GLMN_HUMAN - dbPTM
GLMN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLMN_HUMAN
UniProt AC Q92990
Protein Name Glomulin
Gene Name GLMN
Organism Homo sapiens (Human).
Sequence Length 594
Subcellular Localization
Protein Description Essential for normal development of the vasculature. May represent a naturally occurring ligand of the immunophilins FKBP59 and FKBP12. May function as an membrane anchoring protein. Isoform 1 may stimulate the p70S6K pathway. Isoform 2 may inhibit cell proliferation and increase IL2 production..
Protein Sequence MAVEELQSIIKRCQILEEQDFKEEDFGLFQLAGQRCIEEGHTDQLLEIIQNEKNKVIIKNMGWNLVGPVVRCLLCKDKEDSKRKVYFLIFDLLVKLCNPKELLLGLLELIEEPSGKQISQSILLLLQPLQTVIQKLHNKAYSIGLALSTLWNQLSLLPVPYSKEQIQMDDYGLCQCCKALIEFTKPFVEEVIDNKENSLENEKLKDELLKFCFKSLKCPLLTAQFFEQSEEGGNDPFRYFASEIIGFLSAIGHPFPKMIFNHGRKKRTWNYLEFEEEENKQLADSMASLAYLVFVQGIHIDQLPMVLSPLYLLQFNMGHIEVFLQRTEESVISKGLELLENSLLRIEDNSLLYQYLEIKSFLTVPQGLVKVMTLCPIETLRKKSLAMLQLYINKLDSQGKYTLFRCLLNTSNHSGVEAFIIQNIKNQIDMSLKRTRNNKWFTGPQLISLLDLVLFLPEGAETDLLQNSDRIMASLNLLRYLVIKDNENDNQTGLWTELGNIENNFLKPLHIGLNMSKAHYEAEIKNSQEAQKSKDLCSITVSGEEIPNMPPEMQLKVLHSALFTFDLIESVLARVEELIEIKTKSTSEENIGIK
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------MAVEELQSI
------CHHHHHHHH		19.8922223895
8PhosphorylationMAVEELQSIIKRCQI
CHHHHHHHHHHHHHH		38.6224719451
11UbiquitinationEELQSIIKRCQILEE
HHHHHHHHHHHHHCC		45.51-
53UbiquitinationLEIIQNEKNKVIIKN
HHHHHCCCCCEEEEC		70.40-
55UbiquitinationIIQNEKNKVIIKNMG
HHHCCCCCEEEECCC		45.97-
59UbiquitinationEKNKVIIKNMGWNLV
CCCCEEEECCCCCCH		29.74-
86PhosphorylationEDSKRKVYFLIFDLL
HHHCCHHHHHHHHHH		8.83-
185 (in isoform 2)Ubiquitination-41.6021906983
185 (in isoform 1)Ubiquitination-41.6021906983
185UbiquitinationKALIEFTKPFVEEVI
HHHHHHHHHHHHHHH		41.6021906983
195UbiquitinationVEEVIDNKENSLENE
HHHHHHCCCCCCCCH		55.30-
198PhosphorylationVIDNKENSLENEKLK
HHHCCCCCCCCHHHH		37.85-
203UbiquitinationENSLENEKLKDELLK
CCCCCCHHHHHHHHH		72.86-
214UbiquitinationELLKFCFKSLKCPLL
HHHHHHHHHCCCCHH		56.94-
217UbiquitinationKFCFKSLKCPLLTAQ
HHHHHHCCCCHHHHH		40.68-
271PhosphorylationRKKRTWNYLEFEEEE
CCCCCEECCCCCHHH		10.1227642862
330PhosphorylationFLQRTEESVISKGLE
HHHHHHHHHHHHHHH		20.6522468782
333PhosphorylationRTEESVISKGLELLE
HHHHHHHHHHHHHHH		20.6522468782
353PhosphorylationIEDNSLLYQYLEIKS
EECCCHHHHHHHHHH		10.6225147952
383AcetylationPIETLRKKSLAMLQL
CHHHHHHHHHHHHHH		44.247711421
391PhosphorylationSLAMLQLYINKLDSQ
HHHHHHHHHHHHCCC		6.89-
431PhosphorylationIKNQIDMSLKRTRNN
HHHHHHHHCCCCCCC		27.3024719451
433UbiquitinationNQIDMSLKRTRNNKW
HHHHHHCCCCCCCCC		44.4021906983
433 (in isoform 1)Ubiquitination-44.4021906983
435PhosphorylationIDMSLKRTRNNKWFT
HHHHCCCCCCCCCCC		35.84-
525UbiquitinationAHYEAEIKNSQEAQK
HHHHHHHCCCHHHHH		41.8921906983
525 (in isoform 1)Ubiquitination-41.8921906983
584 (in isoform 1)Ubiquitination-46.8921906983
584UbiquitinationELIEIKTKSTSEENI
HHHHCCCCCCCCCCC		46.892190698
585PhosphorylationLIEIKTKSTSEENIG
HHHCCCCCCCCCCCC		42.2630622161
586PhosphorylationIEIKTKSTSEENIGI
HHCCCCCCCCCCCCC		41.5330622161
587PhosphorylationEIKTKSTSEENIGIK
HCCCCCCCCCCCCCC		50.4325159151
594AcetylationSEENIGIK-------
CCCCCCCC-------		49.42164315
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 GLMN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLMN_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 GLMN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MET_HUMANMETphysical
11571281
FKBP4_HUMANFKBP4physical
8955134
FKB1A_HUMANFKBP1Aphysical
8955134
CUL1_HUMANCUL1physical
22405651
CUL4A_HUMANCUL4Aphysical
22405651
RBX1_HUMANRBX1physical
22405651
RBX1_HUMANRBX1physical
22748924
CUL1_HUMANCUL1physical
22748924
FKBP4_HUMANFKBP4physical
12604780
FBXW7_HUMANFBXW7physical
22405651
SKP1_HUMANSKP1physical
22405651
IMDH2_HUMANIMPDH2physical
26344197
CUL7_HUMANCUL7physical
28514442
CUL9_HUMANCUL9physical
28514442
ZSWM6_HUMANZSWIM6physical
28514442
ANKL2_HUMANANKLE2physical
28514442
FEM1B_HUMANFEM1Bphysical
28514442
TM143_HUMANTMEM143physical
28514442
KLDC3_HUMANKLHDC3physical
28514442
APBP2_HUMANAPPBP2physical
28514442
DCAF4_HUMANDCAF4physical
28514442
FEM1C_HUMANFEM1Cphysical
28514442
CUL4B_HUMANCUL4Bphysical
28514442
KLD10_HUMANKLHDC10physical
28514442
KCTD6_HUMANKCTD6physical
28514442
DTL_HUMANDTLphysical
28514442
CUL4A_HUMANCUL4Aphysical
28514442
KLDC2_HUMANKLHDC2physical
28514442
CUL2_HUMANCUL2physical
28514442
KLH42_HUMANKLHL42physical
28514442
CUL1_HUMANCUL1physical
28514442
CRBN_HUMANCRBNphysical
28514442
BTBD1_HUMANBTBD1physical
28514442
BACD3_HUMANKCTD10physical
28514442
BTBD9_HUMANBTBD9physical
28514442
BIRC2_HUMANBIRC2physical
29191979
BIRC3_HUMANBIRC3physical
29191979
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
138000Glomuvenous malformations (GVMs)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLMN_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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