P06748

PTMD Annotation Information

※ Protein Information

Tag	Content
UniProt Accession	NPM_HUMAN; P06748;
Entrez ID	4869
GenBank Protein ID	NM_001037738.2; NM_002520.6; NM_199185.3;
GenBank Nucleotide ID	NP_001032827.1; NP_002511.1; NP_954654.1;
Protein Name	Nucleophosmin (NPM) (Nucleolar phosphoprotein B23) (Nucleolar protein NO38) (Numatrin)
Gene Name	NPM1; NPM
Organism	Homo sapiens
NCBI Taxa ID	9606
Functional Description	Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity o(view all) Functional Description Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade (PubMed:22528486). In complex with MYC enhances the transcription of MYC target genes (PubMed:25956029).
Sequence (Fasta)	MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV 60 EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE 120 EDAESEDEEE EDVKLLSISG KRSAPGGGSK VPQKKVKLAA DEDDDDDDEE DDDEDDDDDD 180 FDDEEAEEKA PVKKSIRDTP AKNAQKSNQN GKDSKPSSTP RSKGQESFKK QEKTPKTPKG 240 PSSVEDIKAK MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL 295 Fasta Sequence >P06748\|NPM1; NPM\|Homo sapiens (Human) MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEEEEDVKLLSISGKRSAPGGGSKVPQKKVKLAADEDDDDDDEEDDDEDDDDDDFDDEEAEEKAPVKKSIRDTPAKNAQKSNQNGKDSKPSSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL

※ PTM-Disease Association

Num	PTM	Disease	Cell Type	Type	PTM Site	PMID
1	Threonine Phosphorylation	Prostate cancer/carcinoma/adenocarcinoma		U	T199	26993766
1	[Reference]: In this study, we first investigated the implication of the NPM1 and its Thr199 and Thr234/237 phosphorylated forms in PCa. We showed that phosphorylated forms of NPM1 interact with androgen receptor (AR) in nucleoplasm.
2	Threonine Phosphorylation	Kaposi's sarcoma		U	T199	20333249
2	[Reference]: Our study demonstrates that the KSHV v-cyclin and cellular CDK6 kinase phosphorylate NPM on threonine 199 (Thr199) in de novo and naturally KSHV-infected cells and that NPM is phosphorylated to the same site in primary KS tumors.
3	Threonine Phosphorylation	Prostate cancer/carcinoma/adenocarcinoma		U	T234	26993766
3	[Reference]: In this study, we first investigated the implication of the NPM1 and its Thr199 and Thr234/237 phosphorylated forms in PCa. We showed that phosphorylated forms of NPM1 interact with androgen receptor (AR) in nucleoplasm.?
4	Threonine Phosphorylation	Hepatocellular carcinoma/Hepatocarcinoma/Hepatoma		U	T234	26536659
4	[Reference]: Phosphorylation of nucleophosmin at threonine 234/237 is associated with HCC metastasis.
5	Threonine Phosphorylation	Prostate cancer/carcinoma/adenocarcinoma		U	T237	26993766
5	[Reference]: In this study, we first investigated the implication of the NPM1 and its Thr199 and Thr234/237 phosphorylated forms in PCa. We showed that phosphorylated forms of NPM1 interact with androgen receptor (AR) in nucleoplasm.?
6	Threonine Phosphorylation	Hepatocellular carcinoma/Hepatocarcinoma/Hepatoma		U	T237	26536659
6	[Reference]: Phosphorylation of nucleophosmin at threonine 234/237 is associated with HCC metastasis.

※ Disease Cross-ref Annotation

Database	Annotation
Cancer Gene Census	NHL, APL, AML
CTD (Curated) (count: 3)	MESH:D015470 ; Leukemia, Myeloid, Acute MESH:D015473 ; Leukemia, Promyelocytic, Acute MESH:D013274 ; Stomach Neoplasms

