SPIR1_HUMAN - dbPTM
SPIR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPIR1_HUMAN
UniProt AC Q08AE8
Protein Name Protein spire homolog 1
Gene Name SPIRE1 {ECO:0000312|EMBL:AAI25207.1}
Organism Homo sapiens (Human).
Sequence Length 756
Subcellular Localization Cytoplasm, cytoskeleton . Cytoplasm, perinuclear region . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Detected at the cleavage furrow during asymmetric
Protein Description Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for asymmetric spindle positioning and asymmetric cell division during meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis..
Protein Sequence MAQAAGPAGGGEPRTEAVGGEGPREPGAAGGAAGGSRDALSLEEILRLYNQPINEEQAWAVCYQCCGSLRAAARRRQPRHRVRSAAQIRVWRDGAVTLAPAADDAGEPPPVAGKLGYSQCMETEVIESLGIIIYKALDYGLKENEERELSPPLEQLIDHMANTVEADGSNDEGYEAAEEGLGDEDEKRKISAIRSYRDVMKLCAAHLPTESDAPNHYQAVCRALFAETMELHTFLTKIKSAKENLKKIQEMEKSDESSTDLEELKNADWARFWVQVMRDLRNGVKLKKVQERQYNPLPIEYQLTPYEMLMDDIRCKRYTLRKVMVNGDIPPRLKKSAHEIILDFIRSRPPLNPVSARKLKPTPPRPRSLHERILEEIKAERKLRPVSPEEIRRSRLAMRPLSMSYSFDLSDVTTPESTKNLVESSMVNGGLTSQTKENGLSTSQQVPAQRKKLLRAPTLAELDSSESEEETLHKSTSSSSVSPSFPEEPVLEAVSTRKKPPKFLPISSTPQPERRQPPQRRHSIEKETPTNVRQFLPPSRQSSRSLEEFCYPVECLALTVEEVMHIRQVLVKAELEKYQQYKDIYTALKKGKLCFCCRTRRFSFFTWSYTCQFCKRPVCSQCCKKMRLPSKPYSTLPIFSLGPSALQRGESSMRSEKPSTAHHRPLRSIARFSSKSKSMDKSDEELQFPKELMEDWSTMEVCVDCKKFISEIISSSRRSLVLANKRARLKRKTQSFYMSSPGPSEYCPSERTISEI
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
2Acetylation------MAQAAGPAG
------CCCCCCCCC
14.0222814378
15PhosphorylationAGGGEPRTEAVGGEG
CCCCCCCCCCCCCCC
38.7224247654
15 (in isoform 3)Phosphorylation-38.7222210691
15 (in isoform 4)Phosphorylation-38.7222210691
41PhosphorylationGGSRDALSLEEILRL
CCCCCCCCHHHHHHH
35.1429214152
84PhosphorylationQPRHRVRSAAQIRVW
CCCHHHHHHHEEEEE
25.71-
97PhosphorylationVWRDGAVTLAPAADD
EECCCCEEEEECCCC
19.3727461979
122UbiquitinationLGYSQCMETEVIESL
CCCCHHHHHHHHHHH
49.8232015554
169PhosphorylationNTVEADGSNDEGYEA
HHCCCCCCCHHHHHH
41.4727422710
174PhosphorylationDGSNDEGYEAAEEGL
CCCCHHHHHHHHHCC
10.5927642862
209PhosphorylationLCAAHLPTESDAPNH
HHHHHCCCCCCCCCH
55.2526356563
211PhosphorylationAAHLPTESDAPNHYQ
HHHCCCCCCCCCHHH
41.3626356563
217PhosphorylationESDAPNHYQAVCRAL
CCCCCCHHHHHHHHH
12.5726356563
228PhosphorylationCRALFAETMELHTFL
HHHHHHHHHHHHHHH
16.7122798277
228 (in isoform 3)Phosphorylation-16.7125849741
228 (in isoform 4)Phosphorylation-16.7125849741
235 (in isoform 3)Phosphorylation-5.1128348404
235 (in isoform 4)Phosphorylation-5.1128348404
240 (in isoform 3)Phosphorylation-48.3128348404
240 (in isoform 4)Phosphorylation-48.3128348404
241 (in isoform 3)Phosphorylation-20.4121815630
241 (in isoform 4)Phosphorylation-20.4121815630
