LN28A_HUMAN - dbPTM
LN28A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LN28A_HUMAN
UniProt AC Q9H9Z2
Protein Name Protein lin-28 homolog A
Gene Name LIN28A
Organism Homo sapiens (Human).
Sequence Length 209
Subcellular Localization Cytoplasm . Rough endoplasmic reticulum . Cytoplasm, P-body . Cytoplasm, Stress granule . Nucleus, nucleolus . Predominantly cytoplasmic (PubMed:22118463). In the cytoplasm, localizes to peri-endoplasmic reticulum regions and detected in the microsom
Protein Description RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism. [PubMed: 21247876 Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits ZCCHC11/TUT4 uridylyltransferase. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells]
Protein Sequence MGSVSNQQFAGGCAKAAEEAPEEAPEDAARAADEPQLLHGAGICKWFNVRMGFGFLSMTARAGVALDPPVDVFVHQSKLHMEGFRSLKEGEAVEFTFKKSAKGLESIRVTGPGGVFCIGSERRPKGKSMQKRRSKGDRCYNCGGLDHHAKECKLPPQPKKCHFCQSISHMVASCPLKAQQGPSAQGKPTYFREEEEEIHSPTLLPEAQN
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------MGSVSNQQF
------CCCCCHHHC		36.4321406692
3Phosphorylation-----MGSVSNQQFA
-----CCCCCHHHCC		22.5219664995
5Phosphorylation---MGSVSNQQFAGG
---CCCCCHHHCCCH		30.5321406692
120PhosphorylationGGVFCIGSERRPKGK
CCEEEECCCCCCCCC		14.1821406692
183O-linked_GlycosylationLKAQQGPSAQGKPTY
CCCCCCCCCCCCCCC		39.8029351928
183PhosphorylationLKAQQGPSAQGKPTY
CCCCCCCCCCCCCCC		39.8021406692
187UbiquitinationQGPSAQGKPTYFREE
CCCCCCCCCCCCCCC		23.31-
189PhosphorylationPSAQGKPTYFREEEE
CCCCCCCCCCCCCHH		38.4921406692
190PhosphorylationSAQGKPTYFREEEEE
CCCCCCCCCCCCHHC		14.7921406692
200PhosphorylationEEEEEIHSPTLLPEA
CCHHCCCCCCCCCCC		25.8219664995
202PhosphorylationEEEIHSPTLLPEAQN
HHCCCCCCCCCCCCC		43.8919664995
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
200SPhosphorylationKinaseERK2P28482
PSP
200SPhosphorylationKinaseERK1P27361
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LN28A_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 LN28A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DOT1L_HUMANDOT1Lgenetic
22388813
AATF_HUMANAATFphysical
24778252
BRX1_HUMANBRIX1physical
24778252
BYST_HUMANBYSLphysical
24778252
NOA1_HUMANNOA1physical
24778252
CDC5L_HUMANCDC5Lphysical
24778252
DDX50_HUMANDDX50physical
24778252
DHX57_HUMANDHX57physical
24778252
FAKD2_HUMANFASTKD2physical
24778252
FBRL_HUMANFBLphysical
24778252
G45IP_HUMANGADD45GIP1physical
24778252
H10_HUMANH1F0physical
24778252
HNRL2_HUMANHNRNPUL2physical
24778252
HP1B3_HUMANHP1BP3physical
24778252
ICT1_HUMANICT1physical
24778252
KRI1_HUMANKRI1physical
24778252
KRR1_HUMANKRR1physical
24778252
LARP4_HUMANLARP4physical
24778252
LIN41_HUMANTRIM71physical
24778252
LTV1_HUMANLTV1physical
24778252
MET17_HUMANMETTL17physical
24778252
MEPCE_HUMANMEPCEphysical
24778252
NCBP1_HUMANNCBP1physical
24778252
NHP2_HUMANNHP2physical
24778252
NOB1_HUMANNOB1physical
24778252
NOC3L_HUMANNOC3Lphysical
24778252
NOL6_HUMANNOL6physical
24778252
NOP10_HUMANNOP10physical
24778252
PHAX_HUMANPHAXphysical
24778252
POP1_HUMANPOP1physical
24778252
PRP19_HUMANPRPF19physical
24778252
DHX8_HUMANDHX8physical
24778252
ZCCHV_HUMANZC3HAV1physical
24778252
PURA_HUMANPURAphysical
24778252
PTCD1_HUMANPTCD1physical
24778252
RUXG_HUMANSNRPGphysical
24778252
PRPF3_HUMANPRPF3physical
24778252
DDX41_HUMANDDX41physical
24778252
TCOF_HUMANTCOF1physical
24778252
ZBT11_HUMANZBTB11physical
24778252
STRBP_HUMANSTRBPphysical
24778252
RALY_HUMANRALYphysical
24778252
RSMB_HUMANSNRPBphysical
24778252
IFIT5_HUMANIFIT5physical
24778252
EBP2_HUMANEBNA1BP2physical
24778252
RENT1_HUMANUPF1physical
24778252
SF3B2_HUMANSF3B2physical
24778252
NCBP2_HUMANNCBP2physical
24778252
SRRT_HUMANSRRTphysical
24778252
SRP72_HUMANSRP72physical
24778252
RU2B_HUMANSNRPB2physical
24778252
LARP7_HUMANLARP7physical
24778252
IMA3_HUMANKPNA4physical
24778252
PWP1_HUMANPWP1physical
24778252
RU17_HUMANSNRNP70physical
24778252
RBM28_HUMANRBM28physical
24778252
RBM34_HUMANRBM34physical
24778252
ROAA_HUMANHNRNPABphysical
24778252
RRP12_HUMANRRP12physical
24778252
RRS1_HUMANRRS1physical
24778252
RUXF_HUMANSNRPFphysical
24778252
SREK1_HUMANSREK1physical
24778252
SNRPA_HUMANSNRPAphysical
24778252
SRP14_HUMANSRP14physical
24778252
SRRM1_HUMANSRRM1physical
24778252
SSF1_HUMANPPANphysical
24778252
SURF6_HUMANSURF6physical
24778252
TGS1_HUMANTGS1physical
24778252
TSR1_HUMANTSR1physical
24778252
U3IP2_HUMANRRP9physical
24778252
XRN2_HUMANXRN2physical
24778252
ZC11A_HUMANZC3H11Aphysical
24778252
KAT3_HUMANCCBL2physical
24778252
DHX36_HUMANDHX36physical
24778252
DKC1_HUMANDKC1physical
24778252
ROA3_HUMANHNRNPA3physical
24778252
IF2B3_HUMANIGF2BP3physical
24778252
LARP1_HUMANLARP1physical
24778252
LAR4B_HUMANLARP4Bphysical
24778252
NH2L1_HUMANNHP2L1physical
24778252
NOP2_HUMANNOP2physical
24778252
SND1_HUMANSND1physical
24778252
LA_HUMANSSBphysical
24778252
TRI25_HUMANTRIM25physical
25457611
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 LN28A_HUMAN

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Related Literatures of Post-Translational Modification

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