SLMAP_HUMAN - dbPTM
SLMAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLMAP_HUMAN
UniProt AC Q14BN4
Protein Name Sarcolemmal membrane-associated protein
Gene Name SLMAP
Organism Homo sapiens (Human).
Sequence Length 828
Subcellular Localization Cell membrane, sarcolemma
Single-pass type IV membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Membrane-associated. Distributed in the transverse tubules and near the junctional sarcoplasmic reticulum. Detected a
Protein Description May play a role during myoblast fusion..
Protein Sequence MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLPDGMEARLRSDVIHAPLPSPVDKVAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNNKPWPWMPMLAALVAVTAIVLYVPGLARASP
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
3Phosphorylation-----MPSALAIFTC
-----CCCEEEEEEE		34.3224043423
9PhosphorylationPSALAIFTCRPNSHP
CCEEEEEEECCCCCC		11.0724043423
29AcetylationVYLDEPIKIGRSVAR
EEECCCCCCCCCCCC		50.2325953088
29 (in isoform 3)Acetylation-50.23-
29MalonylationVYLDEPIKIGRSVAR
EEECCCCCCCCCCCC		50.2326320211
89PhosphorylationSQRLSRGSEESPPCE
CEECCCCCCCCCCCE		36.7630576142
92PhosphorylationLSRGSEESPPCEILS
CCCCCCCCCCCEECC		30.0530576142
99PhosphorylationSPPCEILSGDIIQFG
CCCCEECCCCEEEEC		39.8330576142
115UbiquitinationDVTENTRKVTHGCIV
ECCCCCCCCCCCCEE		49.82-
139PhosphorylationGMEARLRSDVIHAPL
CHHHHCCCCCCCCCC		40.60-
148 (in isoform 3)Phosphorylation-45.2824719451
148PhosphorylationVIHAPLPSPVDKVAA
CCCCCCCCCCCHHHC		45.2825159151
161PhosphorylationAANTPSMYSQELFQL
HCCCCHHHHHHHHHH		16.13-
162PhosphorylationANTPSMYSQELFQLS
CCCCHHHHHHHHHHH		14.45-
229UbiquitinationNQLQACSKNQTEDSL
HHHHHHCCCCCHHHH		53.62-
232PhosphorylationQACSKNQTEDSLRKE
HHHCCCCCHHHHHHH		51.6723312004
235PhosphorylationSKNQTEDSLRKELIA
CCCCCHHHHHHHHHH		24.6830576142
238UbiquitinationQTEDSLRKELIALQE
CCHHHHHHHHHHHHH		63.26-
238AcetylationQTEDSLRKELIALQE
CCHHHHHHHHHHHHH		63.267693141
247AcetylationLIALQEDKHNYETTA
HHHHHHHHCCHHHHH		32.757693151
254 (in isoform 8)Phosphorylation-22.4922199227
255AcetylationHNYETTAKESLRRVL
CCHHHHHHHHHHHHH		45.827693161
255UbiquitinationHNYETTAKESLRRVL
CCHHHHHHHHHHHHH		45.82-
273 (in isoform 3)Phosphorylation-42.5027251275
273PhosphorylationIEVVRKLSEVERSLS
HHHHHHHHHHHHHHC		42.5028060719
278PhosphorylationKLSEVERSLSNTEDE
HHHHHHHHHCCCHHH		23.7327251275
280PhosphorylationSEVERSLSNTEDECT
HHHHHHHCCCHHHHH		42.8427251275
282 (in isoform 3)Phosphorylation-41.2427251275
282PhosphorylationVERSLSNTEDECTHL
HHHHHCCCHHHHHHH		41.2428985074
287 (in isoform 3)Phosphorylation-28.35-
287PhosphorylationSNTEDECTHLKEMNE
CCCHHHHHHHHHHHH		28.3518452278
359UbiquitinationKEQELQAKIEALQAD
HHHHHHHHHHHHHCC		28.28-
385 (in isoform 3)Phosphorylation-52.6425159151
387UbiquitinationRLEHLQEKTLKECSS
HHHHHHHHHHHHCCC		46.31-
393PhosphorylationEKTLKECSSLEHLLS
HHHHHHCCCHHHHHH		38.7623312004
394PhosphorylationKTLKECSSLEHLLSK
HHHHHCCCHHHHHHH		49.8123312004
400PhosphorylationSSLEHLLSKSGGDCT
CCHHHHHHHCCCCCC		31.0023312004
402PhosphorylationLEHLLSKSGGDCTFI
HHHHHHHCCCCCCHH		44.6330108239
407PhosphorylationSKSGGDCTFIHQFIE
HHCCCCCCHHHHHHH		30.2929449344
435 (in isoform 3)Phosphorylation-39.2124719451
435PhosphorylationAVEETKLSKENQTRA
HHHHHCCCHHHHHHH		39.2119664994
440PhosphorylationKLSKENQTRAKESDF
CCCHHHHHHHHHCCC		44.1430576142
445PhosphorylationNQTRAKESDFSDTLS
HHHHHHHCCCCCCCC		43.1625850435
448PhosphorylationRAKESDFSDTLSPSK
HHHHCCCCCCCCCCC		34.3823927012
450PhosphorylationKESDFSDTLSPSKEK
HHCCCCCCCCCCCCC		28.1230266825
452PhosphorylationSDFSDTLSPSKEKSS
CCCCCCCCCCCCCCC		29.2619664994
454PhosphorylationFSDTLSPSKEKSSDD
CCCCCCCCCCCCCCC		50.5030266825
458PhosphorylationLSPSKEKSSDDTTDA
CCCCCCCCCCCCCHH		39.8427732954
459PhosphorylationSPSKEKSSDDTTDAQ
CCCCCCCCCCCCHHH		51.0427732954
