B3A2_HUMAN - dbPTM
B3A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID B3A2_HUMAN
UniProt AC P04920
Protein Name Anion exchange protein 2
Gene Name SLC4A2
Organism Homo sapiens (Human).
Sequence Length 1241
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Plasma membrane anion exchange protein of wide distribution..
Protein Sequence MSSAPRRPAKGADSFCTPEPESLGPGTPGFPEQEEDELHRTLGVERFEEILQEAGSRGGEEPGRSYGEEDFEYHRQSSHHIHHPLSTHLPPDARRRKTPQGPGRKPRRRPGASPTGETPTIEEGEEDEDEASEAEGARALTQPSPVSTPSSVQFFLQEDDSADRKAERTSPSSPAPLPHQEATPRASKGAQAGTQVEEAEAEAVAVASGTAGGDDGGASGRPLPKAQPGHRSYNLQERRRIGSMTGAEQALLPRVPTDEIEAQTLATADLDLMKSHRFEDVPGVRRHLVRKNAKGSTQSGREGREPGPTPRARPRAPHKPHEVFVELNELLLDKNQEPQWRETARWIKFEEDVEEETERWGKPHVASLSFRSLLELRRTLAHGAVLLDLDQQTLPGVAHQVVEQMVISDQIKAEDRANVLRALLLKHSHPSDEKDFSFPRNISAGSLGSLLGHHHGQGAESDPHVTEPLMGGVPETRLEVERERELPPPAPPAGITRSKSKHELKLLEKIPENAEATVVLVGCVEFLSRPTMAFVRLREAVELDAVLEVPVPVRFLFLLLGPSSANMDYHEIGRSISTLMSDKQFHEAAYLADEREDLLTAINAFLDCSVVLPPSEVQGEELLRSVAHFQRQMLKKREEQGRLLPTGAGLEPKSAQDKALLQMVEAAGAAEDDPLRRTGRPFGGLIRDVRRRYPHYLSDFRDALDPQCLAAVIFIYFAALSPAITFGGLLGEKTQDLIGVSELIMSTALQGVVFCLLGAQPLLVIGFSGPLLVFEEAFFSFCSSNHLEYLVGRVWIGFWLVFLALLMVALEGSFLVRFVSRFTQEIFAFLISLIFIYETFYKLVKIFQEHPLHGCSASNSSEVDGGENMTWAGARPTLGPGNRSLAGQSGQGKPRGQPNTALLSLVLMAGTFFIAFFLRKFKNSRFFPGRIRRVIGDFGVPIAILIMVLVDYSIEDTYTQKLSVPSGFSVTAPEKRGWVINPLGEKSPFPVWMMVASLLPAILVFILIFMETQITTLIISKKERMLQKGSGFHLDLLLIVAMGGICALFGLPWLAAATVRSVTHANALTVMSKAVAPGDKPKIQEVKEQRVTGLLVALLVGLSIVIGDLLRQIPLAVLFGIFLYMGVTSLNGIQFYERLHLLLMPPKHHPDVTYVKKVRTLRMHLFTALQLLCLALLWAVMSTAASLAFPFILILTVPLRMVVLTRIFTDREMKCLDANEAEPVFDEREGVDEYNEMPMPV
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
14PhosphorylationRPAKGADSFCTPEPE
CCCCCCCCCCCCCHH		22.9928348404
17PhosphorylationKGADSFCTPEPESLG
CCCCCCCCCCHHHCC		28.7728348404
22PhosphorylationFCTPEPESLGPGTPG
CCCCCHHHCCCCCCC		49.7128348404
27PhosphorylationPESLGPGTPGFPEQE
HHHCCCCCCCCCHHH		24.3025159151
56PhosphorylationEILQEAGSRGGEEPG
HHHHHHHHCCCCCCC		34.5021815630
57MethylationILQEAGSRGGEEPGR
HHHHHHHCCCCCCCC		57.10115917125
65PhosphorylationGGEEPGRSYGEEDFE
CCCCCCCCCCHHHHH		43.3225884760
66PhosphorylationGEEPGRSYGEEDFEY
CCCCCCCCCHHHHHH		27.4825884760
72PhosphorylationSYGEEDFEYHRQSSH
CCCHHHHHHHHCCCC		53.3917389395
73PhosphorylationYGEEDFEYHRQSSHH
CCHHHHHHHHCCCCC		11.4221082442
77PhosphorylationDFEYHRQSSHHIHHP
HHHHHHCCCCCCCCC		31.4329449344
78PhosphorylationFEYHRQSSHHIHHPL
HHHHHCCCCCCCCCH		15.6729449344
86PhosphorylationHHIHHPLSTHLPPDA
CCCCCCHHHCCCCCH		20.4529449344
87PhosphorylationHIHHPLSTHLPPDAR
CCCCCHHHCCCCCHH		34.8129449344
113PhosphorylationPRRRPGASPTGETPT
CCCCCCCCCCCCCCC		28.9826503892
115PhosphorylationRRPGASPTGETPTIE
CCCCCCCCCCCCCCC		45.1929255136
118PhosphorylationGASPTGETPTIEEGE
CCCCCCCCCCCCCCC		27.3829255136
120PhosphorylationSPTGETPTIEEGEED
CCCCCCCCCCCCCCC		48.7329255136
132PhosphorylationEEDEDEASEAEGARA
CCCHHHHHHHHHHHH		34.9826503892
