LMF2_HUMAN - dbPTM
LMF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LMF2_HUMAN
UniProt AC Q9BU23
Protein Name Lipase maturation factor 2
Gene Name LMF2
Organism Homo sapiens (Human).
Sequence Length 707
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Involved in the maturation of specific proteins in the endoplasmic reticulum. May be required for maturation and transport of active lipoprotein lipase (LPL) through the secretory pathway (By similarity)..
Protein Sequence MAGSRLPRQLFLQGVAAVFMFAFASLYTQIPGLYGPEGILPARRTLRPQGKGRWQQLWETPTLLWEAPRLGLDTAQGLELLSLLGALVALGALLLSPLRHPVIYLLLWAAYLSACQVGQVFLYFQWDSLLLETGFLAVLVAPLRPASHRKEAPQGRQAGALPHEDLPFWLVRWLLFRLMFASGVVKLTSRCPAWWGLTALTYHYETQCLPTPAAWFAHHLPVWLHKLSVVATFLIEIAVPPLFFAPIRRLRLAAFYSQVLLQVLIIITGNYNFFNLMTLVLTTALLDDQHLAAEPGHGSRKKTATSWPKALLATLSLLLELAVYGLLAYGTVHYFGLEVDWQQRTIHSRTTFTFHQFSQWLKTLTLPTVWLGVASLVWELLSALWRWTQVRGWLRKLSAVVQLSLVGTATVALFLISLVPYSYVEPGTHGRLWTGAHRLFGAVEHLQLANSYGLFRRMTGLGGRPEVVLEGSYDGHHWTEIEFMYKPGNLSRPPPVVVPHQPRLDWQMWFAALGPHTHSPWFTSLVLRLLQGKEPVIRLVQSQVARYPFHKQPPTYVRAQRYKYWFSQPGEQGQWWRRQWVEEFFPSVSLGDPTLETLLRQFGLQEKSPPRTRSANSTLAQALHWTRSQLSPLEAPALLWGLLMAVGAVRFVQALLAPCSLRSSPLAPVSGEKRRPASQKDSGAASEQATAAPNPCSSSSRTTRRKK
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
4Phosphorylation----MAGSRLPRQLF
----CCCCCCCHHHH		22.5526074081
25PhosphorylationVFMFAFASLYTQIPG
HHHHHHHHHHHCCCC		18.5624043423
26 (in isoform 2)Ubiquitination-4.8721890473
27PhosphorylationMFAFASLYTQIPGLY
HHHHHHHHHCCCCCC		8.2924043423
28PhosphorylationFAFASLYTQIPGLYG
HHHHHHHHCCCCCCC		25.8924043423
34PhosphorylationYTQIPGLYGPEGILP
HHCCCCCCCCCCCCC		36.2324043423
51UbiquitinationRTLRPQGKGRWQQLW
CCCCCCCCCHHHHHH		39.8021906983
51 (in isoform 3)Ubiquitination-39.8021890473
51 (in isoform 1)Ubiquitination-39.8021890473
60PhosphorylationRWQQLWETPTLLWEA
HHHHHHCCCCCHHHC		15.2522468782
62PhosphorylationQQLWETPTLLWEAPR
HHHHCCCCCHHHCCC		41.7322468782
96PhosphorylationALGALLLSPLRHPVI
HHHHHHHHCCCCHHH		23.1224719451
302UbiquitinationPGHGSRKKTATSWPK
CCCCCCCCCCCCHHH		42.13-
420 (in isoform 3)Ubiquitination-20.0421890473
438 (in isoform 3)Ubiquitination-31.0421890473
459PhosphorylationYGLFRRMTGLGGRPE
HCHHHHHHCCCCCCE		27.6924719451
478UbiquitinationGSYDGHHWTEIEFMY
CCCCCCCEEEEEEEE		7.0521890473
489N-linked_GlycosylationEFMYKPGNLSRPPPV
EEEECCCCCCCCCCE		43.29UniProtKB CARBOHYD
495UbiquitinationGNLSRPPPVVVPHQP
CCCCCCCCEECCCCC		33.9321890473
496UbiquitinationNLSRPPPVVVPHQPR
CCCCCCCEECCCCCC		9.2721890473
508 (in isoform 2)Ubiquitination-2.5021890473
508UbiquitinationQPRLDWQMWFAALGP
CCCCCHHHHHHHHCC		2.5021890473
513UbiquitinationWQMWFAALGPHTHSP
HHHHHHHHCCCCCCH		11.1321890473
526 (in isoform 2)Ubiquitination-2.6821890473
526UbiquitinationSPWFTSLVLRLLQGK
CHHHHHHHHHHHCCC		2.6821890473
5332-HydroxyisobutyrylationVLRLLQGKEPVIRLV
