FEM1B_HUMAN - dbPTM
FEM1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FEM1B_HUMAN
UniProt AC Q9UK73
Protein Name Protein fem-1 homolog B
Gene Name FEM1B
Organism Homo sapiens (Human).
Sequence Length 627
Subcellular Localization Cytoplasm . Nucleus . In the nucleus, the protein level increased slightly after camptothecin (CPT) treatment. Associated with chromatin.
Protein Description Component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit. Involved in apoptosis by acting as a death receptor-associated protein that mediates apoptosis. Also involved in glucose homeostasis in pancreatic islet. Functions as an adapter/mediator in replication stress-induced signaling that leads to the activation of CHEK1..
Protein Sequence MEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARNGHAKVVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVELLLSHADCDRRSRIEALELLGASFANDRENYDIIKTYHYLYLAMLERFQDGDNILEKEVLPPIHAYGNRTECRNPQELESIRQDRDALHMEGLIVRERILGADNIDVSHPIIYRGAVYADNMEFEQCIKLWLHALHLRQKGNRNTHKDLLRFAQVFSQMIHLNETVKAPDIECVLRCSVLEIEQSMNRVKNISDADVHNAMDNYECNLYTFLYLVCISTKTQCSEEDQCKINKQIYNLIHLDPRTREGFTLLHLAVNSNTPVDDFHTNDVCSFPNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPISDFLTLHSIIISLVEAGAHTDMTNKQNKTPLDKSTTGVSEILLKTQMKMSLKCLAARAVRANDINYQDQIPRTLEEFVGFH
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
7Phosphorylation-MEGLAGYVYKAASE
-CCCHHHHHHHHHHH		8.5929449344
9PhosphorylationEGLAGYVYKAASEGK
CCHHHHHHHHHHHCC		6.0929449344
13PhosphorylationGYVYKAASEGKVLTL
HHHHHHHHHCCHHHH		52.3129449344
34PhosphorylationRSESDIRYLLGYVSQ
CCHHHHHHHHHHHHC		13.4519835603
38PhosphorylationDIRYLLGYVSQQGGQ
HHHHHHHHHHCCCCC		9.2621964256
40PhosphorylationRYLLGYVSQQGGQRS
HHHHHHHHCCCCCCC		14.3321060948
60UbiquitinationAARNGHAKVVRLLLE
EECCCCHHHHHHHHH		35.2721890473
120PhosphorylationNVNHTTVTNSTPLRA
CCCCCEECCCCCCCC		22.7422798277
122PhosphorylationNHTTVTNSTPLRAAC
CCCEECCCCCCCCHH		23.2624719451
153PhosphorylationNISIANKYDNTCLMI
CEEEEECCCCCEEEE		17.7721214269
156PhosphorylationIANKYDNTCLMIAAY
EEECCCCCEEEEEEE		12.2428270605
163PhosphorylationTCLMIAAYKGHTDVV
CEEEEEEECCCHHHH		14.4221214269
231UbiquitinationKVAAESCKADVVELL
HHHHHHCCCHHHHHH		57.83-
248PhosphorylationHADCDRRSRIEALEL
CCCCCHHHHHHHHHH		38.2022210691
259PhosphorylationALELLGASFANDREN
HHHHHCCCCCCCCCC		24.0822210691
267PhosphorylationFANDRENYDIIKTYH
CCCCCCCCHHHHHHH		12.0822210691
308UbiquitinationAYGNRTECRNPQELE
CCCCCCCCCCHHHHH		5.1423000965
311UbiquitinationNRTECRNPQELESIR
CCCCCCCHHHHHHHH		15.0721890473
436UbiquitinationSDADVHNAMDNYECN
CHHHHHHHHHHCCCC		7.5723000965
440UbiquitinationVHNAMDNYECNLYTF
HHHHHHHCCCCHHHH		20.0023000965
466UbiquitinationCSEEDQCKINKQIYN
CCHHHHHHHHHHHHH		43.6223000965
469UbiquitinationEDQCKINKQIYNLIH
HHHHHHHHHHHHHHH		41.3623000965
472PhosphorylationCKINKQIYNLIHLDP
HHHHHHHHHHHHCCC		11.0424043423
481PhosphorylationLIHLDPRTREGFTLL
HHHCCCCCCCCEEEE		38.1624043423
575PhosphorylationMTNKQNKTPLDKSTT
CCCCCCCCCCCCCCC		36.31-
579UbiquitinationQNKTPLDKSTTGVSE
CCCCCCCCCCCCHHH		58.3429967540
594UbiquitinationILLKTQMKMSLKCLA
HHHHHHHHHHHHHHH		18.6023000965
598UbiquitinationTQMKMSLKCLAARAV
HHHHHHHHHHHHHHH		21.6423000965
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 FEM1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FEM1B_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 FEM1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELOC_HUMANTCEB1physical
19855191
RACK1_HUMANGNB2L1physical
19855191
CUL2_HUMANCUL2physical
18187417
CUL5_HUMANCUL5physical
18187417
ELOB_HUMANTCEB2physical
18187417
ELOC_HUMANTCEB1physical
18187417
CHK1_HUMANCHEK1physical
19330022
RAD9A_HUMANRAD9Aphysical
19330022
CUL2_HUMANCUL2physical
15601820
RBX1_HUMANRBX1physical
15601820
ELOB_HUMANTCEB2physical
15601820
ELOC_HUMANTCEB1physical
15601820
GLI1_HUMANGLI1physical
24076122
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 FEM1B_HUMAN

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Related Literatures of Post-Translational Modification

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