FIBP_HUMAN - dbPTM
FIBP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FIBP_HUMAN
UniProt AC O43427
Protein Name Acidic fibroblast growth factor intracellular-binding protein
Gene Name FIBP
Organism Homo sapiens (Human).
Sequence Length 364
Subcellular Localization Nucleus. Endomembrane system
Peripheral membrane protein. Also associated with cytoplasmic membranes, particularly of mitochondria.
Protein Description May be involved in mitogenic function of FGF1. May mediate with IER2 FGF-signaling in the establishment of laterality in the embryo (By similarity)..
Protein Sequence MTSELDIFVGNTTLIDEDVYRLWLDGYSVTDAVALRVRSGILEQTGATAAVLQSDTMDHYRTFHMLERLLHAPPKLLHQLIFQIPPSRQALLIERYYAFDEAFVREVLGKKLSKGTKKDLDDISTKTGITLKSCRRQFDNFKRVFKVVEEMRGSLVDNIQQHFLLSDRLARDYAAIVFFANNRFETGKKKLQYLSFGDFAFCAELMIQNWTLGAVGEAPTDPDSQMDDMDMDLDKEFLQDLKELKVLVADKDLLDLHKSLVCTALRGKLGVFSEMEANFKNLSRGLVNVAAKLTHNKDVRDLFVDLVEKFVEPCRSDHWPLSDVRFFLNQYSASVHSLDGFRHQALWDRYMGTLRGCLLRLYHD
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
2Phosphorylation------MTSELDIFV
------CCCCCEEEE		30.7919369195
2Acetylation------MTSELDIFV
------CCCCCEEEE		30.7919369195
75UbiquitinationRLLHAPPKLLHQLIF
HHHCCCHHHHHHHHH		63.72-
118UbiquitinationKLSKGTKKDLDDIST
HCCCCCCCCHHHCHH		64.46-
124PhosphorylationKKDLDDISTKTGITL
CCCHHHCHHHCCCCH		30.7426074081
125PhosphorylationKDLDDISTKTGITLK
CCHHHCHHHCCCCHH		32.7226074081
126UbiquitinationDLDDISTKTGITLKS
CHHHCHHHCCCCHHH		37.6521906983
126 (in isoform 1)Ubiquitination-37.6521890473
126 (in isoform 2)Ubiquitination-37.6521890473
127PhosphorylationLDDISTKTGITLKSC
HHHCHHHCCCCHHHH		33.6326074081
130PhosphorylationISTKTGITLKSCRRQ
CHHHCCCCHHHHHHH		29.4926074081
132UbiquitinationTKTGITLKSCRRQFD
HHCCCCHHHHHHHHH		38.5729967540
142AcetylationRRQFDNFKRVFKVVE
HHHHHHHHHHHHHHH		54.6425953088
142UbiquitinationRRQFDNFKRVFKVVE
HHHHHHHHHHHHHHH		54.6424816145
146UbiquitinationDNFKRVFKVVEEMRG
HHHHHHHHHHHHHHC		42.3824816145
146AcetylationDNFKRVFKVVEEMRG
HHHHHHHHHHHHHHC		42.3825953088
235UbiquitinationDMDMDLDKEFLQDLK
CCCCCCCHHHHHHHH		58.6322817900
238UbiquitinationMDLDKEFLQDLKELK
CCCCHHHHHHHHHHC		3.9821890473
238 (in isoform 2)Ubiquitination-3.9821890473
242UbiquitinationKEFLQDLKELKVLVA
HHHHHHHHHHCCEEE		70.1022817900
244UbiquitinationFLQDLKELKVLVADK
HHHHHHHHCCEEECH		4.4321890473
244 (in isoform 2)Ubiquitination-4.4321890473
245 (in isoform 1)Ubiquitination-34.3221890473
245UbiquitinationLQDLKELKVLVADKD
HHHHHHHCCEEECHH		34.3223000965
251 (in isoform 1)Ubiquitination-40.3021890473
251AcetylationLKVLVADKDLLDLHK
HCCEEECHHHHHHHH		40.3025953088
251UbiquitinationLKVLVADKDLLDLHK
HCCEEECHHHHHHHH		40.3023000965
258UbiquitinationKDLLDLHKSLVCTAL
HHHHHHHHHHHHHHH		53.4323000965
261UbiquitinationLDLHKSLVCTALRGK
HHHHHHHHHHHHHHC		3.3523000965
268UbiquitinationVCTALRGKLGVFSEM
HHHHHHHCCCCCCHH		35.3223000965
273UbiquitinationRGKLGVFSEMEANFK
HHCCCCCCHHHHHHC		33.3621963094
273 (in isoform 2)Ubiquitination-33.3621890473
280 (in isoform 1)Ubiquitination-57.7121890473
280UbiquitinationSEMEANFKNLSRGLV
CHHHHHHCHHHHHHH		57.7121963094
285UbiquitinationNFKNLSRGLVNVAAK
HHCHHHHHHHHHHHH		30.5129967540
290UbiquitinationSRGLVNVAAKLTHNK
HHHHHHHHHHHHCCC		8.1529967540
292UbiquitinationGLVNVAAKLTHNKDV
HHHHHHHHHHCCCCH		44.1529967540
297UbiquitinationAAKLTHNKDVRDLFV
HHHHHCCCCHHHHHH		50.4229967540
331PhosphorylationVRFFLNQYSASVHSL
HHHHHHHHCCCHHCC		12.7227732954
332PhosphorylationRFFLNQYSASVHSLD
HHHHHHHCCCHHCCC		12.3327732954
334PhosphorylationFLNQYSASVHSLDGF
HHHHHCCCHHCCCCC		17.8927732954
337PhosphorylationQYSASVHSLDGFRHQ
HHCCCHHCCCCCHHH		26.4627732954
353PhosphorylationLWDRYMGTLRGCLLR
HHHHHHHHHHHHHHH		9.2128060719
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 FIBP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FIBP_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 FIBP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
C2CD5_HUMANC2CD5physical
17353931
OGT1_HUMANOGTphysical
17353931
IF6_HUMANEIF6physical
17353931
GEMI4_HUMANGEMIN4physical
17353931
AP4B1_HUMANAP4B1physical
17353931
CLC2L_HUMANCLEC2Lphysical
17353931
MIF_HUMANMIFphysical
17353931
A4_HUMANAPPphysical
21832049
C2CD5_HUMANC2CD5physical
26186194
TMM94_HUMANKIAA0195physical
26186194
CABL2_HUMANCABLES2physical
26186194
CABL1_HUMANCABLES1physical
26186194
CDK5_HUMANCDK5physical
26186194
GRM1C_HUMANGRAMD1Cphysical
26186194
CDK5_HUMANCDK5physical
28514442
C2CD5_HUMANC2CD5physical
28514442
CABL2_HUMANCABLES2physical
28514442
CABL1_HUMANCABLES1physical
28514442
TMM94_HUMANKIAA0195physical
28514442
GRM1C_HUMANGRAMD1Cphysical
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 FIBP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2, AND MASSSPECTROMETRY.

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