FOXP1_HUMAN - dbPTM
FOXP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOXP1_HUMAN
UniProt AC Q9H334
Protein Name Forkhead box protein P1
Gene Name FOXP1
Organism Homo sapiens (Human).
Sequence Length 677
Subcellular Localization Nucleus . Not found in the nucleolus.
Protein Description Transcriptional repressor. [PubMed: 18347093]
Protein Sequence MMQESGTETKSNGSAIQNGSGGSNHLLECGGLREGRSNGETPAVDIGAADLAHAQQQQQQALQVARQLLLQQQQQQQVSGLKSPKRNDKQPALQVPVSVAMMTPQVITPQQMQQILQQQVLSPQQLQVLLQQQQALMLQQQQLQEFYKKQQEQLQLQLLQQQHAGKQPKEQQQVATQQLAFQQQLLQMQQLQQQHLLSLQRQGLLTIQPGQPALPLQPLAQGMIPTELQQLWKEVTSAHTAEETTGNNHSSLDLTTTCVSSSAPSKTSLIMNPHASTNGQLSVHTPKRESLSHEEHPHSHPLYGHGVCKWPGCEAVCEDFQSFLKHLNSEHALDDRSTAQCRVQMQVVQQLELQLAKDKERLQAMMTHLHVKSTEPKAAPQPLNLVSSVTLSKSASEASPQSLPHTPTTPTAPLTPVTQGPSVITTTSMHTVGPIRRRYSDKYNVPISSADIAQNQEFYKNAEVRPPFTYASLIRQAILESPEKQLTLNEIYNWFTRMFAYFRRNAATWKNAVRHNLSLHKCFVRVENVKGAVWTVDEVEFQKRRPQKISGNPSLIKNMQSSHAYCTPLNAALQASMAENSIPLYTTASMGNPTLGNLASAIREELNGAMEHTNSNESDSSPGRSPMQAVHPVHVKEEPLDPEEAEGPLSLVTTANHSPDFDHDRDYEDEPVNEDME
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
25PhosphorylationNGSGGSNHLLECGGL
CCCCCCCCEEEECCC
33.2327251275
25 (in isoform 3)Phosphorylation-33.2327251275
25 (in isoform 4)Phosphorylation-33.2327251275
27PhosphorylationSGGSNHLLECGGLRE
CCCCCCEEEECCCCC
3.8827251275
27 (in isoform 3)Phosphorylation-3.8827251275
27 (in isoform 4)Phosphorylation-3.8827251275
29PhosphorylationGSNHLLECGGLREGR
CCCCEEEECCCCCCC
5.4527251275
29 (in isoform 3)Phosphorylation-5.4527251275
29 (in isoform 4)Phosphorylation-5.4527251275
32 (in isoform 3)Phosphorylation-2.4627251275
32 (in isoform 4)Phosphorylation-2.4627251275
40 (in isoform 3)Phosphorylation-56.7329083192
40 (in isoform 4)Phosphorylation-56.7329083192
41 (in isoform 3)Phosphorylation-20.2529083192
41 (in isoform 4)Phosphorylation-20.2529083192
44 (in isoform 3)Phosphorylation-6.0829083192
44 (in isoform 4)Phosphorylation-6.0829083192
79PhosphorylationQQQQQQVSGLKSPKR
HHHHHHHCCCCCCCC
33.7923401153
81 (in isoform 5)Phosphorylation-3.7528176443
82UbiquitinationQQQVSGLKSPKRNDK
HHHHCCCCCCCCCCC
69.14-
82 (in isoform 5)Phosphorylation-69.1428176443
83PhosphorylationQQVSGLKSPKRNDKQ
HHHCCCCCCCCCCCC
40.4723401153
83 (in isoform 6)Phosphorylation-40.4729116813
85 (in isoform 3)Phosphorylation-71.5629116813
100 (in isoform 5)Phosphorylation-3.7328176443
103 (in isoform 5)Phosphorylation-9.4828176443
112 (in isoform 5)Phosphorylation-2.3928176443
149UbiquitinationQLQEFYKKQQEQLQL
HHHHHHHHHHHHHHH
45.92-
166UbiquitinationLQQQHAGKQPKEQQQ
HHHHHCCCCCHHHHH
65.30-
198PhosphorylationLQQQHLLSLQRQGLL
HHHHHHHHHHHCCCE
28.9024719451
276PhosphorylationLIMNPHASTNGQLSV
EEECCCCCCCCCEEE
21.2619690332
285PhosphorylationNGQLSVHTPKRESLS
CCCEEEECCCCCCCC
28.4925159151
287SumoylationQLSVHTPKRESLSHE
CEEEECCCCCCCCCC
70.7028112733
290PhosphorylationVHTPKRESLSHEEHP
EECCCCCCCCCCCCC
38.9227251275
292PhosphorylationTPKRESLSHEEHPHS
CCCCCCCCCCCCCCC
37.8227251275
299PhosphorylationSHEEHPHSHPLYGHG
CCCCCCCCCCCCCCC
31.1127251275