242UbiquitinationLTKIKSAKENLKKIQ
HHHHHHHHHHHHHHH
54.9832015554
244 (in isoform 3)Phosphorylation-57.35-
244 (in isoform 4)Phosphorylation-57.35-
246AcetylationKSAKENLKKIQEMEK
HHHHHHHHHHHHHHH
60.45133835
247AcetylationSAKENLKKIQEMEKS
HHHHHHHHHHHHHHC
53.43133831
257PhosphorylationEMEKSDESSTDLEEL
HHHHCCCCCCCHHHH
43.4525627689
267PhosphorylationDLEELKNADWARFWV
CHHHHHCHHHHHHHH
16.4932142685
267 (in isoform 5)Phosphorylation-16.4925849741
274 (in isoform 5)Phosphorylation-2.5628348404
279 (in isoform 5)Phosphorylation-31.7028348404
280 (in isoform 5)Phosphorylation-3.0221815630
283 (in isoform 5)Phosphorylation-16.11-
319PhosphorylationDIRCKRYTLRKVMVN
HHHCCCCEECHHHHC
24.9124719451
333PhosphorylationNGDIPPRLKKSAHEI
CCCCCHHHCHHHHHH
11.4733259812
336PhosphorylationIPPRLKKSAHEIILD
CCHHHCHHHHHHHHH
33.0227251275
355PhosphorylationRPPLNPVSARKLKPT
CCCCCCCCCCCCCCC
24.5028555341
362PhosphorylationSARKLKPTPPRPRSL
CCCCCCCCCCCCCCH
44.3223312004
375PhosphorylationSLHERILEEIKAERK
CHHHHHHHHHHHHHC
56.1332142685
387PhosphorylationERKLRPVSPEEIRRS
HHCCCCCCHHHHHHH
29.3129255136
387 (in isoform 2)Phosphorylation-29.3125849741
389PhosphorylationKLRPVSPEEIRRSRL
CCCCCCHHHHHHHHH
59.5632645325
394 (in isoform 2)Phosphorylation-23.0728348404
399 (in isoform 2)Phosphorylation-24.3328348404
400 (in isoform 2)Phosphorylation-18.7221815630
403 (in isoform 2)Phosphorylation-6.01-
406PhosphorylationRPLSMSYSFDLSDVT
CCCCCCEEECHHHCC
12.65-
424PhosphorylationSTKNLVESSMVNGGL
HHHHHHHHHHHCCCC
19.0928122231
425PhosphorylationTKNLVESSMVNGGLT
HHHHHHHHHHCCCCC
17.1628122231
432PhosphorylationSMVNGGLTSQTKENG
HHHCCCCCCCCCCCC
23.2828555341
433PhosphorylationMVNGGLTSQTKENGL
HHCCCCCCCCCCCCC
40.6828674419
435PhosphorylationNGGLTSQTKENGLST
CCCCCCCCCCCCCCC
39.8425627689
441PhosphorylationQTKENGLSTSQQVPA
CCCCCCCCCCCCCCH
27.66-
442PhosphorylationTKENGLSTSQQVPAQ
CCCCCCCCCCCCCHH
35.28-
443PhosphorylationKENGLSTSQQVPAQR
CCCCCCCCCCCCHHH
18.4228555341
453PhosphorylationVPAQRKKLLRAPTLA
CCHHHHHHHHCCCHH
4.3733259812
458PhosphorylationKKLLRAPTLAELDSS
HHHHHCCCHHHCCCC
37.3027273156
464PhosphorylationPTLAELDSSESEEET
CCHHHCCCCCCHHHH
48.9427273156
465PhosphorylationTLAELDSSESEEETL
CHHHCCCCCCHHHHH
44.8227273156
467PhosphorylationAELDSSESEEETLHK
HHCCCCCCHHHHHHH
52.8627273156
471PhosphorylationSSESEEETLHKSTSS
CCCCHHHHHHHCCCC
37.1321955146
475PhosphorylationEEETLHKSTSSSSVS
HHHHHHHCCCCCCCC
23.8325850435
476PhosphorylationEETLHKSTSSSSVSP
HHHHHHCCCCCCCCC
37.1125850435
477PhosphorylationETLHKSTSSSSVSPS
HHHHHCCCCCCCCCC
35.0025627689
478PhosphorylationTLHKSTSSSSVSPSF
HHHHCCCCCCCCCCC
27.0722199227
479PhosphorylationLHKSTSSSSVSPSFP
HHHCCCCCCCCCCCC
34.2322199227
480PhosphorylationHKSTSSSSVSPSFPE