※ PTM Sites

PTM	Modification Sites
Phosphorylation (count: 38) (view all)	10 DSMDMDMSPLRPQNY dbPAF 106 VLRLKCGSGPVHISG dbPAF 112 GSGPVHISGQHLVAV dbPAF 125 AVEEDAESEDEEEED dbPAF 137 EEDVKLLSISGKRSA dbPAF 139 DVKLLSISGKRSAPG dbPAF 143 LSISGKRSAPGGGSK dbPAF 17 SPLRPQNYLFGCELK dbPAF 195 EKAPVKKSIRDTPAK dbPAF 199 VKKSIRDTPAKNAQK dbPAF 207 PAKNAQKSNQNGKDS dbPAF 214 SNQNGKDSKPSSTPR dbPAF 217 NGKDSKPSSTPRSKG dbPAF 218 GKDSKPSSTPRSKGQ dbPAF 219 KDSKPSSTPRSKGQE dbPAF 222 KPSSTPRSKGQESFK dbPAF 227 PRSKGQESFKKQEKT dbPAF 234 SFKKQEKTPKTPKGP dbPAF 237 KQEKTPKTPKGPSSV dbPAF 242 PKTPKGPSSVEDIKA dbPAF 243 KTPKGPSSVEDIKAK dbPAF 254 IKAKMQASIEKGGSL dbPAF 260 ASIEKGGSLPKVEAK dbPAF 279 VKNCFRMTDQEAIQD dbPAF 29 ELKADKDYHFKVDND dbPAF 293 DLWQWRKSL**** dbPAF 4 **MEDSMDMDMSP dbPAF 43 DENEHQLSLRTVSLG dbPAF 46 EHQLSLRTVSLGAGA dbPAF 48 QLSLRTVSLGAGAKD dbPAF 67 VEAEAMNYEGSPIKV dbPAF 70 EAMNYEGSPIKVTLA dbPAF 75 EGSPIKVTLATLKMS dbPAF 78 PIKVTLATLKMSVQP dbPAF 82 TLATLKMSVQPTVSL dbPAF 86 LKMSVQPTVSLGGFE dbPAF 88 MSVQPTVSLGGFEIT dbPAF 95 SLGGFEITPPVVLRL dbPAF
Acetylation (count: 25) (view all)	141 KLLSISGKRSAPGGG PLMD 150 SAPGGGSKVPQKKVK PLMD 154 GGSKVPQKKVKLAAD PLMD 157 KVPQKKVKLAADEDD PLMD 189 DDEEAEEKAPVKKSI PLMD 193 AEEKAPVKKSIRDTP PLMD 202 SIRDTPAKNAQKSNQ PLMD 212 QKSNQNGKDSKPSST PLMD 215 NQNGKDSKPSSTPRS PLMD 223 PSSTPRSKGQESFKK PLMD 229 SKGQESFKKQEKTPK PLMD 230 KGQESFKKQEKTPKT PLMD 239 EKTPKTPKGPSSVED PLMD 24 YLFGCELKADKDYHF PLMD 248 PSSVEDIKAKMQASI PLMD 250 SVEDIKAKMQASIEK PLMD 257 KMQASIEKGGSLPKV PLMD 263 EKGGSLPKVEAKFIN PLMD 267 SLPKVEAKFINYVKN PLMD 27 GCELKADKDYHFKVD PLMD 273 AKFINYVKNCFRMTD PLMD 292 QDLWQWRKSL***** PLMD 32 ADKDYHFKVDNDENE PLMD 54 VSLGAGAKDELHIVE PLMD 73 NYEGSPIKVTLATLK PLMD
Ubiquitination (count: 20) (view all)	141 KLLSISGKRSAPGGG PLMD 155 GSKVPQKKVKLAADE PLMD 157 KVPQKKVKLAADEDD PLMD 189 DDEEAEEKAPVKKSI PLMD 193 AEEKAPVKKSIRDTP PLMD 202 SIRDTPAKNAQKSNQ PLMD 215 NQNGKDSKPSSTPRS PLMD 229 SKGQESFKKQEKTPK PLMD 239 EKTPKTPKGPSSVED PLMD 248 PSSVEDIKAKMQASI PLMD 250 SVEDIKAKMQASIEK PLMD 257 KMQASIEKGGSLPKV PLMD 263 EKGGSLPKVEAKFIN PLMD 267 SLPKVEAKFINYVKN PLMD 27 GCELKADKDYHFKVD PLMD 273 AKFINYVKNCFRMTD PLMD 32 ADKDYHFKVDNDENE PLMD 54 VSLGAGAKDELHIVE PLMD 73 NYEGSPIKVTLATLK PLMD 80 KVTLATLKMSVQPTV PLMD
Sumoylation (count: 25) (view all)	134 DEEEEDVKLLSISGK PLMD 141 KLLSISGKRSAPGGG PLMD 150 SAPGGGSKVPQKKVK PLMD 154 GGSKVPQKKVKLAAD PLMD 155 GSKVPQKKVKLAADE PLMD 157 KVPQKKVKLAADEDD PLMD 189 DDEEAEEKAPVKKSI PLMD 194 EEKAPVKKSIRDTPA PLMD 202 SIRDTPAKNAQKSNQ PLMD 206 TPAKNAQKSNQNGKD PLMD 212 QKSNQNGKDSKPSST PLMD 215 NQNGKDSKPSSTPRS PLMD 223 PSSTPRSKGQESFKK PLMD 229 SKGQESFKKQEKTPK PLMD 230 KGQESFKKQEKTPKT PLMD 233 ESFKKQEKTPKTPKG PLMD 236 KKQEKTPKTPKGPSS PLMD 239 EKTPKTPKGPSSVED PLMD 248 PSSVEDIKAKMQASI PLMD 250 SVEDIKAKMQASIEK PLMD 257 KMQASIEKGGSLPKV PLMD 263 EKGGSLPKVEAKFIN PLMD 267 SLPKVEAKFINYVKN PLMD 27 GCELKADKDYHFKVD PLMD 32 ADKDYHFKVDNDENE PLMD
Malonylation (count: 5)	141 KLLSISGKRSAPGGG PLMD 239 EKTPKTPKGPSSVED PLMD 257 KMQASIEKGGSLPKV PLMD 273 AKFINYVKNCFRMTD PLMD 32 ADKDYHFKVDNDENE PLMD
Succinylation (count: 8) (view all)	141 KLLSISGKRSAPGGG PLMD 212 QKSNQNGKDSKPSST PLMD 229 SKGQESFKKQEKTPK PLMD 239 EKTPKTPKGPSSVED PLMD 248 PSSVEDIKAKMQASI PLMD 267 SLPKVEAKFINYVKN PLMD 27 GCELKADKDYHFKVD PLMD 273 AKFINYVKNCFRMTD PLMD

※ Protein-Protein Interaction

Network

Interaction

A

B

Source

P03372	P06748	IntAct
P04637	P06748	HPRD; IntAct; MINT;IntAct
P06493	P06748	HPRD
P06748	P09874	HPRD
P06748	P19525	HPRD; MINT
P06748	P35568	HPRD
P06748	P53350	HPRD
P06748	P62805	IntAct
P06748	P68431	DIP
P06748	Q04206	IntAct
P06748	Q14164	IntAct
P06748	Q8N726	IntAct; MINT
P06748	Q9UM73	HPRD
P06748	Q9Y4K3	IntAct