322PhosphorylationAVCEDFQSFLKHLNS
HHHHHHHHHHHHCCC
32.3224719451
329O-linked_GlycosylationSFLKHLNSEHALDDR
HHHHHCCCCCCCCCC
36.8032574038
336MethylationSEHALDDRSTAQCRV
CCCCCCCCCHHHHHH
35.26-
362 (in isoform 4)Ubiquitination-3.90-
367PhosphorylationERLQAMMTHLHVKST
HHHHHHHHHHHHCCC
14.27-
372SumoylationMMTHLHVKSTEPKAA
HHHHHHHCCCCCCCC
40.7028112733
377SumoylationHVKSTEPKAAPQPLN
HHCCCCCCCCCCCCE
51.4528112733
377UbiquitinationHVKSTEPKAAPQPLN
HHCCCCCCCCCCCCE
51.45-
387PhosphorylationPQPLNLVSSVTLSKS
CCCCEEEEEEEECCC
23.4327251275
388PhosphorylationQPLNLVSSVTLSKSA
CCCEEEEEEEECCCH
16.1928555341
390PhosphorylationLNLVSSVTLSKSASE
CEEEEEEEECCCHHC
27.5427251275
392PhosphorylationLVSSVTLSKSASEAS
EEEEEEECCCHHCCC
18.3927251275
394PhosphorylationSSVTLSKSASEASPQ
EEEEECCCHHCCCCC
33.3829449344
396PhosphorylationVTLSKSASEASPQSL
EEECCCHHCCCCCCC
40.5629449344
399PhosphorylationSKSASEASPQSLPHT
CCCHHCCCCCCCCCC
21.3029449344
402PhosphorylationASEASPQSLPHTPTT
HHCCCCCCCCCCCCC
47.4529449344
406PhosphorylationSPQSLPHTPTTPTAP
CCCCCCCCCCCCCCC
22.0129449344
408O-linked_GlycosylationQSLPHTPTTPTAPLT
CCCCCCCCCCCCCCC
46.7132574038
408PhosphorylationQSLPHTPTTPTAPLT
CCCCCCCCCCCCCCC
46.7128348404
409PhosphorylationSLPHTPTTPTAPLTP
CCCCCCCCCCCCCCC
21.6128348404
411O-linked_GlycosylationPHTPTTPTAPLTPVT
CCCCCCCCCCCCCCC
38.5232574038
411PhosphorylationPHTPTTPTAPLTPVT
CCCCCCCCCCCCCCC
38.5228348404
415O-linked_GlycosylationTTPTAPLTPVTQGPS
CCCCCCCCCCCCCCC
18.0432574038
415PhosphorylationTTPTAPLTPVTQGPS
CCCCCCCCCCCCCCC
18.0429449344
418O-linked_GlycosylationTAPLTPVTQGPSVIT
CCCCCCCCCCCCEEE
29.0732574038
418PhosphorylationTAPLTPVTQGPSVIT
CCCCCCCCCCCCEEE
29.0729449344
422O-linked_GlycosylationTPVTQGPSVITTTSM
CCCCCCCCEEEECCC
32.7332574038
422PhosphorylationTPVTQGPSVITTTSM
CCCCCCCCEEEECCC
32.7329449344
427O-linked_GlycosylationGPSVITTTSMHTVGP
CCCEEEECCCCCCCC
18.5332574038
439PhosphorylationVGPIRRRYSDKYNVP
CCCCCHHCCCCCCCC
21.2923401153
439 (in isoform 7)Phosphorylation-21.2926434776
440PhosphorylationGPIRRRYSDKYNVPI
CCCCHHCCCCCCCCC
26.3023401153
440 (in isoform 7)Phosphorylation-26.3028450419
442PhosphorylationIRRRYSDKYNVPISS
CCHHCCCCCCCCCCH
32.5527642862
442SumoylationIRRRYSDKYNVPISS
CCHHCCCCCCCCCCH
32.5528112733
443PhosphorylationRRRYSDKYNVPISSA
CHHCCCCCCCCCCHH
26.7827134283
443 (in isoform 7)Phosphorylation-26.7826434776
445PhosphorylationRYSDKYNVPISSADI
HCCCCCCCCCCHHHH
3.9627642862
448O-linked_GlycosylationDKYNVPISSADIAQN
CCCCCCCCHHHHHHC
17.2632574038
448PhosphorylationDKYNVPISSADIAQN
CCCCCCCCHHHHHHC
17.2628450419
448 (in isoform 7)Phosphorylation-17.2626434776
449O-linked_GlycosylationKYNVPISSADIAQNQ
CCCCCCCHHHHHHCH
30.5832574038
449PhosphorylationKYNVPISSADIAQNQ
CCCCCCCHHHHHHCH
30.5828450419
449 (in isoform 7)Phosphorylation-30.5826434776
460UbiquitinationAQNQEFYKNAEVRPP
HHCHHHHHCCCCCCC
55.81-
472PhosphorylationRPPFTYASLIRQAIL
CCCCCHHHHHHHHHH
17.5728555341
518PhosphorylationNAVRHNLSLHKCFVR
HHHHHHCEEEEEEEE
33.47-
521UbiquitinationRHNLSLHKCFVRVEN
HHHCEEEEEEEEEEE
34.36-
