F171B_HUMAN - dbPTM
F171B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F171B_HUMAN
UniProt AC Q6P995
Protein Name Protein FAM171B
Gene Name FAM171B
Organism Homo sapiens (Human).
Sequence Length 826
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description
Protein Sequence MARLCRRVPCTLLLGLAVVLLKARLVPAAARAELSRSDLSLIQQQQQQQQQQQQQQKQLEEAEEERTEVPGATSTLTVPVSVFMLKVQVNDIISRQYLSQAVVEVFVNYTKTNSTVTKSNGAVLIKVPYKLGLSLTIIAYKDGYVLTPLPWKTRRMPIYSSVTLSLFPQSQANIWLFEDTVLITGKLADAKSQPSVQFSKALIKLPDNHHISNVTGYLTVLQQFLKVDNFLHTTGITLNKPGFENIELTPLAAICVKIYSGGKELKVNGSIQVSLPLLRLNDISAGDRIPAWTFDMNTGAWVNHGRGMVKEHNNHLIWTYDAPHLGYWIAAPLPGTRGSGINEDSKDITAYHTVFLTAILGGTIVIVIGFFAVLLCYCRDKCGTPQKRERNITKLEVLKRDQTTSTTHINHISTVKVALKAEDKSQLFNAKNSSYSPQKKEPSKAETEERVSMVKTRDDFKIYNEDVSFLSVNQNNYSRNPTQSLEPNVGSKQPKHINNNLSSSLGDAQDEKRYLTGNEEAYGRSHIPEQLMHIYSQPIAILQTSDLFSTPEQLHTAKSATLPRKGQLVYGQLMEPVNRENFTQTLPKMPIHSHAQPPDAREEDIILEGQQSLPSQASDWSRYSSSLLESVSVPGTLNEAVVMTPFSSELQGISEQTLLELSKGKPSPHPRAWFVSLDGKPVAQVRHSFIDLKKGKRTQSNDTSLDSGVDMNELHSSRKLEREKTFIKSMHQPKILYLEDLDLSSSESGTTVCSPEDPALRHILDGGSGVIMEHPGEESPGRKSTVEDFEANTSPTKRRGRPPLAKRDSKTNIWKKREERPLIPIN
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
108N-linked_GlycosylationAVVEVFVNYTKTNST
HHHHHEEECCCCCCE
27.56UniProtKB CARBOHYD
113N-linked_GlycosylationFVNYTKTNSTVTKSN
EEECCCCCCEEEECC
36.92UniProtKB CARBOHYD
114PhosphorylationVNYTKTNSTVTKSNG
EECCCCCCEEEECCC
29.5023898821
115PhosphorylationNYTKTNSTVTKSNGA
ECCCCCCEEEECCCE
33.9723898821
153PhosphorylationLTPLPWKTRRMPIYS
EECCCCCCCCCCCCE
21.4623403867
184PhosphorylationFEDTVLITGKLADAK
EECEEEEECCCCCCC
24.8923403867
192PhosphorylationGKLADAKSQPSVQFS
CCCCCCCCCCCCEEE
49.3923403867
195PhosphorylationADAKSQPSVQFSKAL
CCCCCCCCCEEEEEH
22.4023403867
199PhosphorylationSQPSVQFSKALIKLP
CCCCCEEEEEHHCCC
10.4223403867
213N-linked_GlycosylationPDNHHISNVTGYLTV
CCCCCCCCHHHHHHH
34.46UniProtKB CARBOHYD
268N-linked_GlycosylationGGKELKVNGSIQVSL
CCEEEEECCEEEEEE
36.59UniProtKB CARBOHYD
393PhosphorylationQKRERNITKLEVLKR
CHHCCCCCEEEEEEC
32.8823312004
394UbiquitinationKRERNITKLEVLKRD
HHCCCCCEEEEEECC
38.5633845483
403PhosphorylationEVLKRDQTTSTTHIN
EEEECCCCCCCEEEC
27.3123403867
404PhosphorylationVLKRDQTTSTTHINH
EEECCCCCCCEEECE
20.6026657352
405PhosphorylationLKRDQTTSTTHINHI
EECCCCCCCEEECEE
34.3925849741
406PhosphorylationKRDQTTSTTHINHIS
ECCCCCCCEEECEEE
21.9426657352
407PhosphorylationRDQTTSTTHINHIST
CCCCCCCEEECEEEE
22.1123403867
413PhosphorylationTTHINHISTVKVALK
CEEECEEEEEEEEEE
21.4323403867
414PhosphorylationTHINHISTVKVALKA
EEECEEEEEEEEEEC
24.6023403867
424UbiquitinationVALKAEDKSQLFNAK
EEEECCCHHHHHCCC
31.4430230243
425PhosphorylationALKAEDKSQLFNAKN
EEECCCHHHHHCCCC
44.42-
433PhosphorylationQLFNAKNSSYSPQKK
HHHCCCCCCCCCCCC
29.9123312004
434PhosphorylationLFNAKNSSYSPQKKE
HHCCCCCCCCCCCCC
38.7423312004
435PhosphorylationFNAKNSSYSPQKKEP
HCCCCCCCCCCCCCC
24.9623312004
436PhosphorylationNAKNSSYSPQKKEPS
CCCCCCCCCCCCCCC
23.8523312004
