DLK1_HUMAN - dbPTM
DLK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DLK1_HUMAN
UniProt AC P80370
Protein Name Protein delta homolog 1
Gene Name DLK1
Organism Homo sapiens (Human).
Sequence Length 383
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description May have a role in neuroendocrine differentiation..
Protein Sequence MTATEALLRVLLLLLAFGHSTYGAECFPACNPQNGFCEDDNVCRCQPGWQGPLCDQCVTSPGCLHGLCGEPGQCICTDGWDGELCDRDVRACSSAPCANNRTCVSLDDGLYECSCAPGYSGKDCQKKDGPCVINGSPCQHGGTCVDDEGRASHASCLCPPGFSGNFCEIVANSCTPNPCENDGVCTDIGGDFRCRCPAGFIDKTCSRPVTNCASSPCQNGGTCLQHTQVSYECLCKPEFTGLTCVKKRALSPQQVTRLPSGYGLAYRLTPGVHELPVQQPEHRILKVSMKELNKKTPLLTEGQAICFTILGVLTSLVVLGTVGIVFLNKCETWVSNLRYNHMLRKKKNLLLQYNSGEDLAVNIIFPEKIDMTTFSKEAGDEEI
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
94O-linked_GlycosylationRDVRACSSAPCANNR
CCHHHHCCCCCCCCC
35.79UniProtKB CARBOHYD
100N-linked_GlycosylationSSAPCANNRTCVSLD
CCCCCCCCCEEEECC
23.327925474
143O-linked_GlycosylationSPCQHGGTCVDDEGR
CCCCCCCEEECCCCC
17.59UniProtKB CARBOHYD
163O-linked_GlycosylationCLCPPGFSGNFCEIV
EECCCCCCCCCEEEE
38.45UniProtKB CARBOHYD
165N-linked_GlycosylationCPPGFSGNFCEIVAN
CCCCCCCCCEEEEEE
36.887925474
172N-linked_GlycosylationNFCEIVANSCTPNPC
CCEEEEEECCCCCCC
27.077925474
214O-linked_GlycosylationRPVTNCASSPCQNGG
CCCCCCCCCCCCCCC
36.69UniProtKB CARBOHYD
222O-linked_GlycosylationSPCQNGGTCLQHTQV
CCCCCCCCCEEEEEE
16.08UniProtKB CARBOHYD
251O-linked_GlycosylationCVKKRALSPQQVTRL
EEECCCCCHHHCCCC
21.48UniProtKB CARBOHYD
256O-linked_GlycosylationALSPQQVTRLPSGYG
CCCHHHCCCCCCCCC
23.3522171320
260O-linked_GlycosylationQQVTRLPSGYGLAYR
HHCCCCCCCCCEEEE
49.60UniProtKB CARBOHYD
269O-linked_GlycosylationYGLAYRLTPGVHELP
CCEEEEECCCCCCCC
14.7055830429
303 (in isoform 2)Ubiquitination-22.71-
353PhosphorylationKKNLLLQYNSGEDLA
HCCEEEEECCCCCEE
15.97-
355PhosphorylationNLLLQYNSGEDLAVN
CEEEEECCCCCEEEE
38.3329116813
375PhosphorylationKIDMTTFSKEAGDEE
CCCCCEECCCCCCCC
27.7426091039
376UbiquitinationIDMTTFSKEAGDEEI
CCCCEECCCCCCCCC
47.60-

