IL16_MOUSE - dbPTM
IL16_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IL16_MOUSE
UniProt AC O54824
Protein Name Pro-interleukin-16
Gene Name Il16
Organism Mus musculus (Mouse).
Sequence Length 1322
Subcellular Localization Secreted.
Isoform 1: Cytoplasm . Colocalizes with GRIN2C in neuronal cell bodies and neurites.
Isoform 2: Cytoplasm. Nucleus.
Protein Description Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.; Isoform 1 may act as a scaffolding protein that anchors ion channels in the membrane.; Isoform 2 is involved in cell cycle progression in T-cells. Appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells..
Protein Sequence MEPHGHSGKSRKSTKFRSISRSLILCNAKTSDDGSSPDEKYPDPFETSLCQGKEGFFHSSMQLADTFEAGLSNIPDLALASDSAQLAAAGSDRGKHCRKMFFMKESSSTSSKEKSGKPEAQSSSFLFPKACHQRTRSNSTSVNPYSAGEIDFPMTKKSAAPTDRQPYSLCSNRKSLSQQLDYPILGTARPTRSLSTAQLGQLSGGLQASVISNIVLMKGQAKGLGFSIVGGKDSIYGPIGIYVKSIFAGGAAAADGRLQEGDEILELNGESMAGLTHQDALQKFKQAKKGLLTLTVRTRLTTPPSLCSHLSPPLCRSLSSSTCGAQDSSPFSLESPASPASTAKPNYRIMVEVSLKKEAGVGLGIGLCSIPYFQCISGIFVHTLSPGSVAHLDGRLRCGDEIVEINDSPVHCLTLNEVYTILSHCDPGPVPIIVSRHPDPQVSEQQLKEAVAQAVEGVKFGKDRHQWSLEGVKRLESSWHGRPTLEKEREKHSAPPHRRAQKIMVRSSSDSSYMSGSPGGSPCSAGAEPQPSEREGSTHSPSLSPGEEQEPCPGVPSRPQQESPPLPESLERESHPPLRLKKSFEILVRKPTSSKPKPPPRKYFKNDSEPQKKLEEKEKVTDPSGHTLPTCSQETRELLPLLLQEDTAGRAPCTAACCPGPAASTQTSSSTEGESRRSASPETPASPGKHPLLKRQARMDYSFDITAEDPWVRISDCIKNLFSPIMSENHSHTPLQPNTSLGEEDGTQGCPEGGLSKMDAANGAPRVYKSADGSTVKKGPPVAPKPAWFRQSLKGLRNRAPDPRRPPEVASAIQPTPVSRDPPGPQPQASSSIRQRISSFENFGSSQLPDRGVQRLSLQPSSGETTKFPGKQDGGRFSGLLGQGATVTAKHRQTEVESMSTTFPNSSEVRDPGLPESPPPGQRPSTKALSPDPLLRLLTTQSEDTQGPGLKMPSQRARSFPLTRTQSCETKLLDEKASKLYSISSQLSSAVMKSLLCLPSSVSCGQITCIPKERVSPKSPCNNSSAAEGFGEAMASDTGFSLNLSELREYSEGLTEPGETEDRNHCSSQAGQSVISLLSAEELEKLIEEVRVLDEATLKQLDSIHVTILHKEEGAGLGFSLAGGADLENKVITVHRVFPNGLASQEGTIQKGNEVLSINGKSLKGATHNDALAILRQARDPRQAVIVTRRTTVEATHDLNSSTDSAASASAASDISVESKEATVCTVTLEKTSAGLGFSLEGGKGSLHGDKPLTINRIFKGTEQGEMVQPGDEILQLAGTAVQGLTRFEAWNVIKALPDGPVTIVIRRTSLQCKQTTASADS
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
30PhosphorylationLILCNAKTSDDGSSP
EEECCCCCCCCCCCC		34.6729899451
31PhosphorylationILCNAKTSDDGSSPD
EECCCCCCCCCCCCC		32.7629899451
35PhosphorylationAKTSDDGSSPDEKYP
CCCCCCCCCCCCCCC		45.7729899451
41PhosphorylationGSSPDEKYPDPFETS
CCCCCCCCCCHHHCC		15.7229899451
137PhosphorylationACHQRTRSNSTSVNP
HHCHHCCCCCCCCCC		34.22-
139PhosphorylationHQRTRSNSTSVNPYS
CHHCCCCCCCCCCCC		24.2527180971
141PhosphorylationRTRSNSTSVNPYSAG
HCCCCCCCCCCCCCC		21.51-
175PhosphorylationSLCSNRKSLSQQLDY
CCCCCCCCHHHHCCC		29.9829899451
177PhosphorylationCSNRKSLSQQLDYPI
CCCCCCHHHHCCCCC		23.9929899451
193PhosphorylationGTARPTRSLSTAQLG
CCCCCCCCCCHHHHH		29.20-
195PhosphorylationARPTRSLSTAQLGQL
CCCCCCCCHHHHHHH		23.96-
218AcetylationISNIVLMKGQAKGLG
CCEEEEECCCCCCCC		43.6519843233
222AcetylationVLMKGQAKGLGFSIV
EEECCCCCCCCCEEE		46.9419843241
468PhosphorylationGKDRHQWSLEGVKRL
CCCCCCCCHHHHHHH		15.2421183079
508PhosphorylationQKIMVRSSSDSSYMS
CEEEEECCCCCCCCC		27.8329899451
512PhosphorylationVRSSSDSSYMSGSPG
EECCCCCCCCCCCCC		29.8229899451
524PhosphorylationSPGGSPCSAGAEPQP
CCCCCCCCCCCCCCC		32.8724719451
583PhosphorylationPPLRLKKSFEILVRK
CCCCCCCEEEEEECC		26.9021183079
678PhosphorylationTEGESRRSASPETPA