141PhosphorylationAEGARALTQPSPVST
HHHHHHHCCCCCCCC		37.1329255136
144PhosphorylationARALTQPSPVSTPSS
HHHHCCCCCCCCCCH		28.2828355574
147PhosphorylationLTQPSPVSTPSSVQF
HCCCCCCCCCCHHHE		37.6829255136
148PhosphorylationTQPSPVSTPSSVQFF
CCCCCCCCCCHHHEE		27.6829255136
150PhosphorylationPSPVSTPSSVQFFLQ
CCCCCCCCHHHEEEC		43.1428176443
151PhosphorylationSPVSTPSSVQFFLQE
CCCCCCCHHHEEECC		22.5728176443
161PhosphorylationFFLQEDDSADRKAER
EEECCCCCCCHHHHH		44.3720068231
169PhosphorylationADRKAERTSPSSPAP
CCHHHHHCCCCCCCC		36.1729255136
170PhosphorylationDRKAERTSPSSPAPL
CHHHHHCCCCCCCCC		29.0729255136
172PhosphorylationKAERTSPSSPAPLPH
HHHHCCCCCCCCCCC		49.0429255136
173PhosphorylationAERTSPSSPAPLPHQ
HHHCCCCCCCCCCCC		28.5929255136
183PhosphorylationPLPHQEATPRASKGA
CCCCCCCCCCCCCCC		16.7425159151
187PhosphorylationQEATPRASKGAQAGT
CCCCCCCCCCCCCCC		32.6622468782
188UbiquitinationEATPRASKGAQAGTQ
CCCCCCCCCCCCCCC		58.23-
194PhosphorylationSKGAQAGTQVEEAEA
CCCCCCCCCHHHHHH		32.2420068231
219PhosphorylationGGDDGGASGRPLPKA
CCCCCCCCCCCCCCC		38.3120068231
232PhosphorylationKAQPGHRSYNLQERR
CCCCCCCCCCHHHHH		16.8228634120
233PhosphorylationAQPGHRSYNLQERRR
CCCCCCCCCHHHHHC		21.6125884760
243PhosphorylationQERRRIGSMTGAEQA
HHHHCHHCCCCHHHH		15.7025159151
244SulfoxidationERRRIGSMTGAEQAL
HHHCHHCCCCHHHHH		3.1921406390
245PhosphorylationRRRIGSMTGAEQALL
HHCHHCCCCHHHHHC		34.6328102081
257PhosphorylationALLPRVPTDEIEAQT
HHCCCCCCHHHHHHH		43.3327273156
264PhosphorylationTDEIEAQTLATADLD
CHHHHHHHHHHCCHH		25.9620068231
267PhosphorylationIEAQTLATADLDLMK
HHHHHHHHCCHHHHH		24.6627690223
274MethylationTADLDLMKSHRFEDV
HCCHHHHHHCCCCCC		50.8624129315
275PhosphorylationADLDLMKSHRFEDVP
CCHHHHHHCCCCCCC		13.1129449344
296PhosphorylationVRKNAKGSTQSGREG
HHHCCCCCCCCCCCC		23.6728102081
297PhosphorylationRKNAKGSTQSGREGR
HHCCCCCCCCCCCCC		35.1128102081
299PhosphorylationNAKGSTQSGREGREP
CCCCCCCCCCCCCCC		39.6524961811
301MethylationKGSTQSGREGREPGP
CCCCCCCCCCCCCCC		48.74-
309PhosphorylationEGREPGPTPRARPRA
CCCCCCCCCCCCCCC		31.1828102081
319UbiquitinationARPRAPHKPHEVFVE
CCCCCCCCCCHHHHH		47.19-
320 (in isoform 2)Ubiquitination-26.32-
334UbiquitinationLNELLLDKNQEPQWR
HHHHHHCCCCCCHHH		61.57-
334 (in isoform 2)Ubiquitination-61.57-
362UbiquitinationEETERWGKPHVASLS
HHHHHHCCCCHHHHH		25.62-
367PhosphorylationWGKPHVASLSFRSLL
HCCCCHHHHHHHHHH		24.3721406692
369PhosphorylationKPHVASLSFRSLLEL
CCCHHHHHHHHHHHH		19.0024719451
372PhosphorylationVASLSFRSLLELRRT
HHHHHHHHHHHHHHH		34.9821406692
426UbiquitinationVLRALLLKHSHPSDE
HHHHHHHHCCCCCCC		42.93-
434UbiquitinationHSHPSDEKDFSFPRN
CCCCCCCCCCCCCCC		69.89-
443PhosphorylationFSFPRNISAGSLGSL
CCCCCCCCCCHHHHH		30.0823927012
446PhosphorylationPRNISAGSLGSLLGH
CCCCCCCHHHHHHCC		29.3123927012
449PhosphorylationISAGSLGSLLGHHHG
CCCCHHHHHHCCCCC		26.2223927012
461PhosphorylationHHGQGAESDPHVTEP
CCCCCCCCCCCCCCC		56.7723927012
466PhosphorylationAESDPHVTEPLMGGV
CCCCCCCCCCCCCCC		28.9323927012
