F149B_HUMAN - dbPTM
F149B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F149B_HUMAN
UniProt AC Q96BN6
Protein Name Protein FAM149B1
Gene Name FAM149B1
Organism Homo sapiens (Human).
Sequence Length 582
Subcellular Localization
Protein Description
Protein Sequence MISRYTRKAVPQSLELKGITKHALNHHPPPEKLEEISPTSDSHEKDTSSQSKSDITRESSFTSADTGNSLSAFPSYTGAGISTEGSSDFSWGYGELDQNATEKVQTMFTAIDELLYEQKLSVHTKSLQEECQQWTASFPHLRILGRQIITPSEGYRLYPRSPSAVSASYETTLSQERDSTIFGIRGKKLHFSSSYAHKASSIAKSSSFCSMERDEEDSIIVSEGIIEEYLAFDHIDIEEGFHGKKSEAATEKQKLGYPPIAPFYCMKEDVLAYVFDSVWCKVVSCMEQLTRSHWEGFASDDESNVAVTRPDSESSCVLSELHPLVLPRVPQSKVLYITSNPMSLCQASRHQPNVNDLLVHGMPLQPRNLSLMDKLLDLDDKLLMRPGSSTILSTRNWPNRAVEFSTSSLSYTVQSTRRRNPPPRTLHPISTSHSCAETPRSVEEILRGARVPVAPDSLSSPSPTPLSRNNLLPPIGTAEVEHVSTVGPQRQMKPHGDSSRAQSAVVDEPNYQQPQERLLLPDFFPRPNTTQSFLLDTQYRRSCAVEYPHQARPGRGSAGPQLHGSTKSQSGGRPVSRTRQGP
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
6Phosphorylation--MISRYTRKAVPQS
--CCCCCCCCCCCCC
25.28-
37PhosphorylationPEKLEEISPTSDSHE
HHHHHHCCCCCCCCC
25.9629255136
39PhosphorylationKLEEISPTSDSHEKD
HHHHCCCCCCCCCCC
38.0729255136
40PhosphorylationLEEISPTSDSHEKDT
HHHCCCCCCCCCCCC
40.2629255136
42PhosphorylationEISPTSDSHEKDTSS
HCCCCCCCCCCCCCC
33.0627251275
116PhosphorylationTAIDELLYEQKLSVH
HHHHHHHHHHHCCHH
29.0119413330
135PhosphorylationQEECQQWTASFPHLR
HHHHHHHHHHCCCCE
14.2123401153
137PhosphorylationECQQWTASFPHLRIL
HHHHHHHHCCCCEEE
31.7523401153
150PhosphorylationILGRQIITPSEGYRL
EECEEEECCCCCCCC
23.5324043423
152PhosphorylationGRQIITPSEGYRLYP
CEEEECCCCCCCCCC
34.7024043423
155PhosphorylationIITPSEGYRLYPRSP
EECCCCCCCCCCCCH
8.0624043423
158PhosphorylationPSEGYRLYPRSPSAV
CCCCCCCCCCCHHCC
6.3924043423
166PhosphorylationPRSPSAVSASYETTL
CCCHHCCCEEEECCC
15.9424275569
168PhosphorylationSPSAVSASYETTLSQ
CHHCCCEEEECCCCC
18.9224275569
192PhosphorylationRGKKLHFSSSYAHKA
CCCEEEECCCHHHHH
13.97-
193PhosphorylationGKKLHFSSSYAHKAS
CCEEEECCCHHHHHH
26.82-
200PhosphorylationSSYAHKASSIAKSSS
CCHHHHHHHHHHCCC
27.38-
201PhosphorylationSYAHKASSIAKSSSF
CHHHHHHHHHHCCCC
31.27-
257PhosphorylationTEKQKLGYPPIAPFY
HHHHHHCCCCCCCCE
19.10-
264PhosphorylationYPPIAPFYCMKEDVL
CCCCCCCEECHHHHH
7.20-
299PhosphorylationSHWEGFASDDESNVA
HHHCCCCCCCCCCEE
43.2528348404
303PhosphorylationGFASDDESNVAVTRP
CCCCCCCCCEEEECC
43.5328348404
340 (in isoform 2)Phosphorylation-27.8722210691
389PhosphorylationLLMRPGSSTILSTRN
EECCCCCCCEEECCC
25.9430631047
485PhosphorylationAEVEHVSTVGPQRQM
EEEEEEEECCCCCCC
28.5222210691
529PhosphorylationDFFPRPNTTQSFLLD
CCCCCCCCCCHHHHC
28.9729978859
530PhosphorylationFFPRPNTTQSFLLDT
CCCCCCCCCHHHHCC
28.9329978859
532PhosphorylationPRPNTTQSFLLDTQY
CCCCCCCHHHHCCCH
18.7729978859
537PhosphorylationTQSFLLDTQYRRSCA
CCHHHHCCCHHHHCC
27.7229978859
539PhosphorylationSFLLDTQYRRSCAVE
HHHHCCCHHHHCCCC
15.3029978859

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 F149B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F149B_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 F149B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BROMI_HUMANTBC1D32physical
26186194
BROMI_HUMANTBC1D32physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of F149B_HUMAN

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Related Literatures of Post-Translational Modification

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