LDB1_HUMAN - dbPTM
LDB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LDB1_HUMAN
UniProt AC Q86U70
Protein Name LIM domain-binding protein 1
Gene Name LDB1
Organism Homo sapiens (Human).
Sequence Length 411
Subcellular Localization Nucleus .
Protein Description Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors. May regulate the transcriptional activity of LIM-containing proteins by determining specific partner interactions. Plays a role in the development of interneurons and motor neurons in cooperation with LHX3 and ISL1. Acts synergistically with LHX1/LIM1 in axis formation and activation of gene expression. Acts with LMO2 in the regulation of red blood cell development, maintaining erythroid precursors in an immature state (By similarity)..
Protein Sequence MSVGCACPGCSSKSFKLYSPKEPPNGNAFPPFHPGTMLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKHPKEAFHSNFVSLDCDQGSMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPTRQQPSKRRKRKMSGGSTMSSGGGNTNNSNSKKKSPASTFALSSQVPDVMVVGEPTLMGGEFGDEDERLITRLENTQFDAANGIDDEDSFNNSPALGANSPWNSKPPSSQESKSENPTSQASQ
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
2Acetylation------MSVGCACPG
------CCCCCCCCC		27.5019413330
2Phosphorylation------MSVGCACPG
------CCCCCCCCC		27.5024043423
11PhosphorylationGCACPGCSSKSFKLY
CCCCCCCCCCCEEEE		46.8724043423
12PhosphorylationCACPGCSSKSFKLYS
CCCCCCCCCCEEEEC		36.0724043423
13AcetylationACPGCSSKSFKLYSP
CCCCCCCCCEEEECC		43.5525953088
16AcetylationGCSSKSFKLYSPKEP
CCCCCCEEEECCCCC		54.3125953088
18PhosphorylationSSKSFKLYSPKEPPN
CCCCEEEECCCCCCC		24.4228122231
19PhosphorylationSKSFKLYSPKEPPNG
CCCEEEECCCCCCCC		39.6724719451
25 (in isoform 2)Phosphorylation-68.04-
45PhosphorylationLDRDVGPTPMYPPTY
CCCCCCCCCCCCCCC		18.1126074081
48PhosphorylationDVGPTPMYPPTYLEP
CCCCCCCCCCCCCCC		13.7826074081
51PhosphorylationPTPMYPPTYLEPGIG
CCCCCCCCCCCCCCC		35.9123401153
52PhosphorylationTPMYPPTYLEPGIGR
CCCCCCCCCCCCCCC		18.1626074081
61PhosphorylationEPGIGRHTPYGNQTD
CCCCCCCCCCCCHHH		19.4923401153
63PhosphorylationGIGRHTPYGNQTDYR
CCCCCCCCCCHHHHH		29.8426074081
67PhosphorylationHTPYGNQTDYRIFEL
CCCCCCHHHHHHHHH		38.7126074081
69PhosphorylationPYGNQTDYRIFELNK
CCCCHHHHHHHHHHH		14.7027251275
76UbiquitinationYRIFELNKRLQNWTE
HHHHHHHHHHHHHHH		68.08-
127PhosphorylationGRTLIPRYFRSIFEG
CCCHHHHHHHHHHCC		9.6726074081
130PhosphorylationLIPRYFRSIFEGGAT
HHHHHHHHHHCCCCE		23.0226074081
137PhosphorylationSIFEGGATELYYVLK
HHHCCCCEEEEEEEC		29.7826074081
140PhosphorylationEGGATELYYVLKHPK
CCCCEEEEEEECCHH		5.8226074081
141PhosphorylationGGATELYYVLKHPKE
CCCEEEEEEECCHHH		16.3626074081
144UbiquitinationTELYYVLKHPKEAFH
EEEEEEECCHHHHHH		48.06-
170UbiquitinationSMVTQHGKPMFTQVC
CEEECCCCEEEEEEE		31.05-
225 (in isoform 2)Phosphorylation-43.61-
226 (in isoform 2)Phosphorylation-8.64-
260UbiquitinationQELMSRHKTYSLSPR
HHHHHHCCCCCCCHH		48.31-
261PhosphorylationELMSRHKTYSLSPRD
HHHHHCCCCCCCHHH		16.5319664994
262PhosphorylationLMSRHKTYSLSPRDC
HHHHCCCCCCCHHHH		16.6519664994
263PhosphorylationMSRHKTYSLSPRDCL
HHHCCCCCCCHHHHH		27.8329900121
265PhosphorylationRHKTYSLSPRDCLKT
HCCCCCCCHHHHHHH		16.3723401153
266 (in isoform 2)Phosphorylation-41.23-
270 (in isoform 2)Phosphorylation-6.36-
271MethylationLSPRDCLKTCLFQKW
CCHHHHHHHHHHHHH		43.4524494591
271UbiquitinationLSPRDCLKTCLFQKW
CCHHHHHHHHHHHHH		43.45-
277UbiquitinationLKTCLFQKWQRMVAP
HHHHHHHHHHHHCCC		37.65-
280MethylationCLFQKWQRMVAPPAE
