SPDLY_HUMAN - dbPTM
SPDLY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPDLY_HUMAN
UniProt AC Q96EA4
Protein Name Protein Spindly {ECO:0000255|HAMAP-Rule:MF_03041}
Gene Name SPDL1 {ECO:0000255|HAMAP-Rule:MF_03041}
Organism Homo sapiens (Human).
Sequence Length 605
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Nucleus. Cytoplasm, cytoskeleton, spindle pole. Localizes to the nucleus in interphase and to the kinetochore in early prometaphase. Relocalizes
Protein Description Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Also required for correct spindle orientation. Does not appear to be required for the removal of spindle assembly checkpoint (SAC) proteins from the kinetochore upon bipolar spindle attachment. [PubMed: 17576797]
Protein Sequence MEADIITNLRCRLKEAEEERLKAAQYGLQLVESQNELQNQLDKCRNEMMTMTESYEQEKYTLQREVELKSRMLESLSCECEAIKQQQKMHLEKLEEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQMKGSQTEFEQQERLLAMLEQKNGEIKHLLGEIRNLEKFKNLYDSMESKPSVDSGTLEDNTYYTDLLQMKLDNLNKEIESTKGELSIQRMKALFESQRALDIERKLFANERCLQLSESENMKLRAKLDELKLKYEPEETVEVPVLKKRREVLPVDITTAKDACVNNSALGGEVYRLPPQKEETQSCPNSLEDNNLQLEKSVSIYTPVVSLSPHKNLPVDMQLKKEKKCVKLIGVPADAEALSERSGNTPNSPRLAAESKLQTEVKEGKETSSKLEKETCKKLHPILYVSSKSTPETQCPQQ
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-------MEADIITN
-------CCCHHHHH		9.6322814378
126PhosphorylationELDEARLSEKQLKHQ
HHHHHHCCHHHHHHH		36.8827762562
145PhosphorylationKELLSCKSEELRVMS
HHHHHCCHHHHHHHH		40.4027251275
154MethylationELRVMSERVQESMSS
HHHHHHHHHHHHCCH		28.28-
178PhosphorylationTEMESMKTTLKEEVN
HHHHHHHHHHHHHHH		28.8122210691
179PhosphorylationEMESMKTTLKEEVNE
HHHHHHHHHHHHHHH		30.2522210691
221PhosphorylationEREKEAVSYYNALEK
HHHHHHHHHHHHHHH		29.0223828894
228UbiquitinationSYYNALEKARVANQD
HHHHHHHHHHHHCCC		42.2029967540
256PhosphorylationDPNSKGNSLFAEVED
CCCCCCCCCHHHHHH		33.2728555341
260UbiquitinationKGNSLFAEVEDRRAA
CCCCCHHHHHHHHHH		38.8233845483
279PhosphorylationLISMKVKYQSLKKQN
HHHHHHHHHHHHHCC		13.3024043423
281PhosphorylationSMKVKYQSLKKQNVF
HHHHHHHHHHHCCCC		38.7824043423
303UbiquitinationMKLQIATLLQMKGSQ
HHHHHHHHHHHCCCC		2.0132015554
315UbiquitinationGSQTEFEQQERLLAM
CCCCHHHHHHHHHHH		56.6133845483
331UbiquitinationEQKNGEIKHLLGEIR
HHHCHHHHHHHHHHH		24.7333845483
347PhosphorylationLEKFKNLYDSMESKP
HHHHHHHHHHCCCCC		18.5025159151
355PhosphorylationDSMESKPSVDSGTLE
HHCCCCCCCCCCCCC		42.1430576142
360PhosphorylationKPSVDSGTLEDNTYY
CCCCCCCCCCCCCHH		30.8130576142
365PhosphorylationSGTLEDNTYYTDLLQ
CCCCCCCCHHHHHHH		30.1730576142
366PhosphorylationGTLEDNTYYTDLLQM
CCCCCCCHHHHHHHH		15.6027642862
367PhosphorylationTLEDNTYYTDLLQMK
CCCCCCHHHHHHHHH		7.5527642862
368PhosphorylationLEDNTYYTDLLQMKL
CCCCCHHHHHHHHHH		15.1229978859
374UbiquitinationYTDLLQMKLDNLNKE
HHHHHHHHHHHHHHH		39.4632015554
386UbiquitinationNKEIESTKGELSIQR
HHHHHHCCCHHHHHH		60.7233845483
390PhosphorylationESTKGELSIQRMKAL
HHCCCHHHHHHHHHH		16.6324719451
