dbPTM

PRDM1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PRDM1_HUMAN
UniProt AC	O75626
Protein Name	PR domain zinc finger protein 1
Gene Name	PRDM1
Organism	Homo sapiens (Human).
Sequence Length	825
Subcellular Localization	Nucleus . Cytoplasm .
Protein Description	Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs. Plays a role in the development, retention and long-term establishment of adaptive and innate tissue-resident lymphocyte T cell types in non-lymphoid organs, such as the skin and gut, but also in other nonbarrier tissues like liver and kidney, and therefore may provide immediate immunological protection against reactivating infections or viral reinfection (By similarity). Binds specifically to the PRDI element in the promoter of the beta-interferon gene. [PubMed: 1851123 Drives the maturation of B-lymphocytes into Ig secreting cells]
Protein Sequence	MLDICLEKRVGTTLAAPKCNSSTVRFQGLAEGTKGTMKMDMEDADMTLWTEAEFEEKCTYIVNDHPWDSGADGGTSVQAEASLPRNLLFKYATNSEEVIGVMSKEYIPKGTRFGPLIGEIYTNDTVPKNANRKYFWRIYSRGELHHFIDGFNEEKSNWMRYVNPAHSPREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERLHYPYPGELTMMNLTQTQSSLKQPSTEKNELCPKNVPKREYSVKEILKLDSNPSKGKDLYRSNISPLTSEKDLDDFRRRGSPEMPFYPRVVYPIRAPLPEDFLKASLAYGIERPTYITRSPIPSSTTPSPSARSSPDQSLKSSSPHSSPGNTVSPVGPGSQEHRDSYAYLNASYGTEGLGSYPGYAPLPHLPPAFIPSYNAHYPKFLLPPYGMNCNGLSAVSSMNGINNFGLFPRLCPVYSNLLGGGSLPHPMLNPTSLPSSLPSDGARRLLQPEHPREVLVPAPHSAFSFTGAAASMKDKACSPTSGSPTAGTAATAEHVVQPKATSAAMAAPSSDEAMNLIKNKRNMTGYKTLPYPLKKQNGKIKYECNVCAKTFGQLSNLKVHLRVHSGERPFKCQTCNKGFTQLAHLQKHYLVHTGEKPHECQVCHKRFSSTSNLKTHLRLHSGEKPYQCKVCPAKFTQFVHLKLHKRLHTRERPHKCSQCHKNYIHLCSLKVHLKGNCAAAPAPGLPLEDLTRINEEIEKFDISDNADRLEDVEDDISVISVVEKEILAVVRKEKEETGLKVSLQRNMGNGLLSSGCSLYESSDLPLMKLPPSNPLPLVPVKVKQETVEPMDP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Phosphorylation	LAAPKCNSSTVRFQG EECCCCCCCCEEEEH	36.54	21712546
23	Phosphorylation	APKCNSSTVRFQGLA CCCCCCCCEEEEHHC	18.60	21712546
82	Phosphorylation	TSVQAEASLPRNLLF CCCCCEECCCCCHHH	30.34	24719451
140	Phosphorylation	KYFWRIYSRGELHHF CEEEEEEECCCHHHH	31.29	24719451
227	Phosphorylation	NLTQTQSSLKQPSTE ECHHCHHHCCCCCCC	29.75	-
248	Phosphorylation	KNVPKREYSVKEILK CCCCCCCCCHHHHHC	23.85	24505115
267	Phosphorylation	PSKGKDLYRSNISPL CCCCCCHHHCCCCCC	23.33	28258704
269	Phosphorylation	KGKDLYRSNISPLTS CCCCHHHCCCCCCCC	25.59	23312004
272	Phosphorylation	DLYRSNISPLTSEKD CHHHCCCCCCCCCCC	20.36	26657352
275	Phosphorylation	RSNISPLTSEKDLDD HCCCCCCCCCCCHHH	37.92	23312004
276	Phosphorylation	SNISPLTSEKDLDDF CCCCCCCCCCCHHHH	50.78	23312004
278	Ubiquitination	ISPLTSEKDLDDFRR CCCCCCCCCHHHHHH	64.46	-
288	Phosphorylation	DDFRRRGSPEMPFYP HHHHHCCCCCCCCCC	18.84	30108239
331	Phosphorylation	ITRSPIPSSTTPSPS EECCCCCCCCCCCCC	40.82	30108239
332	Phosphorylation	TRSPIPSSTTPSPSA ECCCCCCCCCCCCCC	30.83	30108239
333	Phosphorylation	RSPIPSSTTPSPSAR CCCCCCCCCCCCCCC	47.25	30108239
334	Phosphorylation	SPIPSSTTPSPSARS CCCCCCCCCCCCCCC	24.58	30108239
336	Phosphorylation	IPSSTTPSPSARSSP CCCCCCCCCCCCCCC	29.42	30108239
338	Phosphorylation	SSTTPSPSARSSPDQ CCCCCCCCCCCCCCC	40.42	30108239
341	Phosphorylation	TPSPSARSSPDQSLK CCCCCCCCCCCCCCC	46.03	26657352
342	Phosphorylation	PSPSARSSPDQSLKS CCCCCCCCCCCCCCC	27.26	30108239
346	Phosphorylation	ARSSPDQSLKSSSPH CCCCCCCCCCCCCCC	45.18	30108239
349	Phosphorylation	SPDQSLKSSSPHSSP CCCCCCCCCCCCCCC	41.14	23663014
350	Phosphorylation	PDQSLKSSSPHSSPG CCCCCCCCCCCCCCC	46.42	23663014
351	Phosphorylation	DQSLKSSSPHSSPGN CCCCCCCCCCCCCCC	33.45	23663014
354	Phosphorylation	LKSSSPHSSPGNTVS CCCCCCCCCCCCCCC	41.43	23663014
355	Phosphorylation	KSSSPHSSPGNTVSP CCCCCCCCCCCCCCC	33.52	23663014
359	Phosphorylation	PHSSPGNTVSPVGPG CCCCCCCCCCCCCCC	28.42	23663014
361	Phosphorylation	SSPGNTVSPVGPGSQ CCCCCCCCCCCCCCH	16.30	23663014
367	Phosphorylation	VSPVGPGSQEHRDSY CCCCCCCCHHHHHHH	35.21	27080861
371	Methylation	GPGSQEHRDSYAYLN CCCCHHHHHHHEEEE	33.54	115383793
511	Phosphorylation	SMKDKACSPTSGSPT HCCCCCCCCCCCCCC	35.75	25159151
513	Phosphorylation	KDKACSPTSGSPTAG CCCCCCCCCCCCCCC	29.44	23663014
514	Phosphorylation	DKACSPTSGSPTAGT CCCCCCCCCCCCCCC	40.43	23663014
516	Phosphorylation	ACSPTSGSPTAGTAA CCCCCCCCCCCCCCC	20.88	23663014
518	Phosphorylation	SPTSGSPTAGTAATA CCCCCCCCCCCCCCC	39.14	23663014
521	Phosphorylation	SGSPTAGTAATAEHV CCCCCCCCCCCCEEE	15.62	23663014
524	Phosphorylation	PTAGTAATAEHVVQP CCCCCCCCCEEECCC	30.07	23663014
534	O-linked_Glycosylation	HVVQPKATSAAMAAP EECCCCCCCHHHHCC	25.65	31492838
534	Phosphorylation	HVVQPKATSAAMAAP EECCCCCCCHHHHCC	25.65	28122231
535	Phosphorylation	VVQPKATSAAMAAPS ECCCCCCCHHHHCCC	20.91	28122231
542	Phosphorylation	SAAMAAPSSDEAMNL CHHHHCCCCHHHHHH	45.77	28122231
543	Phosphorylation	AAMAAPSSDEAMNLI HHHHCCCCHHHHHHH	38.11	28122231
560	Acetylation	KRNMTGYKTLPYPLK CCCCCCCCCCCCCCC	44.95	26051181
564	Phosphorylation	TGYKTLPYPLKKQNG CCCCCCCCCCCCCCC	25.06	25954137
613	Phosphorylation	QTCNKGFTQLAHLQK EECCCCHHHHHHHHH	31.20	28258704
641	Phosphorylation	QVCHKRFSSTSNLKT CCCCCCCCCCCCCEE	36.42	-
678	Acetylation	FVHLKLHKRLHTRER EHHHHHHHHHHCCCC	68.07	30587203
787	Phosphorylation	MGNGLLSSGCSLYES CCCCCCCCCCEEECC	43.73	22210691
795	Phosphorylation	GCSLYESSDLPLMKL CCEEECCCCCCCCCC	31.09	22210691
816	Sumoylation	PLVPVKVKQETVEPM CCCCEEEEECCCCCC	36.38	-
816	Sumoylation	PLVPVKVKQETVEPM CCCCEEEEECCCCCC	36.38	22555612

