API5_HUMAN - dbPTM
API5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID API5_HUMAN
UniProt AC Q9BZZ5
Protein Name Apoptosis inhibitor 5
Gene Name API5
Organism Homo sapiens (Human).
Sequence Length 524
Subcellular Localization Nucleus . Cytoplasm . Mainly nuclear. Can also be cytoplasmic.
Isoform 3: Cytoplasm.
Protein Description Antiapoptotic factor that may have a role in protein assembly. Negatively regulates ACIN1. By binding to ACIN1, it suppresses ACIN1 cleavage from CASP3 and ACIN1-mediated DNA fragmentation. Also known to efficiently suppress E2F1-induced apoptosis. Its depletion enhances the cytotoxic action of the chemotherapeutic drugs..
Protein Sequence MPTVEELYRNYGILADATEQVGQHKDAYQVILDGVKGGTKEKRLAAQFIPKFFKHFPELADSAINAQLDLCEDEDVSIRRQAIKELPQFATGENLPRVADILTQLLQTDDSAEFNLVNNALLSIFKMDAKGTLGGLFSQILQGEDIVRERAIKFLSTKLKTLPDEVLTKEVEELILTESKKVLEDVTGEEFVLFMKILSGLKSLQTVSGRQQLVELVAEQADLEQTFNPSDPDCVDRLLQCTRQAVPLFSKNVHSTRFVTYFCEQVLPNLGTLTTPVEGLDIQLEVLKLLAEMSSFCGDMEKLETNLRKLFDKLLEYMPLPPEEAENGENAGNEEPKLQFSYVECLLYSFHQLGRKLPDFLTAKLNAEKLKDFKIRLQYFARGLQVYIRQLRLALQGKTGEALKTEENKIKVVALKITNNINVLIKDLFHIPPSYKSTVTLSWKPVQKVEIGQKRASEDTTSGSPPKKSSAGPKRDARQIYNPPSGKYSSNLGNFNYEQRGAFRGSRGGRGWGTRGNRSRGRLY
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-----MPTVEELYRN
-----CCCHHHHHHH		38.9724043423
8PhosphorylationMPTVEELYRNYGILA
CCCHHHHHHHCCCHH		10.4924043423
11PhosphorylationVEELYRNYGILADAT
HHHHHHHCCCHHHCH		9.1328152594
18PhosphorylationYGILADATEQVGQHK
CCCHHHCHHHHCCCC		27.74-
25UbiquitinationTEQVGQHKDAYQVIL
HHHHCCCCCHHHHHH		35.85-
28PhosphorylationVGQHKDAYQVILDGV
HCCCCCHHHHHHCCC		17.2828152594
30UbiquitinationQHKDAYQVILDGVKG
CCCCHHHHHHCCCCC		2.8221890473
36 (in isoform 4)Ubiquitination-58.0921890473
36 (in isoform 2)Ubiquitination-58.0921890473
362-HydroxyisobutyrylationQVILDGVKGGTKEKR
HHHHCCCCCCHHHHH		58.09-
36UbiquitinationQVILDGVKGGTKEKR
HHHHCCCCCCHHHHH		58.0921890473
36UbiquitinationQVILDGVKGGTKEKR
HHHHCCCCCCHHHHH		58.0921890473
36UbiquitinationQVILDGVKGGTKEKR
HHHHCCCCCCHHHHH		58.09-
36 (in isoform 1)Ubiquitination-58.0921890473
36 (in isoform 3)Ubiquitination-58.0921890473
40UbiquitinationDGVKGGTKEKRLAAQ
CCCCCCHHHHHHHHH		65.59-
43UbiquitinationKGGTKEKRLAAQFIP
CCCHHHHHHHHHHHH		30.56-
51UbiquitinationLAAQFIPKFFKHFPE
HHHHHHHHHHHHCHH		59.6321890473
51 (in isoform 1)Ubiquitination-59.6321890473
51UbiquitinationLAAQFIPKFFKHFPE
HHHHHHHHHHHHCHH		59.6321890473
51UbiquitinationLAAQFIPKFFKHFPE
HHHHHHHHHHHHCHH		59.6321890473
51AcetylationLAAQFIPKFFKHFPE
HHHHHHHHHHHHCHH		59.6325953088
51 (in isoform 3)Ubiquitination-59.6321890473
51 (in isoform 4)Ubiquitination-59.6321890473
51 (in isoform 2)Ubiquitination-59.6321890473
54UbiquitinationQFIPKFFKHFPELAD
HHHHHHHHHCHHHHH		47.68-