405 (in isoform 2)Phosphorylation-39.4521406692
407 (in isoform 2)Phosphorylation-43.3521406692
409UbiquitinationRALDIERKLFANERC
HHHHHHHHHHHCHHH		34.8629967540
410 (in isoform 2)Phosphorylation-6.5021406692
414 (in isoform 2)Phosphorylation-41.1421406692
416 (in isoform 2)Phosphorylation-2.0121406692
461PhosphorylationEVLPVDITTAKDACV
CCCCCCCCCCHHHHC		19.08-
471PhosphorylationKDACVNNSALGGEVY
HHHHCCCCCCCCCEE		21.4821815630
484PhosphorylationVYRLPPQKEETQSCP
EEECCCCCCCCCCCC		64.3933259812
487PhosphorylationLPPQKEETQSCPNSL
CCCCCCCCCCCCCCC		27.2017525332
489PhosphorylationPQKEETQSCPNSLED
CCCCCCCCCCCCCCC		38.6725627689
492UbiquitinationEETQSCPNSLEDNNL
CCCCCCCCCCCCCCC		64.6532015554
493PhosphorylationETQSCPNSLEDNNLQ
CCCCCCCCCCCCCCC		20.4825159151
504PhosphorylationNNLQLEKSVSIYTPV
CCCCEEEEEEEEECC		16.2428450419
506PhosphorylationLQLEKSVSIYTPVVS
CCEEEEEEEEECCEE		19.5728450419
508PhosphorylationLEKSVSIYTPVVSLS
EEEEEEEEECCEECC		9.4828450419
509PhosphorylationEKSVSIYTPVVSLSP
EEEEEEEECCEECCC		14.1328450419
513PhosphorylationSIYTPVVSLSPHKNL
EEEECCEECCCCCCC		24.3022617229
515PhosphorylationYTPVVSLSPHKNLPV
EECCEECCCCCCCCC		19.9022617229
534AcetylationKKEKKCVKLIGVPAD
CCCCCCEEECCCCCC		43.8025953088
546PhosphorylationPADAEALSERSGNTP
CCCHHHHHHHCCCCC		37.7021815630
549PhosphorylationAEALSERSGNTPNSP
HHHHHHHCCCCCCCH		32.1322199227
552PhosphorylationLSERSGNTPNSPRLA
HHHHCCCCCCCHHHH		27.6323663014
555PhosphorylationRSGNTPNSPRLAAES
HCCCCCCCHHHHHHH		16.7625159151
562PhosphorylationSPRLAAESKLQTEVK
CHHHHHHHHHHHHHH		33.6626074081
563UbiquitinationPRLAAESKLQTEVKE
HHHHHHHHHHHHHHC		35.8032015554
566PhosphorylationAAESKLQTEVKEGKE
HHHHHHHHHHHCCCC		53.86-
593PhosphorylationLHPILYVSSKSTPET
HCCEEEECCCCCCCC		20.6322210691
594PhosphorylationHPILYVSSKSTPETQ
CCEEEECCCCCCCCC		22.1522210691
600PhosphorylationSSKSTPETQCPQQ--
CCCCCCCCCCCCC--		36.35-
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

Oops, there are no upstream regulatory protein records of SPDLY_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
48Kubiquitylation

30258100
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 SPDLY_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GPS2_HUMANGPS2physical
16169070
CE126_HUMANKIAA1377physical
16169070
YLPM1_HUMANYLPM1physical
22939629
NEK9_HUMANNEK9physical
22863883
SPDLY_HUMANSPDL1physical
25416956
DAAF4_HUMANDYX1C1physical
25416956
PPR18_HUMANPPP1R18physical
25416956
RTP5_HUMANRTP5physical
25416956
SYHC_HUMANHARSphysical
26344197
PSDE_HUMANPSMD14physical
26344197
RS5_HUMANRPS5physical
26344197
UBXN1_HUMANUBXN1physical
26344197
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 SPDLY_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555, AND MASSSPECTROMETRY.
"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 SER-515, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASSSPECTROMETRY.

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