SPIR2_HUMAN - dbPTM
SPIR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPIR2_HUMAN
UniProt AC Q8WWL2
Protein Name Protein spire homolog 2
Gene Name SPIRE2
Organism Homo sapiens (Human).
Sequence Length 714
Subcellular Localization Cytoplasm, cytoskeleton. Cytoplasm, cytosol. Cytoplasm, perinuclear region. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Detected at the cleavage furrow dur
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 MARAGSCGGAAAGAGRPEPWELSLEEVLKAYEQPLNEEQAWAVCFQGCRGLRGSPGRRLRDTGDLLLRGDGSVGAREPEAAEPATMVVPLASSEAQTVQSLGFAIYRALDWGLDESEERELSPQLERLIDLMANNDSEDSGCGAADEGYGGPEEEEEAEGVPRSVRTFAQAMRLCAARLTDPRGAQAHYQAVCRALFVETLELRAFLARVREAKEMLQKLREDEPHLETPRAELDSLGHTDWARLWVQLMRELRRGVKLKKVQEQEFNPLPTEFQLTPFEMLMQDIRARNYKLRKVMVDGDIPPRVKKDAHELILDFIRSRPPLKQVSERRLRPLPPKQRSLHEKILEEIKQERRLRPVRGEGWAARGFGSLPCILNACSGDAKSTSCINLSVTDAGGSAQRPRPRVLLKAPTLAEMEEMNTSEEEESPCGEVTLKRDRSFSEHDLAQLRSEVASGLQSATHPPGGTEPPRPRAGSAHVWRPGSRDQGTCPASVSDPSHPLLSNRGSSGDRPEASMTPDAKHLWLEFSHPVESLALTVEEVMDVRRVLVKAEMEKFLQNKELFSSLKKGKICCCCRAKFPLFSWPPSCLFCKRAVCTSCSIKMKMPSKKFGHIPVYTLGFESPQRVSAAKTAPIQRRDIFQSLQGPQWQSVEEAFPHIYSHGCVLKDVCSECTSFVADVVRSSRKSVDVLNTTPRRSRQTQSLYIPNTRTLDFK
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
62PhosphorylationPGRRLRDTGDLLLRG
CCCCCCCCCCEEECC		26.6020068231
72PhosphorylationLLLRGDGSVGAREPE
EEECCCCCCCCCCCC		23.3220068231
122PhosphorylationESEERELSPQLERLI
HHHHHHHCHHHHHHH		13.0723403867
272PhosphorylationQEFNPLPTEFQLTPF
CCCCCCCCCCCCCHH		58.0526074081
277PhosphorylationLPTEFQLTPFEMLMQ
CCCCCCCCHHHHHHH		18.3626074081
291PhosphorylationQDIRARNYKLRKVMV
HHHHHCCCCCCEEEE		13.0718083107
371PhosphorylationWAARGFGSLPCILNA
HHHCCCCCCCCHHHH		27.2030266825
380PhosphorylationPCILNACSGDAKSTS
CCHHHHCCCCCCCCC		36.9820068231
385PhosphorylationACSGDAKSTSCINLS
HCCCCCCCCCEEEEE		27.5523312004
386PhosphorylationCSGDAKSTSCINLSV
CCCCCCCCCEEEEEE		27.2323312004
387PhosphorylationSGDAKSTSCINLSVT
CCCCCCCCEEEEEEE		21.7930576142
392PhosphorylationSTSCINLSVTDAGGS
CCCEEEEEEECCCCC		20.6223312004
394PhosphorylationSCINLSVTDAGGSAQ
CEEEEEEECCCCCCC		19.4323312004
399PhosphorylationSVTDAGGSAQRPRPR
EEECCCCCCCCCCCE		21.9523312004
422PhosphorylationAEMEEMNTSEEEESP
HHHHHHCCCCCCCCC		35.8825159151
423PhosphorylationEMEEMNTSEEEESPC
HHHHHCCCCCCCCCC		37.7030576142
428PhosphorylationNTSEEEESPCGEVTL
CCCCCCCCCCCCCEE		28.8628102081
434PhosphorylationESPCGEVTLKRDRSF
CCCCCCCEECCCCCC		23.4328102081
440PhosphorylationVTLKRDRSFSEHDLA
CEECCCCCCCHHHHH		37.1030266825
442PhosphorylationLKRDRSFSEHDLAQL
ECCCCCCCHHHHHHH		34.9630266825
476PhosphorylationPPRPRAGSAHVWRPG
CCCCCCCCCCCCCCC		17.7620873877
484PhosphorylationAHVWRPGSRDQGTCP
CCCCCCCCCCCCCCC		35.0523312004
503PhosphorylationDPSHPLLSNRGSSGD
CCCCCCCCCCCCCCC		31.9623898821
517PhosphorylationDRPEASMTPDAKHLW
CCCCCCCCCCCCCHH		18.6023898821
598PhosphorylationCKRAVCTSCSIKMKM
HCCHHEECCCEEEEC		10.76-
600PhosphorylationRAVCTSCSIKMKMPS
CHHEECCCEEEECCC		25.63-
607PhosphorylationSIKMKMPSKKFGHIP
CEEEECCCCCCCCCC		45.0024702127
622PhosphorylationVYTLGFESPQRVSAA
EEECCCCCCHHCCCC		24.8725159151
627PhosphorylationFESPQRVSAAKTAPI
CCCCHHCCCCCCCCC		25.38-
631PhosphorylationQRVSAAKTAPIQRRD
HHCCCCCCCCCCHHH		32.70-
692PhosphorylationKSVDVLNTTPRRSRQ
CCEEECCCCCCCCCC		33.7321815630
693PhosphorylationSVDVLNTTPRRSRQT
CEEECCCCCCCCCCC		17.4525850435
697PhosphorylationLNTTPRRSRQTQSLY
CCCCCCCCCCCCCEE		29.9817081983
700PhosphorylationTPRRSRQTQSLYIPN
CCCCCCCCCCEEECC		21.0020068231
702PhosphorylationRRSRQTQSLYIPNTR
CCCCCCCCEEECCCC		26.9130576142
704PhosphorylationSRQTQSLYIPNTRTL
CCCCCCEEECCCCCC		21.4120068231
708PhosphorylationQSLYIPNTRTLDFK-
CCEEECCCCCCCCC-		21.4820068231
710PhosphorylationLYIPNTRTLDFK---
EEECCCCCCCCC---		28.7420068231
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 SPIR2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPIR2_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 SPIR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SPIR2_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 SPIR2_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-371 AND SER-442, ANDMASS SPECTROMETRY.

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