73UbiquitinationAQLDLCEDEDVSIRR
HHHHHCCCCCHHHHH		57.30-
84 (in isoform 4)Ubiquitination-57.1021890473
84 (in isoform 2)Ubiquitination-57.1021890473
84UbiquitinationSIRRQAIKELPQFAT
HHHHHHHHHCHHHCC		57.1021890473
84UbiquitinationSIRRQAIKELPQFAT
HHHHHHHHHCHHHCC		57.1021890473
84 (in isoform 1)Ubiquitination-57.1021890473
84 (in isoform 3)Ubiquitination-57.1021890473
84UbiquitinationSIRRQAIKELPQFAT
HHHHHHHHHCHHHCC		57.102189047
123PhosphorylationLVNNALLSIFKMDAK
HHHHHHHHHHCCCCC		27.1624719451
142UbiquitinationGLFSQILQGEDIVRE
HHHHHHHCCCHHHHH		55.66-
153AcetylationIVRERAIKFLSTKLK
HHHHHHHHHHHHHHC		38.9926051181
1532-HydroxyisobutyrylationIVRERAIKFLSTKLK
HHHHHHHHHHHHHHC		38.99-
153UbiquitinationIVRERAIKFLSTKLK
HHHHHHHHHHHHHHC		38.99-
158AcetylationAIKFLSTKLKTLPDE
HHHHHHHHHCCCCHH		44.6125953088
1582-HydroxyisobutyrylationAIKFLSTKLKTLPDE
HHHHHHHHHCCCCHH		44.61-
160 (in isoform 2)Ubiquitination-49.96-
177PhosphorylationEVEELILTESKKVLE
HHHHHHHHCCCHHHH		31.0821406692
179PhosphorylationEELILTESKKVLEDV
HHHHHHCCCHHHHHC		32.3220068231
1802-HydroxyisobutyrylationELILTESKKVLEDVT
HHHHHCCCHHHHHCC		40.44-
197AcetylationEFVLFMKILSGLKSL
HHHHHHHHHHCCCCC		2.1919608861
2022-HydroxyisobutyrylationMKILSGLKSLQTVSG
HHHHHCCCCCCCCCC		53.28-
250PhosphorylationRQAVPLFSKNVHSTR
HHHHHHHCCCCCCHH		30.8824719451
251AcetylationQAVPLFSKNVHSTRF
HHHHHHCCCCCCHHH		56.5122334682
3642-HydroxyisobutyrylationLPDFLTAKLNAEKLK
CCHHHHHHCCHHHHC		36.72-
3692-HydroxyisobutyrylationTAKLNAEKLKDFKIR
HHHCCHHHHCCHHHH		59.43-
374AcetylationAEKLKDFKIRLQYFA
HHHHCCHHHHHHHHH		36.7326051181
3982-HydroxyisobutyrylationLRLALQGKTGEALKT
HHHHHCCCCCCCCCC		40.16-
399PhosphorylationRLALQGKTGEALKTE
HHHHCCCCCCCCCCC		47.2624732914
409AcetylationALKTEENKIKVVALK
CCCCCCCCEEEEEEE		47.3825953088
417 (in isoform 1)Phosphorylation-5.3217081983
431 (in isoform 5)Phosphorylation-4.1525159151
433UbiquitinationKDLFHIPPSYKSTVT
HHHHCCCCCCCCEEE		50.0821890473
434 (in isoform 5)Phosphorylation-39.5828152594
435 (in isoform 5)Phosphorylation-18.0928152594
443 (in isoform 5)Phosphorylation-16.4528796482
444AcetylationSTVTLSWKPVQKVEI
CEEEEEEEEEEEEEC		31.7526051181
446 (in isoform 5)Phosphorylation-8.3625159151
448AcetylationLSWKPVQKVEIGQKR
EEEEEEEEEECCCEE		41.9125953088
454AcetylationQKVEIGQKRASEDTT
EEEECCCEECCCCCC		44.7225953088
4542-HydroxyisobutyrylationQKVEIGQKRASEDTT
EEEECCCEECCCCCC		44.72-
457PhosphorylationEIGQKRASEDTTSGS
ECCCEECCCCCCCCC		39.7823927012
460PhosphorylationQKRASEDTTSGSPPK
CEECCCCCCCCCCCC		20.8630266825
461PhosphorylationKRASEDTTSGSPPKK
EECCCCCCCCCCCCC		43.3330266825
462PhosphorylationRASEDTTSGSPPKKS
ECCCCCCCCCCCCCC		39.0929255136
464PhosphorylationSEDTTSGSPPKKSSA
CCCCCCCCCCCCCCC		37.4829255136
469PhosphorylationSGSPPKKSSAGPKRD