HHHHHCCCCCCHHHH		45.98-
533 (in isoform 1)Ubiquitination-45.9821890473
533UbiquitinationVLRLLQGKEPVIRLV
HHHHHCCCCCCHHHH		45.9821890473
551UbiquitinationVARYPFHKQPPTYVR
HHCCCCCCCCCCEEE		65.9521890473
551 (in isoform 1)Ubiquitination-65.9521890473
552UbiquitinationARYPFHKQPPTYVRA
HCCCCCCCCCCEEEE		40.4124816145
563UbiquitinationYVRAQRYKYWFSQPG
EEEEEEEEEECCCCC		37.89-
569UbiquitinationYKYWFSQPGEQGQWW
EEEECCCCCCCCCHH		47.2724816145
582UbiquitinationWWRRQWVEEFFPSVS
HHHHHHHHHHCCCCC		46.2424816145
607UbiquitinationRQFGLQEKSPPRTRS
HHCCCCCCCCCCCCC		56.1333845483
608PhosphorylationQFGLQEKSPPRTRSA
HCCCCCCCCCCCCCC		39.11-
612PhosphorylationQEKSPPRTRSANSTL
CCCCCCCCCCCHHHH		34.45-
616N-linked_GlycosylationPPRTRSANSTLAQAL
CCCCCCCHHHHHHHH		36.45UniProtKB CARBOHYD
617PhosphorylationPRTRSANSTLAQALH
CCCCCCHHHHHHHHH		25.23-
618UbiquitinationRTRSANSTLAQALHW
CCCCCHHHHHHHHHH		26.3924816145
635UbiquitinationSQLSPLEAPALLWGL
HCCCCCHHHHHHHHH		11.4424816145
648UbiquitinationGLLMAVGAVRFVQAL
HHHHHHHHHHHHHHH		5.2324816145
659S-palmitoylationVQALLAPCSLRSSPL
HHHHHCCCCCCCCCC		5.0729575903
663PhosphorylationLAPCSLRSSPLAPVS
HCCCCCCCCCCCCCC		41.4227251275
664PhosphorylationAPCSLRSSPLAPVSG
CCCCCCCCCCCCCCC		19.9429396449
670PhosphorylationSSPLAPVSGEKRRPA
CCCCCCCCCCCCCCC		39.9326055452
673UbiquitinationLAPVSGEKRRPASQK
CCCCCCCCCCCCCCC		58.1824816145
6732-HydroxyisobutyrylationLAPVSGEKRRPASQK
CCCCCCCCCCCCCCC		58.18-
673MalonylationLAPVSGEKRRPASQK
CCCCCCCCCCCCCCC		58.1826320211
678PhosphorylationGEKRRPASQKDSGAA
CCCCCCCCCCCCCHH		40.2123401153
680AcetylationKRRPASQKDSGAASE
CCCCCCCCCCCHHHH		51.907925397
682PhosphorylationRPASQKDSGAASEQA
CCCCCCCCCHHHHHH		37.0519413330
686PhosphorylationQKDSGAASEQATAAP
CCCCCHHHHHHCCCC		29.7019413330
690PhosphorylationGAASEQATAAPNPCS
CHHHHHHCCCCCCCC		24.0528985074
697PhosphorylationTAAPNPCSSSSRTTR
CCCCCCCCCCCCCCC		34.2225159151
698PhosphorylationAAPNPCSSSSRTTRR
CCCCCCCCCCCCCCC		38.7625159151
699PhosphorylationAPNPCSSSSRTTRRK
CCCCCCCCCCCCCCC		13.9328450419
700PhosphorylationPNPCSSSSRTTRRKK
CCCCCCCCCCCCCCC		35.2821712546
702PhosphorylationPCSSSSRTTRRKK--
CCCCCCCCCCCCC--		26.9730177828
703PhosphorylationCSSSSRTTRRKK---
CCCCCCCCCCCC---		27.6330177828
706AcetylationSSRTTRRKK------
CCCCCCCCC------		60.597925407
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

Oops, there are no upstream regulatory protein records of LMF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LMF2_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 LMF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
K1C40_HUMANKRT40physical
25416956
KR103_HUMANKRTAP10-3physical
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 LMF2_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-682 AND SER-686, ANDMASS SPECTROMETRY.

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