SPA5L_HUMAN - dbPTM
SPA5L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPA5L_HUMAN
UniProt AC Q9BVQ7
Protein Name Spermatogenesis-associated protein 5-like protein 1
Gene Name SPATA5L1
Organism Homo sapiens (Human).
Sequence Length 753
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MAPDSDPFPEGPLLKLLPLDARDRGTQRCRLGPAALHALGARLGSAVKISLPDGGSCLCTAWPRRDGADGFVQLDPLCASPGAAVGASRSRRSLSLNRLLLVPCPPLRRVAVWPVLRERAGAPGARNTAAVLEAAQELLRNRPISLGHVVVAPPGAPGLVAALHIVGGTPSPDPAGLVTPRTRVSLGGEPPSEAQPQPEVPLGGLSEAADSLRELLRLPLRYPRALTALGLAVPRGVLLAGPPGVGKTQLVRAVAREAGAELLAVSAPALQGSRPGETEENVRRVFQRARELASRGPSLLFLDEMDALCPQRGSRAPESRVVAQVLTLLDGASGDREVVVVGATNRPDALDPALRRPGRFDREVVIGTPTLKQRKEILQVITSKMPISSHVDLGLLAEMTVGYVGADLTALCREAAMHALLHSEKNQDNPVIDEIDFLEAFKNIQPSSFRSVIGLMDIKPVDWEEIGGLEDVKLKLKQSIEWPLKFPWEFVRMGLTQPKGVLLYGPPGCAKTTLVRALATSCHCSFVSVSGADLFSPFVGDSEKVLSQIFRQARASTPAILFLDEIDSILGARSASKTGCDVQERVLSVLLNELDGVGLKTIERRGSKSSQQEFQEVFNRSVMIIAATNRPDVLDTALLRPGRLDKIIYIPPPDHKGRLSILKVCTKTMPIGPDVSLENLAAETCFFSGADLRNLCTEAALLALQENGLDATTVKQEHFLKSLKTVKPSLSCKDLALYENLFKKEGFSNVEGI
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-------MAPDSDPF
-------CCCCCCCC
12.6222814378
5Phosphorylation---MAPDSDPFPEGP
---CCCCCCCCCCCC
46.23-
15UbiquitinationFPEGPLLKLLPLDAR
CCCCCCCEECCCCHH
56.51-
48UbiquitinationARLGSAVKISLPDGG
HCCCCCEEEECCCCC
26.71-
80PhosphorylationQLDPLCASPGAAVGA
EECHHHCCCCCCCCC
23.9121712546
93PhosphorylationGASRSRRSLSLNRLL
CCCCCCCCCCCCEEE
22.6224719451
179PhosphorylationPDPAGLVTPRTRVSL
CCCCCCCCCCCEEEC
16.4624719451
182PhosphorylationAGLVTPRTRVSLGGE
CCCCCCCCEEECCCC
36.3028555341
185PhosphorylationVTPRTRVSLGGEPPS
CCCCCEEECCCCCCC
20.2927050516
247UbiquitinationAGPPGVGKTQLVRAV
CCCCCCCHHHHHHHH
30.5923000965
309GlutathionylationLDEMDALCPQRGSRA
EHHHHHHCCCCCCCC
2.6422555962
368PhosphorylationDREVVIGTPTLKQRK
CCEEEECCCCHHHHH
11.2823403867
370PhosphorylationEVVIGTPTLKQRKEI
EEEECCCCHHHHHHH
46.5623403867
372 (in isoform 2)Ubiquitination-51.0021906983
372 (in isoform 1)Ubiquitination-51.0021906983
372AcetylationVIGTPTLKQRKEILQ
EECCCCHHHHHHHHH
51.0030592581
372UbiquitinationVIGTPTLKQRKEILQ
EECCCCHHHHHHHHH
51.0021906983
375AcetylationTPTLKQRKEILQVIT
CCCHHHHHHHHHHHH
46.7630592587
375UbiquitinationTPTLKQRKEILQVIT
CCCHHHHHHHHHHHH
46.7622817900
425UbiquitinationHALLHSEKNQDNPVI
HHHHHCCCCCCCCCC
64.0221963094
442UbiquitinationIDFLEAFKNIQPSSF
HHHHHHHHCCCCCCC
61.2521987572
451PhosphorylationIQPSSFRSVIGLMDI
CCCCCCHHHEECCCC
18.9722210691
459 (in isoform 1)Ubiquitination-34.4221906983
459UbiquitinationVIGLMDIKPVDWEEI
HEECCCCCCCCHHHC
34.4221906983
459 (in isoform 2)Ubiquitination-34.4221906983
473UbiquitinationIGGLEDVKLKLKQSI