CCCCCCCCCCCCCCC		31.3926074081
470PhosphorylationGSPPKKSSAGPKRDA
CCCCCCCCCCCCCCH		46.2330576142
4742-HydroxyisobutyrylationKKSSAGPKRDARQIY
CCCCCCCCCCHHHHC		63.09-
481PhosphorylationKRDARQIYNPPSGKY
CCCHHHHCCCCCCCC		17.1828152594
485PhosphorylationRQIYNPPSGKYSSNL
HHHCCCCCCCCCCCC		49.5322199227
485 (in isoform 2)Phosphorylation-49.5325159151
487MethylationIYNPPSGKYSSNLGN
HCCCCCCCCCCCCCC		46.42-
487UbiquitinationIYNPPSGKYSSNLGN
HCCCCCCCCCCCCCC		46.42-
487 (in isoform 2)Ubiquitination-46.4221890473
487AcetylationIYNPPSGKYSSNLGN
HCCCCCCCCCCCCCC		46.4226051181
488 (in isoform 2)Phosphorylation-22.3628152594
489 (in isoform 2)Phosphorylation-19.0828152594
489PhosphorylationNPPSGKYSSNLGNFN
CCCCCCCCCCCCCCC		19.0817081983
497 (in isoform 2)Phosphorylation-14.8628796482
500 (in isoform 2)Phosphorylation-26.8525159151
500MethylationGNFNYEQRGAFRGSR
CCCCHHHCCCCCCCC		26.8524129315
500DimethylationGNFNYEQRGAFRGSR
CCCCHHHCCCCCCCC		26.85-
504MethylationYEQRGAFRGSRGGRG
HHHCCCCCCCCCCCC		41.46-
504DimethylationYEQRGAFRGSRGGRG
HHHCCCCCCCCCCCC		41.46-
507MethylationRGAFRGSRGGRGWGT
CCCCCCCCCCCCCCC		55.18-
507DimethylationRGAFRGSRGGRGWGT
CCCCCCCCCCCCCCC		55.18-
510MethylationFRGSRGGRGWGTRGN
CCCCCCCCCCCCCCC		40.28-
510DimethylationFRGSRGGRGWGTRGN
CCCCCCCCCCCCCCC		40.28-
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 API5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
251KAcetylation

22334682
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 API5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EBP2_HUMANEBNA1BP2physical
22939629
DDX27_HUMANDDX27physical
22939629
5NTC_HUMANNT5C2physical
22863883
NUBP1_HUMANNUBP1physical
22863883
OXSR1_HUMANOXSR1physical
22863883
DX39A_HUMANDDX39Aphysical
26344197
IF6_HUMANEIF6physical
26344197
IMDH2_HUMANIMPDH2physical
26344197
OSGEP_HUMANOSGEPphysical
26344197
TBC23_HUMANTBC1D23physical
26344197
TTI1_HUMANTTI1physical
26344197
XRN2_HUMANXRN2physical
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 API5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules.";
Han B.G., Kim K.H., Lee S.J., Jeong K.C., Cho J.W., Noh K.H.,Kim T.W., Kim S.J., Yoon H.J., Suh S.W., Lee S., Lee B.I.;
J. Biol. Chem. 0:0-0(2012).
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-498 OF WILD-TYPE AND MUTANTGLN-251, NUCLEAR LOCALIZATION SIGNAL, ACETYLATION AT LYS-251, REPEATS,AND SUBUNIT.
"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-251, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-28 AND SER-464, AND MASSSPECTROMETRY.
"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-464, AND MASSSPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND MASSSPECTROMETRY.

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