P07355

PTMD Annotation Information

※ Protein Information

Tag	Content
UniProt Accession	ANXA2_HUMAN; P07355;
Entrez ID	302
GenBank Protein ID	NM_001002857.1; NM_001002858.2; NM_001136015.2; NM_004039.2; XM_017022090.1; XM_017022091.1;
GenBank Nucleotide ID	NP_001002857.1; NP_001002858.1; NP_001129487.1; NP_004030.1; XP_016877579.1; XP_016877580.1;
Protein Name	Annexin A2 (Annexin II) (Annexin-2) (Calpactin I heavy chain) (Calpactin-1 heavy chain) (Chromobindin-8) (Lipocortin II) (Placental anticoagulant protein IV) (PAP-IV) (Protein I) (p36)
Gene Name	ANXA2; ANX2; ANX2L4; CAL1H; LPC2D
Organism	Homo sapiens
NCBI Taxa ID	9606
Functional Description	Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:18799458, PubMed:24808179, PubMed:22848640). Functional Description Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:18799458, PubMed:24808179, PubMed:22848640).
Sequence (Fasta)	MSTVHEILCK LSLEGDHSTP PSAYGSVKAY TNFDAERDAL NIETAIKTKG VDEVTIVNIL 60 TNRSNAQRQD IAFAYQRRTK KELASALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG 120 LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDII SDTSGDFRKL MVALAKGRRA 180 EDGSVIDYEL IDQDARDLYD AGVKRKGTDV PKWISIMTER SVPHLQKVFD RYKSYSPYDM 240 LESIRKEVKG DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM 300 LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD Fasta Sequence >P07355\|ANXA2; ANX2; ANX2L4; CAL1H; LPC2D\|Homo sapiens (Human) MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNAQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD

※ PTM-Disease Association

Num	PTM	Disease	Cell Type	Type	PTM Site	PMID
1	Phosphorylation	Hepatocellular carcinoma/Hepatocarcinoma/Hepatoma		U		7542850
1	[Reference]: These studies suggest that one possible mechanism of ethanol inhibitory effect on cell proliferation is through reduced TP of putative intracellular signal transduction molecules, such as p36 and IRS-1.
2	Tyrosine Phosphorylation	Breast cancer/tumor/carcinoma	SK-BR-3 Cell	P	Y24	23691485
2	[Reference]: Tyrosine 23 Phosphorylation of Annexin A2 Promotes Proliferation, Invasion, and Stat3 Phosphorylation in the Nucleus of Human Breast Cancer SK-BR-3 Cells
3	Tyrosine Phosphorylation	Pancreatic cancer/carcinoma/adenocarcinoma		P	Y24	21572519
3	[Reference]: Tyrosine 23 phosphorylation-dependent cell-surface localization of annexin A2 is required for invasion and metastases of pancreatic cancer

※ Disease Cross-ref Annotation

Database	Annotation
CTD (Curated) (count: 12) (view all)	MESH:D002294 ; Carcinoma, Squamous Cell MESH:D056486 ; Chemical and Drug Induced Liver Injury MESH:D015470 ; Leukemia, Myeloid, Acute MESH:D008106 ; Liver Cirrhosis, Experimental MESH:D008113 ; Liver Neoplasms MESH:D008175 ; Lung Neoplasms MESH:D015674 ; Mammary Neoplasms, Animal MESH:C562839 ; Mesothelioma, Malignant MESH:D009062 ; Mouth Neoplasms MESH:D009361 ; Neoplasm Invasiveness MESH:D010024 ; Osteoporosis MESH:D015430 ; Weight Gain
DisGeNet (Curated) (count: 12) (view all)	C0007137; Squamous cell carcinoma C0023467; Leukemia, Myelocytic, Acute C0023893; Liver Cirrhosis, Experimental C0023903; Liver neoplasms C0024121; Lung Neoplasms C0024667; Animal Mammary Neoplasms C0026640; Mouth Neoplasms C0027626; Neoplasm Invasiveness C0029456; Osteoporosis C0043094; Weight Gain C0345967; Malignant mesothelioma C4277682; Chemical and Drug Induced Liver Injury
GWASdb (count: 6)	rs11629852; Gamma gluatamyl transferase levels (interaction with age); alcohol abuse\|liver disease rs6494194; Intracerebral hemorrhage; cerebrovascular disease rs12595605; Intracerebral hemorrhage; cerebrovascular disease rs12593075; Intracerebral hemorrhage; cerebrovascular disease rs4774359; Intracerebral hemorrhage; cerebrovascular disease rs3743268; Multiple complex diseases; Null