HHCCCCCCCCCCCCC
28.6725850435
482PhosphorylationSTSSSSVSPSFPEEP
CCCCCCCCCCCCCCC
19.4422199227
484PhosphorylationSSSSVSPSFPEEPVL
CCCCCCCCCCCCCHH
46.0225850435
495PhosphorylationEPVLEAVSTRKKPPK
CCHHHHHCCCCCCCC
29.5532142685
507PhosphorylationPPKFLPISSTPQPER
CCCCCCCCCCCCHHH
26.6430266825
508PhosphorylationPKFLPISSTPQPERR
CCCCCCCCCCCHHHC
44.8430266825
509PhosphorylationKFLPISSTPQPERRQ
CCCCCCCCCCHHHCC
21.1019664994
523PhosphorylationQPPQRRHSIEKETPT
CCCCCCCCCCCCCCC
30.5423401153
528PhosphorylationRHSIEKETPTNVRQF
CCCCCCCCCCCHHHH
46.6223403867
542PhosphorylationFLPPSRQSSRSLEEF
HCCCCCCCCCCHHHH
26.9723090842
543PhosphorylationLPPSRQSSRSLEEFC
CCCCCCCCCCHHHHC
19.9723090842
545PhosphorylationPSRQSSRSLEEFCYP
CCCCCCCCHHHHCHH
41.9225849741
551PhosphorylationRSLEEFCYPVECLAL
CCHHHHCHHHHHHHC
18.6823090842
578PhosphorylationVKAELEKYQQYKDIY
HHHHHHHHHHHHHHH
7.47-
630PhosphorylationCKKMRLPSKPYSTLP
HHHCCCCCCCCCCCC
51.3524719451
652PhosphorylationALQRGESSMRSEKPS
HHHHCCHHCCCCCCC
17.57-
668PhosphorylationAHHRPLRSIARFSSK
CCCCCHHHHHHHHCC
28.4330177828
673PhosphorylationLRSIARFSSKSKSMD
HHHHHHHHCCCCCCC
31.1630177828
674PhosphorylationRSIARFSSKSKSMDK
HHHHHHHCCCCCCCC
37.9330177828
676PhosphorylationIARFSSKSKSMDKSD
HHHHHCCCCCCCCCH
31.7323403867
678PhosphorylationRFSSKSKSMDKSDEE
HHHCCCCCCCCCHHH
39.0323401153
682PhosphorylationKSKSMDKSDEELQFP
CCCCCCCCHHHHCCC
46.0930266825
710PhosphorylationVDCKKFISEIISSSR
HHHHHHHHHHHHHHH
26.35-
714PhosphorylationKFISEIISSSRRSLV
HHHHHHHHHHHHHHH
28.1129507054
715PhosphorylationFISEIISSSRRSLVL
HHHHHHHHHHHHHHH
19.9120058876
716PhosphorylationISEIISSSRRSLVLA
HHHHHHHHHHHHHHH
25.5620058876
719PhosphorylationIISSSRRSLVLANKR
HHHHHHHHHHHHCHH
23.0127251275
733PhosphorylationRARLKRKTQSFYMSS
HHHHCHHCCCCCCCC
33.2223401153
735PhosphorylationRLKRKTQSFYMSSPG
HHCHHCCCCCCCCCC
24.4725159151
737PhosphorylationKRKTQSFYMSSPGPS
CHHCCCCCCCCCCHH
11.0126074081
739PhosphorylationKTQSFYMSSPGPSEY
HCCCCCCCCCCHHHC
23.2321815630
740PhosphorylationTQSFYMSSPGPSEYC
CCCCCCCCCCHHHCC
19.8328985074
744PhosphorylationYMSSPGPSEYCPSER
CCCCCCHHHCCCCCC
47.3027080861
746PhosphorylationSSPGPSEYCPSERTI
CCCCHHHCCCCCCCC
17.6327642862

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 SPIR1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPIR1_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 SPIR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SPIR1_HUMAN !!

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 SPIR1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-464; SER-465 ANDSER-467, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-465 ANDSER-467, AND MASS SPECTROMETRY.

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