443PhosphorylationSPQKKEPSKAETEER
CCCCCCCCCHHHHHH
45.6623312004
447PhosphorylationKEPSKAETEERVSMV
CCCCCHHHHHHHEEE
48.2623312004
452PhosphorylationAETEERVSMVKTRDD
HHHHHHHEEEECCCC
24.8729514088
477PhosphorylationLSVNQNNYSRNPTQS
EECCCCCCCCCCCCC
19.2925884760
491PhosphorylationSLEPNVGSKQPKHIN
CCCCCCCCCCCHHCC
24.6830576142
495UbiquitinationNVGSKQPKHINNNLS
CCCCCCCHHCCCCCC
55.4030230243
502PhosphorylationKHINNNLSSSLGDAQ
HHCCCCCCHHCCCCC
21.7223403867
503PhosphorylationHINNNLSSSLGDAQD
HCCCCCCHHCCCCCH
32.5223403867
504PhosphorylationINNNLSSSLGDAQDE
CCCCCCHHCCCCCHH
32.7521082442
512UbiquitinationLGDAQDEKRYLTGNE
CCCCCHHHHHHCCCH
55.4130230243
514PhosphorylationDAQDEKRYLTGNEEA
CCCHHHHHHCCCHHH
21.4927642862
522PhosphorylationLTGNEEAYGRSHIPE
HCCCHHHHCCCCCCH
19.1525884760
561PhosphorylationLHTAKSATLPRKGQL
HCCCCCCCCCCCCCE
44.3724719451
565UbiquitinationKSATLPRKGQLVYGQ
CCCCCCCCCCEEEEE
49.4130230243
570PhosphorylationPRKGQLVYGQLMEPV
CCCCCEEEEEECCCC
14.0325884760
583PhosphorylationPVNRENFTQTLPKMP
CCCCCCCCCCCCCCC
32.0225850435
585PhosphorylationNRENFTQTLPKMPIH
CCCCCCCCCCCCCCC
41.8029255136
688PhosphorylationPVAQVRHSFIDLKKG
EEEEEEEEEEECCCC
17.2123312004
725PhosphorylationRKLEREKTFIKSMHQ
HHHHHHHHHHHHCCC
26.3229514088
737PhosphorylationMHQPKILYLEDLDLS
CCCCEEEEEEECCCC
16.1222468782
745PhosphorylationLEDLDLSSSESGTTV
EEECCCCCCCCCCEE
45.4822468782
750PhosphorylationLSSSESGTTVCSPED
CCCCCCCCEEECCCC
25.9024076635
751PhosphorylationSSSESGTTVCSPEDP
CCCCCCCEEECCCCH
24.0422468782
754PhosphorylationESGTTVCSPEDPALR
CCCCEEECCCCHHHH
27.3024076635
768PhosphorylationRHILDGGSGVIMEHP
HHHHHCCCCCEEECC
35.1027732954
779PhosphorylationMEHPGEESPGRKSTV
EECCCCCCCCCCCCH
28.4917081983
781PhosphorylationHPGEESPGRKSTVED
CCCCCCCCCCCCHHH
59.9517081983
784PhosphorylationEESPGRKSTVEDFEA
CCCCCCCCCHHHHHH
36.0023312004
785PhosphorylationESPGRKSTVEDFEAN
CCCCCCCCHHHHHHC
30.8329255136
793PhosphorylationVEDFEANTSPTKRRG
HHHHHHCCCCCCCCC
43.0330266825
794PhosphorylationEDFEANTSPTKRRGR
HHHHHCCCCCCCCCC
30.3129255136
796PhosphorylationFEANTSPTKRRGRPP
HHHCCCCCCCCCCCC
36.6329255136
809PhosphorylationPPLAKRDSKTNIWKK
CCCCCCCCCCCCCCC
45.4729496963
811PhosphorylationLAKRDSKTNIWKKRE
CCCCCCCCCCCCCCC
35.5724719451

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 F171B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F171B_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 F171B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPP3_HUMANMPP3physical
21988832
F1711_HUMANFAM171A1physical
28514442
F1712_HUMANFAM171A2physical
28514442
CO4A_HUMANC4Aphysical
28514442
FGFR2_HUMANFGFR2physical
28514442
BMR1A_HUMANBMPR1Aphysical
28514442
STX6_HUMANSTX6physical
28514442
MFAP3_HUMANMFAP3physical
28514442
MIB1_HUMANMIB1physical
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 F171B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-779, AND MASSSPECTROMETRY.

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