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
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DLK1_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 DLK1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GAS1_HUMANGAS1physical
11846389
GRN_HUMANGRNphysical
11846389
TBB8_HUMANTUBB8physical
26186194
DCAKD_HUMANDCAKDphysical
26186194
AVR2B_HUMANACVR2Bphysical
26186194
ZN696_HUMANZNF696physical
26186194
SMG8_HUMANSMG8physical
26186194
AT1A3_HUMANATP1A3physical
26186194
AT12A_HUMANATP12Aphysical
26186194
NCLN_HUMANNCLNphysical
26186194
TBC15_HUMANTBC1D15physical
26186194
AT131_HUMANATP13A1physical
26186194
TFR1_HUMANTFRCphysical
26186194
NU188_HUMANNUP188physical
26186194
PTH2_HUMANPTRH2physical
26186194
WDR44_HUMANWDR44physical
26186194
P121A_HUMANPOM121physical
26186194
SCAM1_HUMANSCAMP1physical
26186194
NFRKB_HUMANNFRKBphysical
26186194
F234B_HUMANKIAA1467physical
26186194
CEP78_HUMANCEP78physical
26186194
LEMD2_HUMANLEMD2physical
26186194
ZZEF1_HUMANZZEF1physical
26186194
AT2B4_HUMANATP2B4physical
26186194
M18BP_HUMANMIS18BP1physical
26186194
C2CD5_HUMANC2CD5physical
26186194
PDS5A_HUMANPDS5Aphysical
26186194
LAP4B_HUMANLAPTM4Bphysical
26186194
TM214_HUMANTMEM214physical
26186194
SCAM2_HUMANSCAMP2physical
26186194
K1161_HUMANKIAA1161physical
26186194
PGES2_HUMANPTGES2physical
26186194
CABL2_HUMANCABLES2physical
26186194
STEA3_HUMANSTEAP3physical
26186194
CNDH2_HUMANNCAPH2physical
26186194
AN13C_HUMANANKRD13Cphysical
26186194
FND3A_HUMANFNDC3Aphysical
26186194
TCAF2_HUMANFAM115Cphysical
26186194
CABL1_HUMANCABLES1physical
26186194
FGFR1_HUMANFGFR1physical
26186194
PCYOX_HUMANPCYOX1physical
26186194
PRAF2_HUMANPRAF2physical
26186194
INT7_HUMANINTS7physical
26186194
DYH14_HUMANDNAH14physical
26186194
NLRX1_HUMANNLRX1physical
26186194
GOGA2_HUMANGOLGA2physical
26186194
UBE3B_HUMANUBE3Bphysical
26186194
ANR27_HUMANANKRD27physical
26186194
MOT8_HUMANSLC16A2physical
26186194
PSN2_HUMANPSEN2physical
26186194
DIP2A_HUMANDIP2Aphysical
26186194
MP2K7_HUMANMAP2K7physical
26186194
MBLC2_HUMANMBLAC2physical
26186194
OCLN_HUMANOCLNphysical
26186194
ANO6_HUMANANO6physical
26186194
S19A2_HUMANSLC19A2physical
26186194
EGFL7_HUMANEGFL7physical
26186194
ADPGK_HUMANADPGKphysical
26186194
CSPG5_HUMANCSPG5physical
26186194
FIBP_HUMANFIBPphysical
26186194
TMM94_HUMANKIAA0195physical
26186194
SGPP1_HUMANSGPP1physical
26186194
DEN6A_HUMANDENND6Aphysical
26186194
OSTC_HUMANOSTCphysical
26186194
BRI3B_HUMANBRI3BPphysical
26186194
AVR2B_HUMANACVR2Bphysical
28514442
AN13C_HUMANANKRD13Cphysical
28514442
UBE3B_HUMANUBE3Bphysical
28514442
TMM94_HUMANKIAA0195physical
28514442
CABL2_HUMANCABLES2physical
28514442
CABL1_HUMANCABLES1physical
28514442
C2CD5_HUMANC2CD5physical
28514442
LAP4B_HUMANLAPTM4Bphysical
28514442
SCAM1_HUMANSCAMP1physical
28514442
K1161_HUMANKIAA1161physical
28514442
FIBP_HUMANFIBPphysical
28514442
CSPG5_HUMANCSPG5physical
28514442
TCAF2_HUMANFAM115Cphysical
28514442
TM214_HUMANTMEM214physical
28514442
OSTC_HUMANOSTCphysical
28514442
ANR27_HUMANANKRD27physical
28514442
NFRKB_HUMANNFRKBphysical
28514442
FND3A_HUMANFNDC3Aphysical
28514442
ZN627_HUMANZNF627physical
28514442
ANO6_HUMANANO6physical
28514442
AT12A_HUMANATP12Aphysical
28514442
PGES2_HUMANPTGES2physical
28514442
BRI3B_HUMANBRI3BPphysical
28514442
AT2B4_HUMANATP2B4physical
28514442
DCAKD_HUMANDCAKDphysical
28514442
MP2K7_HUMANMAP2K7physical
28514442
PRAF2_HUMANPRAF2physical
28514442
S19A2_HUMANSLC19A2physical
28514442
ORC4_HUMANORC4physical
28514442
LEMD2_HUMANLEMD2physical
28514442
ZZEF1_HUMANZZEF1physical
28514442
SGPP1_HUMANSGPP1physical
28514442
PTH2_HUMANPTRH2physical
28514442
AT131_HUMANATP13A1physical
28514442
PCYOX_HUMANPCYOX1physical
28514442
S38A2_HUMANSLC38A2physical
28514442
STEA3_HUMANSTEAP3physical
28514442
EGFL7_HUMANEGFL7physical
28514442
NCLN_HUMANNCLNphysical
28514442
DYH14_HUMANDNAH14physical
28514442
EVA1B_HUMANEVA1Bphysical
28514442

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 DLK1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Protein structure of fetal antigen 1 (FA1). A novel circulating humanepidermal-growth-factor-like protein expressed in neuroendocrinetumors and its relation to the gene products of dlk and pG2.";
Jensen C.H., Krogh T.N., Hoejrup P., Clausen P.P., Skjoedt K.,Larsson L.-I., Enghild J.J., Teisner B.;
Eur. J. Biochem. 225:83-92(1994).
Cited for: PROTEIN SEQUENCE OF 24-383, GLYCOSYLATION AT SER-94; ASN-100; THR-143;SER-163; ASN-165; ASN-172; SER-214; THR-222; SER-251 AND SER-260, ANDVARIANT GLY-101.
O-linked Glycosylation
ReferencePubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT THR-256, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.
"Protein structure of fetal antigen 1 (FA1). A novel circulating humanepidermal-growth-factor-like protein expressed in neuroendocrinetumors and its relation to the gene products of dlk and pG2.";
Jensen C.H., Krogh T.N., Hoejrup P., Clausen P.P., Skjoedt K.,Larsson L.-I., Enghild J.J., Teisner B.;
Eur. J. Biochem. 225:83-92(1994).
Cited for: PROTEIN SEQUENCE OF 24-383, GLYCOSYLATION AT SER-94; ASN-100; THR-143;SER-163; ASN-165; ASN-172; SER-214; THR-222; SER-251 AND SER-260, ANDVARIANT GLY-101.

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