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
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO11	Q86XK2	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
816	K	Sumoylation		22555612
Sumoylation at Lys-816 by PIAS1 augments transcriptional repressor activity, and is critical for plasma cell differentiation.

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 PRDM1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TLE1_HUMAN	TLE1	physical	9887105
TLE2_HUMAN	TLE2	physical	9887105
HDAC2_HUMAN	HDAC2	physical	10713181
EHMT2_HUMAN	EHMT2	physical	14985713
KDM1A_HUMAN	KDM1A	physical	19124609
PIAS1_HUMAN	PIAS1	physical	22555612
HDAC2_HUMAN	HDAC2	physical	22555612
HDAC1_HUMAN	HDAC1	physical	22733990
HDAC2_HUMAN	HDAC2	physical	22733990
ANM5_HUMAN	PRMT5	physical	22733990
EHMT2_HUMAN	EHMT2	physical	22733990
IRF1_HUMAN	IRF1	physical	19828629
IRF2_HUMAN	IRF2	physical	19828629
H11_HUMAN	HIST1H1A	physical	14985713
PRDM1_HUMAN	PRDM1	physical	22851713
IKZF3_HUMAN	IKZF3	physical	26823144
GTF2I_HUMAN	GTF2I	physical	26823144
GRP78_HUMAN	HSPA5	physical	26823144
GRP75_HUMAN	HSPA9	physical	26823144
CH60_HUMAN	HSPD1	physical	26823144
DPYL3_HUMAN	DPYSL3	physical	28514442
BMX_HUMAN	BMX	physical	28514442
SRC_HUMAN	SRC	physical	28514442
RRAS_HUMAN	RRAS	physical	28514442
UBE4A_HUMAN	UBE4A	physical	28514442
DLG1_HUMAN	DLG1	physical	28514442

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PRDM1_HUMAN

Related Literatures of Post-Translational Modification

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