476PhosphorylationLMGGVPETRLEVERE
CCCCCCCCCCCCHHH		34.1920068231
500PhosphorylationAGITRSKSKHELKLL
CCCCCCCCHHHHHHH		40.2626074081
505UbiquitinationSKSKHELKLLEKIPE
CCCHHHHHHHHHCCC		48.30-
577PhosphorylationHEIGRSISTLMSDKQ
HHHHHHHHHHHCCHH		19.4127732954
578PhosphorylationEIGRSISTLMSDKQF
HHHHHHHHHHCCHHH		25.4727732954
581PhosphorylationRSISTLMSDKQFHEA
HHHHHHHCCHHHHHH		44.7827732954
636UbiquitinationFQRQMLKKREEQGRL
HHHHHHHHHHHHCCC		62.17-
639 (in isoform 2)Ubiquitination-63.4721906983
644 (in isoform 2)Ubiquitination-3.2521906983
653UbiquitinationTGAGLEPKSAQDKAL
CCCCCCCCCHHHHHH		49.3921906983
653 (in isoform 1)Ubiquitination-49.3922053931
654PhosphorylationGAGLEPKSAQDKALL
CCCCCCCCHHHHHHH		41.7123403867
658UbiquitinationEPKSAQDKALLQMVE
CCCCHHHHHHHHHHH		28.9322053931
658 (in isoform 1)Ubiquitination-28.9322053931
721PhosphorylationFIYFAALSPAITFGG
HHHHHHHCHHHHHCH		13.94-
725PhosphorylationAALSPAITFGGLLGE
HHHCHHHHHCHHCCH		20.52-
859N-linked_GlycosylationLHGCSASNSSEVDGG
CCCCCCCCCCCCCCC		49.63UniProtKB CARBOHYD
868N-linked_GlycosylationSEVDGGENMTWAGAR
CCCCCCCCCCCCCCC		36.14UniProtKB CARBOHYD
879 (in isoform 2)Ubiquitination-30.4621906983
882N-linked_GlycosylationRPTLGPGNRSLAGQS
CCCCCCCCCCCCCCC		33.24UniProtKB CARBOHYD
893UbiquitinationAGQSGQGKPRGQPNT
CCCCCCCCCCCCCCH		24.5321906983
893 (in isoform 1)Ubiquitination-24.5322053931
961 (in isoform 2)Ubiquitination-34.6221906983
975UbiquitinationFSVTAPEKRGWVINP
CCEECCCCCCEEECC		55.9721906983
975 (in isoform 1)Ubiquitination-55.9722053931
1059 (in isoform 2)Ubiquitination-3.5421906983
1073UbiquitinationNALTVMSKAVAPGDK
HHHHHHHHHCCCCCC		28.8721906983
1073 (in isoform 1)Ubiquitination-28.8722053931
1073 (in isoform 2)Ubiquitination-28.8721906983
1080UbiquitinationKAVAPGDKPKIQEVK
HHCCCCCCCCHHHHH		54.87-
1087UbiquitinationKPKIQEVKEQRVTGL
CCCHHHHHHHHHHHH		47.58-
1087 (in isoform 1)Ubiquitination-47.5822053931
1142 (in isoform 2)Ubiquitination-2.4021906983
1154PhosphorylationKHHPDVTYVKKVRTL
CCCCCCCHHHCHHHH		15.32-
1156UbiquitinationHPDVTYVKKVRTLRM
CCCCCHHHCHHHHHH		34.832190698
1156 (in isoform 1)Ubiquitination-34.8322053931
1173S-palmitoylationFTALQLLCLALLWAV
HHHHHHHHHHHHHHH		2.58-
1234PhosphorylationEREGVDEYNEMPMPV
CCCCCCCCCCCCCCC		16.3829978859
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 B3A2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of B3A2_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 B3A2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of B3A2_HUMAN !!
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 B3A2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND MASSSPECTROMETRY.
"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 SER-172, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-132; SER-170;SER-172; SER-173 AND THR-183, AND MASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-73, AND MASSSPECTROMETRY.

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