462PhosphorylationKEKSSDDTTDAQMDE
CCCCCCCCCHHHHCH		31.4027732954
463PhosphorylationEKSSDDTTDAQMDEQ
CCCCCCCCHHHHCHH		36.0127732954
480PhosphorylationNEPLAKVSLLKDDLQ
CCCHHHHHHHHHHHC		27.5521712546
491PhosphorylationDDLQGAQSEIEAKQE
HHHCHHHHHHHHHHH		39.7530622161
504UbiquitinationQEIQHLRKELIEAQE
HHHHHHHHHHHHHHH		64.33-
579PhosphorylationSTRDELLSARDEILL
CCHHHHHHHHHHHHH		33.6024719451
593UbiquitinationLLHQAAAKVASERDT
HHHHHHHHHHHHCCC		33.34-
611AcetylationSLQEELKKVRAELER
HHHHHHHHHHHHHHH		49.967469377
631PhosphorylationSEYEKEITSLQNSFQ
HHHHHHHHHHHHHHH		25.2023403867
632PhosphorylationEYEKEITSLQNSFQL
HHHHHHHHHHHHHHH		33.3523403867
636PhosphorylationEITSLQNSFQLRCQQ
HHHHHHHHHHHHHHH		11.0423403867
653PhosphorylationDQQREEATRLQGELE
HHHHHHHHHHHHHHH		34.8829083192
664AcetylationGELEKLRKEWNALET
HHHHHHHHHHHHHHH		77.0012432475
675PhosphorylationALETECHSLKRENVL
HHHHHHHHHHHHHHH		47.4428555341
677UbiquitinationETECHSLKRENVLLS
HHHHHHHHHHHHHHC		61.76-
688 (in isoform 2)Ubiquitination-40.74-
699 (in isoform 2)Ubiquitination-41.49-
704 (in isoform 2)Ubiquitination-7.24-
710 (in isoform 2)Ubiquitination-3.94-
716UbiquitinationSILQMSRKELENQVG
HHHHHCHHHHHHHHH		60.38-
724 (in isoform 3)Phosphorylation-37.0924719451
726UbiquitinationENQVGSLKEQHLRDS
HHHHHHHHHHHHHCC		57.96-
727 (in isoform 2)Ubiquitination-48.83-
729 (in isoform 2)Ubiquitination-24.75-
737UbiquitinationLRDSADLKTLLSKAE
HHCCHHHHHHHHHHH		37.36-
741PhosphorylationADLKTLLSKAENQAK
HHHHHHHHHHHHHHH		32.6924719451
742UbiquitinationDLKTLLSKAENQAKD
HHHHHHHHHHHHHHH		60.74-
754PhosphorylationAKDVQKEYEKTQTVL
HHHHHHHHHHHHHHH		29.7524144214
756UbiquitinationDVQKEYEKTQTVLSE
HHHHHHHHHHHHHHH		45.06-
757PhosphorylationVQKEYEKTQTVLSEL
HHHHHHHHHHHHHHH		19.9624144214
759PhosphorylationKEYEKTQTVLSELKL
HHHHHHHHHHHHHHH		28.7524144214
762PhosphorylationEKTQTVLSELKLKFE
HHHHHHHHHHHHHHC		36.2224144214
765UbiquitinationQTVLSELKLKFEMTE
HHHHHHHHHHHCCCH		45.65-
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 SLMAP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLMAP_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 SLMAP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STK4_HUMANSTK4physical
24255178
STK3_HUMANSTK3physical
24255178
CP131_HUMANCEP131physical
24255178
CENPJ_HUMANCENPJphysical
24255178
CNTRB_HUMANCNTROBphysical
24255178
4EBP1_HUMANEIF4EBP1physical
24255178
CCSE2_HUMANCCSER2physical
24255178
STRP1_HUMANSTRIP1physical
24255178
FA83B_HUMANFAM83Bphysical
24255178
FGOP2_HUMANFGFR1OP2physical
24255178
FRYL_HUMANFRYLphysical
24255178
GFOD1_HUMANGFOD1physical
24255178
HDAC6_HUMANHDAC6physical
24255178
C170B_HUMANCEP170Bphysical
24255178
K1522_HUMANKIAA1522physical
24255178
PHOCN_HUMANMOB4physical
24255178
OFD1_HUMANOFD1physical
24255178
RABE1_HUMANRABEP1physical
24255178
RABX5_HUMANRABGEF1physical
24255178
RGPA1_HUMANRALGAPA1physical
24255178
RLGPB_HUMANRALGAPBphysical
24255178
SIKE1_HUMANSIKE1physical
24255178
STRN_HUMANSTRNphysical
24255178
STRN3_HUMANSTRN3physical
24255178
STRN4_HUMANSTRN4physical
24255178
TAB1_HUMANTAB1physical
24255178
2AAB_HUMANPPP2R1Bphysical
24366813
FGOP2_HUMANFGFR1OP2physical
24366813
STK26_HUMANSTK26physical
24366813
PDC10_HUMANPDCD10physical
24366813
PHOCN_HUMANMOB4physical
24366813
RABE1_HUMANRABEP1physical
24366813
RABX5_HUMANRABGEF1physical
24366813
SIKE1_HUMANSIKE1physical
24366813
STK24_HUMANSTK24physical
24366813
STRN_HUMANSTRNphysical
24366813
STRN3_HUMANSTRN3physical
24366813
STRN4_HUMANSTRN4physical
24366813
STRP1_HUMANSTRIP1physical
24366813
STRP2_HUMANSTRIP2physical
24366813
PFD6_HUMANPFDN6physical
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 SLMAP_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-148, AND MASSSPECTROMETRY.

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