CCCHHHHEEEEHHCC
52.8321963094
475UbiquitinationGLEDVKLKLKQSIEW
CHHHHEEEEHHCCCC
48.1722817900
477UbiquitinationEDVKLKLKQSIEWPL
HHHEEEEHHCCCCCC
40.1722817900
485UbiquitinationQSIEWPLKFPWEFVR
HCCCCCCCCCHHHHC
45.3521987572
499UbiquitinationRMGLTQPKGVLLYGP
CCCCCCCCEEEEECC
52.4021963094
504PhosphorylationQPKGVLLYGPPGCAK
CCCEEEEECCCCHHH
24.3529496907
511UbiquitinationYGPPGCAKTTLVRAL
ECCCCHHHHHHHHHH
46.2327667366
547PhosphorylationGDSEKVLSQIFRQAR
CCHHHHHHHHHHHHH
24.9828857561
577UbiquitinationLGARSASKTGCDVQE
HCHHHHHHCCCCHHH
48.96-
600 (in isoform 2)Ubiquitination-41.3421906983
600UbiquitinationELDGVGLKTIERRGS
HCCCCCHHHHHHCCC
41.3421906983
600 (in isoform 1)Ubiquitination-41.3421906983
607PhosphorylationKTIERRGSKSSQQEF
HHHHHCCCCCHHHHH
27.7928464451
608UbiquitinationTIERRGSKSSQQEFQ
HHHHCCCCCHHHHHH
57.8833845483
609PhosphorylationIERRGSKSSQQEFQE
HHHCCCCCHHHHHHH
34.7728450419
610PhosphorylationERRGSKSSQQEFQEV
HHCCCCCHHHHHHHH
39.3528464451
656UbiquitinationYIPPPDHKGRLSILK
EECCCCCCCCEEEEH
53.7829967540
660PhosphorylationPDHKGRLSILKVCTK
CCCCCCEEEEHHHCC
25.2324719451
663UbiquitinationKGRLSILKVCTKTMP
CCCEEEEHHHCCCCC
33.3321963094
667UbiquitinationSILKVCTKTMPIGPD
EEEHHHCCCCCCCCC
37.3921963094
715UbiquitinationGLDATTVKQEHFLKS
CCCCCHHCHHHHHHH
48.1221963094
721UbiquitinationVKQEHFLKSLKTVKP
HCHHHHHHHCCCCCC
53.4529967540
724UbiquitinationEHFLKSLKTVKPSLS
HHHHHHCCCCCCCCC
59.3629967540
724AcetylationEHFLKSLKTVKPSLS
HHHHHHCCCCCCCCC
59.3621339330
727UbiquitinationLKSLKTVKPSLSCKD
HHHCCCCCCCCCHHH
33.8329967540
731PhosphorylationKTVKPSLSCKDLALY
CCCCCCCCHHHHHHH
24.37-
733UbiquitinationVKPSLSCKDLALYEN
CCCCCCHHHHHHHHH
53.0229967540
738PhosphorylationSCKDLALYENLFKKE
CHHHHHHHHHHHHHC
9.3625159151
743UbiquitinationALYENLFKKEGFSNV
HHHHHHHHHCCCCCC
53.7522817900
743SumoylationALYENLFKKEGFSNV
HHHHHHHHHCCCCCC
53.75-
743SumoylationALYENLFKKEGFSNV
HHHHHHHHHCCCCCC
53.75-
744UbiquitinationLYENLFKKEGFSNVE
HHHHHHHHCCCCCCC
56.5922817900
744 (in isoform 1)Ubiquitination-56.5921906983

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 SPA5L_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPA5L_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 SPA5L_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CA109_HUMANC1orf109physical
28514442
FMN2_HUMANFMN2physical
28514442
SPAT5_HUMANSPATA5physical
28514442
HSP7C_HUMANHSPA8physical
28514442
METH_HUMANMTRphysical
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 SPA5L_HUMAN

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Related Literatures of Post-Translational Modification

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