543UbiquitinationVDEVEFQKRRPQKIS
EEEEEHHHCCCCCCC
56.55-
554PhosphorylationQKISGNPSLIKNMQS
CCCCCCHHHHHHCCC
46.8824719451
613PhosphorylationLNGAMEHTNSNESDS
HHHHHCCCCCCCCCC
27.3425850435
615PhosphorylationGAMEHTNSNESDSSP
HHHCCCCCCCCCCCC
43.0325850435
618PhosphorylationEHTNSNESDSSPGRS
CCCCCCCCCCCCCCC
47.2222496350
620PhosphorylationTNSNESDSSPGRSPM
CCCCCCCCCCCCCCC
47.9525849741
621PhosphorylationNSNESDSSPGRSPMQ
CCCCCCCCCCCCCCC
36.0428192239
625PhosphorylationSDSSPGRSPMQAVHP
CCCCCCCCCCCCCCC
30.5525849741
634PhosphorylationMQAVHPVHVKEEPLD
CCCCCCCEECCCCCC
29.4027251275
636PhosphorylationAVHPVHVKEEPLDPE
CCCCCEECCCCCCHH
41.2927251275
636SumoylationAVHPVHVKEEPLDPE
CCCCCEECCCCCCHH
41.29-
641PhosphorylationHVKEEPLDPEEAEGP
EECCCCCCHHHCCCC
60.3227251275
650PhosphorylationEEAEGPLSLVTTANH
HHCCCCEEEEEECCC
24.7520873877
653PhosphorylationEGPLSLVTTANHSPD
CCCEEEEEECCCCCC
26.0330266825
654PhosphorylationGPLSLVTTANHSPDF
CCEEEEEECCCCCCC
20.2730266825
658PhosphorylationLVTTANHSPDFDHDR
EEEECCCCCCCCCCC
26.4430266825
666PhosphorylationPDFDHDRDYEDEPVN
CCCCCCCCCCCCCCC
58.1727251275
667PhosphorylationDFDHDRDYEDEPVNE
CCCCCCCCCCCCCCC
26.6126074081

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 FOXP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOXP1_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 FOXP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FOXP1_HUMANFOXP1physical
14701752
FOXP2_HUMANFOXP2physical
14701752
FOXP4_HUMANFOXP4physical
14701752
P66B_HUMANGATAD2Bphysical
20185820
MTA1_HUMANMTA1physical
20185820
NCOR2_HUMANNCOR2physical
18347093
IL3RA_HUMANIL3RAphysical
21988832
FOXP2_HUMANFOXP2physical
25609649
FOXP4_HUMANFOXP4physical
25609649
RCC1_HUMANRCC1physical
25609649
HXD13_HUMANHOXD13physical
25609649
QSER1_HUMANQSER1physical
25609649
SATB1_HUMANSATB1physical
25609649
SATB2_HUMANSATB2physical
25609649
CTBP2_HUMANCTBP2physical
25609649
MYH10_HUMANMYH10physical
25609649
DNLI3_HUMANLIG3physical
25609649
PEO1_HUMANC10orf2physical
25609649
CUX1_HUMANCUX1physical
25609649
CASP_HUMANCUX1physical
25609649
VRK3_HUMANVRK3physical
25609649
XRCC1_HUMANXRCC1physical
25609649
CHD1L_HUMANCHD1Lphysical
25609649
RFA2_HUMANRPA2physical
25609649
BLM_HUMANBLMphysical
25609649
MRE11_HUMANMRE11Aphysical
25609649
ML12B_HUMANMYL12Bphysical
25609649
TBP_HUMANTBPphysical
25609649
P53_HUMANTP53physical
25609649
TTF2_HUMANTTF2physical
25609649
ZBT10_HUMANZBTB10physical
25609649
MYL9_HUMANMYL9physical
25609649
RFA3_HUMANRPA3physical
25609649
TFCP2_HUMANTFCP2physical
25609649
TOP2A_HUMANTOP2Aphysical
25609649
UBIP1_HUMANUBP1physical
25609649
AURKA_HUMANAURKAphysical
28218735
IKZF1_HUMANIKZF1physical
27588474

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=A chromosomal aberration involving FOXP1 is found in acute lymphoblastic leukemia. Translocation t(9
3)(p13
p14.1) with PAX5.
613670
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FOXP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND MASSSPECTROMETRY.

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