HHHHHHHHHCCCCCC		22.04-
289PhosphorylationVAPPAEPTRQQPSKR
CCCCCCCCCCCCCHH		32.3926074081
291 (in isoform 2)Phosphorylation-63.11-
294PhosphorylationEPTRQQPSKRRKRKM
CCCCCCCCHHCCCCC		34.1626074081
302PhosphorylationKRRKRKMSGGSTMSS
HHCCCCCCCCCCCCC		42.9322167270
305PhosphorylationKRKMSGGSTMSSGGG
CCCCCCCCCCCCCCC		25.1822167270
306PhosphorylationRKMSGGSTMSSGGGN
CCCCCCCCCCCCCCC		25.0923401153
308PhosphorylationMSGGSTMSSGGGNTN
CCCCCCCCCCCCCCC		26.3922167270
309PhosphorylationSGGSTMSSGGGNTNN
CCCCCCCCCCCCCCC		30.5422167270
314PhosphorylationMSSGGGNTNNSNSKK
CCCCCCCCCCCCCCC		38.7723663014
317PhosphorylationGGGNTNNSNSKKKSP
CCCCCCCCCCCCCCC		44.5423663014
319PhosphorylationGNTNNSNSKKKSPAS
CCCCCCCCCCCCCHH		45.7523663014
323PhosphorylationNSNSKKKSPASTFAL
CCCCCCCCCHHHHHH		34.2825159151
326PhosphorylationSKKKSPASTFALSSQ
CCCCCCHHHHHHCCC		27.6922210691
327PhosphorylationKKKSPASTFALSSQV
CCCCCHHHHHHCCCC		18.2928102081
331PhosphorylationPASTFALSSQVPDVM
CHHHHHHCCCCCCEE		18.4619276368
332PhosphorylationASTFALSSQVPDVMV
HHHHHHCCCCCCEEE		35.7327251275
344PhosphorylationVMVVGEPTLMGGEFG
EEEECCCEECCCCCC		25.6927251275
374 (in isoform 2)Phosphorylation-60.73-
377PhosphorylationNGIDDEDSFNNSPAL
CCCCCHHHCCCCCCC		28.0326074081
381PhosphorylationDEDSFNNSPALGANS
CHHHCCCCCCCCCCC		16.8026074081
388PhosphorylationSPALGANSPWNSKPP
CCCCCCCCCCCCCCC		30.6626074081
392PhosphorylationGANSPWNSKPPSSQE
CCCCCCCCCCCCCCC		42.5426074081
393AcetylationANSPWNSKPPSSQES
CCCCCCCCCCCCCCC		58.7023236377
396PhosphorylationPWNSKPPSSQESKSE
CCCCCCCCCCCCCCC		53.8626074081
397PhosphorylationWNSKPPSSQESKSEN
CCCCCCCCCCCCCCC		43.6826074081
400PhosphorylationKPPSSQESKSENPTS
CCCCCCCCCCCCCCC		33.5726074081
402PhosphorylationPSSQESKSENPTSQA
CCCCCCCCCCCCCCC		52.4626074081
406PhosphorylationESKSENPTSQASQ--
CCCCCCCCCCCCC--		45.0826074081
407PhosphorylationSKSENPTSQASQ---
CCCCCCCCCCCC---		25.6326074081
407O-linked_GlycosylationSKSENPTSQASQ---
CCCCCCCCCCCC---		25.6330379171
410O-linked_GlycosylationENPTSQASQ------
CCCCCCCCC------		28.8730379171
410PhosphorylationENPTSQASQ------
CCCCCCCCC------		28.8723663014
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 ligaseRLIMQ9NVW2
PMID:31801865
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LDB1_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 LDB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SSBP4_HUMANSSBP4physical
16189514
LMO3_HUMANLMO3physical
16189514
SSBP2_HUMANSSBP2physical
16189514
TOLIP_HUMANTOLLIPphysical
16189514
RBTN2_HUMANLMO2physical
12727888
LMO4_HUMANLMO4physical
12727888
TAL1_HUMANTAL1physical
16407974
TFE2_HUMANTCF3physical
16407974
MTG16_HUMANCBFA2T3physical
16407974
ESR1_HUMANESR1physical
19117995
RNF12_HUMANRLIMphysical
17437998
RBTN2_HUMANLMO2physical
17437998
LHX2_HUMANLHX2physical
20211142
RB_HUMANRB1physical
10866689
RNF6_HUMANRNF6physical
12874135
RNF38_HUMANRNF38physical
12874135
RF12A_XENLArlim-aphysical
12874135
PSD10_HUMANPSMD10physical
21988832
RBTN2_HUMANLMO2physical
21988832
PSA1_HUMANPSMA1physical
21988832
LSM7_HUMANLSM7physical
21988832
RPA2_HUMANPOLR1Bphysical
21988832
SSBP3_HUMANSSBP3physical
25416956
LHX6_HUMANLHX6physical
25416956
LHX8_HUMANLHX8physical
25416956
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 LDB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-302 AND THR-306, ANDMASS SPECTROMETRY.

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