SPAT6_HUMAN - dbPTM
SPAT6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPAT6_HUMAN
UniProt AC Q9NWH7
Protein Name Spermatogenesis-associated protein 6
Gene Name SPATA6
Organism Homo sapiens (Human).
Sequence Length 488
Subcellular Localization Secreted . Cell projection, cilium, flagellum . Specifically localizes to the segmented columns and the capitulum of the sperm connecting piece.
Protein Description Required for formation of the sperm connecting piece during spermiogenesis. Sperm connecting piece is essential for linking the developing flagellum to the head during late spermiogenesis. May be involved in myosin-based microfilament transport through interaction with myosin subunits..
Protein Sequence MPKVKALQCALALEISSVTCPGVVLKDKEDIYLSICVFGQYKKTQCVPATFPLVFNARMVFEKVFPDAVDPGDVVTQLEYDTAVFELIQLVPPVGETLSTYDENTRDFMFPGPNQMSGHHDSNRQVTMRRISGLRGNAPRLEFSTTSVITECLISSRKCHTQDKFIYHLAPVEKSHGRLQNRTSRSQKKKSKSPERSKYCINAKNYEQPTISSKSHSPSPYTKRRMCELSEDTRRRLAHLNLGPYEFKKETDKPPFVIRHVDPPSPRADTLLGSSGRDCERDGWSRVHNDHSHLGCCRPKDYKVIRTPHGRDFDDSLEKCEEYLSPRSCSKPRHSARTLLVHSAPSTMPKHSPSPVLNRASLRERFHSDWCSPSNCDEIHDRVKNVLKSHQAHQRHLYDERDLEKDDELELKRSLLCRDSAYDSDPEYSSCQQPRGTFHLDDGEYWSNRAASYKGKSHRPIFENSMDKMYRNLYKKACSSASHTQESF
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
17PhosphorylationALALEISSVTCPGVV
HHHHHHCCCCCCCEE		27.40-
19PhosphorylationALEISSVTCPGVVLK
HHHHCCCCCCCEEEC		18.22-
132PhosphorylationQVTMRRISGLRGNAP
HHHHHHHHCCCCCCC		29.9324719451
181N-linked_GlycosylationKSHGRLQNRTSRSQK
HHHCCCCCCCCHHHC		54.51UniProtKB CARBOHYD
191PhosphorylationSRSQKKKSKSPERSK
CHHHCHHCCCCCHHH		47.4430622161
193PhosphorylationSQKKKSKSPERSKYC
HHCHHCCCCCHHHHC		38.8030622161
197PhosphorylationKSKSPERSKYCINAK
HCCCCCHHHHCCCCC		26.7230622161
206PhosphorylationYCINAKNYEQPTISS
HCCCCCCCCCCCCCC		18.4230622161
215PhosphorylationQPTISSKSHSPSPYT
CCCCCCCCCCCCCCC		31.0130622161
217PhosphorylationTISSKSHSPSPYTKR
CCCCCCCCCCCCCHH		33.8822817900
219PhosphorylationSSKSHSPSPYTKRRM
CCCCCCCCCCCHHHH		33.2922817900
221PhosphorylationKSHSPSPYTKRRMCE
CCCCCCCCCHHHHHH		29.2730622161
222PhosphorylationSHSPSPYTKRRMCEL
CCCCCCCCHHHHHHC		22.8130622161
230PhosphorylationKRRMCELSEDTRRRL
HHHHHHCCHHHHHHH		15.9029449344
233PhosphorylationMCELSEDTRRRLAHL
HHHCCHHHHHHHHHC		23.2529449344
248SumoylationNLGPYEFKKETDKPP
CCCCCCCCCCCCCCC		37.4528112733
265PhosphorylationIRHVDPPSPRADTLL
EEECCCCCCCHHHHC		32.1928857561
274PhosphorylationRADTLLGSSGRDCER
CHHHHCCCCCCCCCC		29.59-
292PhosphorylationSRVHNDHSHLGCCRP
CCCCCCCCCCCCCCC		24.2230622161
316PhosphorylationHGRDFDDSLEKCEEY
CCCCCHHHHHHHHHH		40.0330622161
325PhosphorylationEKCEEYLSPRSCSKP
HHHHHHCCCCCCCCC		19.8425693802
335PhosphorylationSCSKPRHSARTLLVH
CCCCCCCCCCEEEEE		22.2630622161
338PhosphorylationKPRHSARTLLVHSAP
CCCCCCCEEEEECCC		24.9430622161
343PhosphorylationARTLLVHSAPSTMPK
CCEEEEECCCCCCCC		34.1027251275
346PhosphorylationLLVHSAPSTMPKHSP
EEEECCCCCCCCCCC		36.7330622161
347PhosphorylationLVHSAPSTMPKHSPS
EEECCCCCCCCCCCC		36.1130622161
352PhosphorylationPSTMPKHSPSPVLNR
CCCCCCCCCCCCCCH		32.9527732954
354PhosphorylationTMPKHSPSPVLNRAS
CCCCCCCCCCCCHHH		30.5628857561
361PhosphorylationSPVLNRASLRERFHS
CCCCCHHHHHHHHCC		25.4030622161
398PhosphorylationQAHQRHLYDERDLEK
HHHHHHCCCCCCCCC		15.05-
414PhosphorylationDELELKRSLLCRDSA
CHHHHHHHHHHCCCC		24.8930622161
420PhosphorylationRSLLCRDSAYDSDPE
HHHHHCCCCCCCCCC		14.9128857561
422PhosphorylationLLCRDSAYDSDPEYS
HHHCCCCCCCCCCCC		21.6727966365
424PhosphorylationCRDSAYDSDPEYSSC
HCCCCCCCCCCCCCC		42.2529507054
428PhosphorylationAYDSDPEYSSCQQPR
CCCCCCCCCCCCCCC		15.9825693802
429PhosphorylationYDSDPEYSSCQQPRG
CCCCCCCCCCCCCCC		23.9930622161
430PhosphorylationDSDPEYSSCQQPRGT
CCCCCCCCCCCCCCE		18.2925693802
465PhosphorylationHRPIFENSMDKMYRN
CCCCCCCHHHHHHHH		22.5930622161
470PhosphorylationENSMDKMYRNLYKKA
CCHHHHHHHHHHHHH		11.3329759185
480PhosphorylationLYKKACSSASHTQES
HHHHHHHHCCCCCCC		33.40-
482PhosphorylationKKACSSASHTQESF-
HHHHHHCCCCCCCC-		29.0830622161
484PhosphorylationACSSASHTQESF---
HHHHCCCCCCCC---		31.3830622161
487PhosphorylationSASHTQESF------
HCCCCCCCC------		26.83-
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 SPAT6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPAT6_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 SPAT6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDB2_HUMANDDB2physical
28514442
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 SPAT6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of capacitated human sperm. Evidence oftyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation.";
Ficarro S., Chertihin O., Westbrook V.A., White F., Jayes F.,Kalab P., Marto J.A., Shabanowitz J., Herr J.C., Hunt D.F.,Visconti P.E.;
J. Biol. Chem. 278:11579-11589(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-219; SER-352AND SER-354, AND MASS SPECTROMETRY.

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