CCCCCCCCCCCCCCC		31.8025521595
680PhosphorylationGESRRSASPETPASP
CCCCCCCCCCCCCCC		25.2325521595
683PhosphorylationRRSASPETPASPGKH
CCCCCCCCCCCCCCC		27.7829899451
686PhosphorylationASPETPASPGKHPLL
CCCCCCCCCCCCCHH		35.0725521595
792PhosphorylationKPAWFRQSLKGLRNR
CCHHHHHHHHHHHHC		28.0025266776
830PhosphorylationPGPQPQASSSIRQRI
CCCCCCCCHHHHHHH		21.2629176673
831PhosphorylationGPQPQASSSIRQRIS
CCCCCCCHHHHHHHH		32.5729176673
832PhosphorylationPQPQASSSIRQRISS
CCCCCCHHHHHHHHH		21.2124704852
838PhosphorylationSSIRQRISSFENFGS
HHHHHHHHHCCCCCC		31.0327742792
839PhosphorylationSIRQRISSFENFGSS
HHHHHHHHCCCCCCC		33.9225521595
845PhosphorylationSSFENFGSSQLPDRG
HHCCCCCCCCCCCCC		15.6928833060
857PhosphorylationDRGVQRLSLQPSSGE
CCCCEEEEECCCCCC		27.4428833060
861PhosphorylationQRLSLQPSSGETTKF
EEEEECCCCCCCCCC		37.7129176673
902PhosphorylationEVESMSTTFPNSSEV
HHHHCCCCCCCCHHC		29.7728285833
906PhosphorylationMSTTFPNSSEVRDPG
CCCCCCCCHHCCCCC		28.2828285833
907PhosphorylationSTTFPNSSEVRDPGL
CCCCCCCHHCCCCCC		46.9128285833
917PhosphorylationRDPGLPESPPPGQRP
CCCCCCCCCCCCCCC		40.5427742792
925PhosphorylationPPPGQRPSTKALSPD
CCCCCCCCCCCCCCC		44.7420531401
926PhosphorylationPPGQRPSTKALSPDP
CCCCCCCCCCCCCCH		24.0227742792
930PhosphorylationRPSTKALSPDPLLRL
CCCCCCCCCCHHHHH		31.9223527152
942PhosphorylationLRLLTTQSEDTQGPG
HHHHHCCCCCCCCCC		35.0329899451
959PhosphorylationMPSQRARSFPLTRTQ
CCCHHHHCCCCCCCC		30.1724704852
963PhosphorylationRARSFPLTRTQSCET
HHHCCCCCCCCCCCC		31.7226745281
965PhosphorylationRSFPLTRTQSCETKL
HCCCCCCCCCCCCHH		21.4326745281
967PhosphorylationFPLTRTQSCETKLLD
CCCCCCCCCCCHHHH		17.2028833060
970PhosphorylationTRTQSCETKLLDEKA
CCCCCCCCHHHHHHH		31.1826745281
981PhosphorylationDEKASKLYSISSQLS
HHHHHHHHCHHHHHH		14.0128833060
982PhosphorylationEKASKLYSISSQLSS
HHHHHHHCHHHHHHH		26.8228833060
994PhosphorylationLSSAVMKSLLCLPSS
HHHHHHHHHHCCCCC		14.4227600695
1000PhosphorylationKSLLCLPSSVSCGQI
HHHHCCCCCCCCCEE		30.3523984901
1001PhosphorylationSLLCLPSSVSCGQIT
HHHCCCCCCCCCEEE		18.9923984901
1003PhosphorylationLCLPSSVSCGQITCI
HCCCCCCCCCEEEEE		17.9325521595
1008PhosphorylationSVSCGQITCIPKERV
CCCCCEEEEEECCCC		9.1123984901
1019PhosphorylationKERVSPKSPCNNSSA
CCCCCCCCCCCCCHH		37.7627600695
1246PhosphorylationSLEGGKGSLHGDKPL
EEECCCCCCCCCCCC		22.2227600695
1310PhosphorylationTIVIRRTSLQCKQTT
EEEEEECCCCCCCCC		18.0327600695
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 IL16_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IL16_MOUSE !!
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 IL16_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NMDE1_MOUSEGrin2aphysical
10479680
KCNJ2_MOUSEKcnj2physical
10479680
KCJ10_MOUSEKcnj10physical
10479680
KCJ15_MOUSEKcnj15physical
10479680
KCND1_MOUSEKcnd1physical
10479680
KCND2_MOUSEKcnd2physical
10479680
CAC1C_MOUSECacna1cphysical
10479680
NMDE2_RATGrin2bphysical
10479680
NMDE3_RATGrin2cphysical
10479680
NMDE4_RATGrin2dphysical
10479680
KCND3_RATKcnd3physical
10479680
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IL16_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-917, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-838, AND MASSSPECTROMETRY.

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