHHHHHHHHH
-

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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
-KUbiquitinationE3 ubiquitin ligaseWWP1Q9H0M0
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPART_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 SPART_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBA1A_HUMANTUBA1Aphysical
16945107
GRP78_HUMANHSPA5physical
19765186
GRP75_HUMANHSPA9physical
19765186
CH60_HUMANHSPD1physical
19765186
ITCH_HUMANITCHphysical
19765186
WWP1_HUMANWWP1physical
19765186
DYHC1_HUMANDYNC1H1physical
19765186
KINH_HUMANKIF5Bphysical
19765186
KLC2_HUMANKLC2physical
19765186
VIME_HUMANVIMphysical
19765186
COPA_HUMANCOPAphysical
19765186
CLH1_HUMANCLTCphysical
19765186
LMNB1_HUMANLMNB1physical
19765186
IMB1_HUMANKPNB1physical
19765186
NUCL_HUMANNCLphysical
19765186
AIFM1_HUMANAIFM1physical
19765186
ECHA_HUMANHADHAphysical
19765186
ACSL4_HUMANACSL4physical
19765186
ACSL3_HUMANACSL3physical
19765186
ITCH_HUMANITCHphysical
19580544
WWP1_HUMANWWP1physical
19580544
ITCH_HUMANITCHphysical
20504295
WWP1_HUMANWWP1physical
19307600
WWP2_HUMANWWP2physical
19307600
ITCH_HUMANITCHphysical
19307600
SMUF1_HUMANSMURF1physical
19307600
SMUF2_HUMANSMURF2physical
19307600
PLIN3_HUMANPLIN3physical
19307600
EPS15_HUMANEPS15physical
16036216
A4_HUMANAPPphysical
21832049
POLK_HUMANPOLKphysical
28514442
SMUF1_HUMANSMURF1physical
28514442
ITCH_HUMANITCHphysical
28514442
WWP1_HUMANWWP1physical
28514442
HECW2_HUMANHECW2physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPART_HUMAN

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Related Literatures of Post-Translational Modification

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