※ PTM Sites

PTM	Modification Sites
Phosphorylation (count: 27) (view all)	109 LLKTPAQYDASELKA dbPAF 12 HEILCKLSLEGDHST dbPAF 123 ASMKGLGTDEDSLIE dbPAF 127 GLGTDEDSLIEIICS dbPAF 147 LQEINRVYKEMYKTD dbPAF 153 VYKEMYKTDLEKDII dbPAF 18 LSLEGDHSTPPSAYG dbPAF 184 GRRAEDGSVIDYELI dbPAF 188 EDGSVIDYELIDQDA dbPAF 19 SLEGDHSTPPSAYGS dbPAF 199 DQDARDLYDAGVKRK dbPAF 2 ****MSTVHEILC dbPAF 22 GDHSTPPSAYGSVKA dbPAF 235 VFDRYKSYSPYDMLE dbPAF 238 RYKSYSPYDMLESIR dbPAF 24 HSTPPSAYGSVKAYT dbPAF 26 TPPSAYGSVKAYTNF dbPAF 275 LYFADRLYDSMKGKG dbPAF 3 ***MSTVHEILCK dbPAF 30 AYGSVKAYTNFDAER dbPAF 316 RKYGKSLYYYIQQDT dbPAF 317 KYGKSLYYYIQQDTK dbPAF 318 YGKSLYYYIQQDTKG dbPAF 55 TKGVDEVTIVNILTN dbPAF 61 VTIVNILTNRSNAQR dbPAF 75 RQDIAFAYQRRTKKE dbPAF 85 RTKKELASALKSALS dbPAF
Acetylation (count: 22) (view all)	10 TVHEILCKLSLEGDH PLMD 104 TVILGLLKTPAQYDA PLMD 115 QYDASELKASMKGLG PLMD 119 SELKASMKGLGTDED PLMD 148 QEINRVYKEMYKTDL PLMD 152 RVYKEMYKTDLEKDI PLMD 157 MYKTDLEKDIISDTS PLMD 176 KLMVALAKGRRAEDG PLMD 204 DLYDAGVKRKGTDVP PLMD 212 RKGTDVPKWISIMTE PLMD 227 RSVPHLQKVFDRYKS PLMD 233 QKVFDRYKSYSPYDM PLMD 266 LVQCIQNKPLYFADR PLMD 279 DRLYDSMKGKGTRDK PLMD 28 PSAYGSVKAYTNFDA PLMD 302 RSEVDMLKIRSEFKR PLMD 310 IRSEFKRKYGKSLYY PLMD 313 EFKRKYGKSLYYYIQ PLMD 324 YYIQQDTKGDYQKAL PLMD 329 DTKGDYQKALLYLCG PLMD 47 LNIETAIKTKGVDEV PLMD 49 IETAIKTKGVDEVTI PLMD
Ubiquitination (count: 24) (view all)	10 TVHEILCKLSLEGDH PLMD 104 TVILGLLKTPAQYDA PLMD 115 QYDASELKASMKGLG PLMD 119 SELKASMKGLGTDED PLMD 148 QEINRVYKEMYKTDL PLMD 152 RVYKEMYKTDLEKDI PLMD 157 MYKTDLEKDIISDTS PLMD 169 DTSGDFRKLMVALAK PLMD 176 KLMVALAKGRRAEDG PLMD 204 DLYDAGVKRKGTDVP PLMD 212 RKGTDVPKWISIMTE PLMD 227 RSVPHLQKVFDRYKS PLMD 233 QKVFDRYKSYSPYDM PLMD 266 LVQCIQNKPLYFADR PLMD 279 DRLYDSMKGKGTRDK PLMD 28 PSAYGSVKAYTNFDA PLMD 281 LYDSMKGKGTRDKVL PLMD 302 RSEVDMLKIRSEFKR PLMD 313 EFKRKYGKSLYYYIQ PLMD 324 YYIQQDTKGDYQKAL PLMD 329 DTKGDYQKALLYLCG PLMD 47 LNIETAIKTKGVDEV PLMD 49 IETAIKTKGVDEVTI PLMD 81 AYQRRTKKELASALK PLMD
Sumoylation (count: 5)	10 TVHEILCKLSLEGDH PLMD 157 MYKTDLEKDIISDTS PLMD 204 DLYDAGVKRKGTDVP PLMD 324 YYIQQDTKGDYQKAL PLMD 49 IETAIKTKGVDEVTI PLMD
Malonylation (count: 19) (view all)	115 QYDASELKASMKGLG PLMD 119 SELKASMKGLGTDED PLMD 148 QEINRVYKEMYKTDL PLMD 152 RVYKEMYKTDLEKDI PLMD 157 MYKTDLEKDIISDTS PLMD 169 DTSGDFRKLMVALAK PLMD 176 KLMVALAKGRRAEDG PLMD 204 DLYDAGVKRKGTDVP PLMD 227 RSVPHLQKVFDRYKS PLMD 233 QKVFDRYKSYSPYDM PLMD 279 DRLYDSMKGKGTRDK PLMD 302 RSEVDMLKIRSEFKR PLMD 310 IRSEFKRKYGKSLYY PLMD 313 EFKRKYGKSLYYYIQ PLMD 324 YYIQQDTKGDYQKAL PLMD 47 LNIETAIKTKGVDEV PLMD 49 IETAIKTKGVDEVTI PLMD 80 FAYQRRTKKELASAL PLMD 81 AYQRRTKKELASALK PLMD
Succinylation (count: 9) (view all)	115 QYDASELKASMKGLG PLMD 119 SELKASMKGLGTDED PLMD 148 QEINRVYKEMYKTDL PLMD 152 RVYKEMYKTDLEKDI PLMD 157 MYKTDLEKDIISDTS PLMD 176 KLMVALAKGRRAEDG PLMD 204 DLYDAGVKRKGTDVP PLMD 227 RSVPHLQKVFDRYKS PLMD 313 EFKRKYGKSLYYYIQ PLMD

※ Protein-Protein Interaction

Network

Interaction

A

B

Source

P03372	P07355	IntAct
P07355	P07858	HPRD
P07355	P12004	MINT
P07355	P12931	HPRD
P07355	P16104	IntAct
P07355	P17252	HPRD
P07355	P40337	IntAct
P07355	P40692	IntAct
P07355	Q14164	IntAct
P07355	Q9Y4K3	IntAct