FHL1_HUMAN - dbPTM
FHL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FHL1_HUMAN
UniProt AC Q13642
Protein Name Four and a half LIM domains protein 1
Gene Name FHL1
Organism Homo sapiens (Human).
Sequence Length 323
Subcellular Localization Isoform 1: Cytoplasm.
Isoform 3: Cytoplasm. Nucleus.
Isoform 2: Nucleus. Cytoplasm, cytosol. Predominantly nuclear in myoblasts but is cytosolic in differentiated myotubes.
Protein Description May have an involvement in muscle development or hypertrophy..
Protein Sequence MAEKFDCHYCRDPLQGKKYVQKDGHHCCLKCFDKFCANTCVECRKPIGADSKEVHYKNRFWHDTCFRCAKCLHPLANETFVAKDNKILCNKCTTREDSPKCKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGTGSFFPKGEDFYCVTCHETKFAKHCVKCNKAITSGGITYQDQPWHADCFVCVTCSKKLAGQRFTAVEDQYYCVDCYKNFVAKKCAGCKNPITGKRTVSRVSHPVSKARKPPVCHGKRLPLTLFPSANLRGRHPGGERTCPSWVVVLYRKNRSLAAPRGPGLVKAPVWWPMKDNPGTTTASTAKNAP
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
2 (in isoform 4)Phosphorylation-28.7824043423
4 (in isoform 4)Phosphorylation-36.6424043423
4Malonylation----MAEKFDCHYCR
----CCCCCCCCCCC
36.6426320211
4Acetylation----MAEKFDCHYCR
----CCCCCCCCCCC
36.64-
7 (in isoform 4)Phosphorylation-2.5124043423
7 (in isoform 5)Phosphorylation-2.5126657352
9PhosphorylationAEKFDCHYCRDPLQG
CCCCCCCCCCCCCCC
8.7726437602
10 (in isoform 5)Phosphorylation-1.4526437602
11 (in isoform 5)Phosphorylation-41.2226437602
16 (in isoform 5)Phosphorylation-35.7826437602
17 (in isoform 4)Phosphorylation-28.1524043423
18 (in isoform 4)Phosphorylation-58.4324043423
22AcetylationQGKKYVQKDGHHCCL
CCCCEECCCCCEEEH
56.4823749302
23 (in isoform 4)Phosphorylation-44.5624043423
24 (in isoform 4)Phosphorylation-21.3424043423
25 (in isoform 4)Phosphorylation-22.4224043423
29 (in isoform 4)Phosphorylation-7.0526437602
51PhosphorylationRKPIGADSKEVHYKN
CCCCCCCCCEEECCC
30.1319764811
572-HydroxyisobutyrylationDSKEVHYKNRFWHDT
CCCEEECCCCCCCHH
27.11-
59MethylationKEVHYKNRFWHDTCF
CEEECCCCCCCHHHH
31.70-
64PhosphorylationKNRFWHDTCFRCAKC
CCCCCCHHHHHHHHC
10.7228857561
79PhosphorylationLHPLANETFVAKDNK
HHHHCCCEEEECCCE
24.1828857561
86SumoylationTFVAKDNKILCNKCT
EEEECCCEEEECCCC
47.3825218447
86MalonylationTFVAKDNKILCNKCT
EEEECCCEEEECCCC
47.3826320211
86SumoylationTFVAKDNKILCNKCT
EEEECCCEEEECCCC
47.38-
91AcetylationDNKILCNKCTTREDS
CCEEEECCCCCCCCC
31.7725953088
93O-linked_GlycosylationKILCNKCTTREDSPK
EEEECCCCCCCCCCC
30.4230379171
93PhosphorylationKILCNKCTTREDSPK
EEEECCCCCCCCCCC
30.4226437602
98PhosphorylationKCTTREDSPKCKGCF
CCCCCCCCCCCCCCC
22.8526437602
106 (in isoform 3)Ubiquitination-41.0821890473
106 (in isoform 2)Ubiquitination-41.0821890473
106UbiquitinationPKCKGCFKAIVAGDQ
CCCCCCCEEEEECCC
41.0821890473
106 (in isoform 1)Ubiquitination-41.0821890473
106UbiquitinationPKCKGCFKAIVAGDQ
CCCCCCCEEEEECCC
41.0821890473
117PhosphorylationAGDQNVEYKGTVWHK
ECCCCCEECCEEEEC
15.5029978859
118 (in isoform 3)Ubiquitination-34.3021890473
118AcetylationGDQNVEYKGTVWHKD
CCCCCEECCEEEECC
34.3023236377
118UbiquitinationGDQNVEYKGTVWHKD
CCCCCEECCEEEECC
34.3021890473
118UbiquitinationGDQNVEYKGTVWHKD
CCCCCEECCEEEECC
34.3021890473
118 (in isoform 2)Ubiquitination-34.3021890473
118 (in isoform 1)Ubiquitination-34.3021890473
120PhosphorylationQNVEYKGTVWHKDCF
CCCEECCEEEECCCC
19.1026437602
122UbiquitinationVEYKGTVWHKDCFTC
CEECCEEEECCCCCC
7.8321890473
134UbiquitinationFTCSNCKQVIGTGSF
CCCCCCCEEEECCCC
33.9721890473
135UbiquitinationTCSNCKQVIGTGSFF
CCCCCCEEEECCCCC
2.3921890473
138PhosphorylationNCKQVIGTGSFFPKG
CCCEEEECCCCCCCC
20.6628857561
140PhosphorylationKQVIGTGSFFPKGED
CEEEECCCCCCCCCC
24.4528857561
147UbiquitinationSFFPKGEDFYCVTCH
CCCCCCCCEEEEEEC
48.7821890473
149PhosphorylationFPKGEDFYCVTCHET
CCCCCCEEEEEECCC
9.8026437602
157AcetylationCVTCHETKFAKHCVK
EEEECCCCCHHHHHH
40.1025953088
157MalonylationCVTCHETKFAKHCVK
EEEECCCCCHHHHHH
40.1026320211
170PhosphorylationVKCNKAITSGGITYQ
HHCCCCEEECCCCCC
26.6128348404
171PhosphorylationKCNKAITSGGITYQD
HCCCCEEECCCCCCC
28.9828348404
176PhosphorylationITSGGITYQDQPWHA
EEECCCCCCCCCCCC
14.26-
207PhosphorylationFTAVEDQYYCVDCYK
CEEECCEEEEHHHHH
15.9124927040
208PhosphorylationTAVEDQYYCVDCYKN
EEECCEEEEHHHHHH
4.7527196784
213PhosphorylationQYYCVDCYKNFVAKK
EEEEHHHHHHHEEHH
12.4222817900
229 (in isoform 1)Phosphorylation-37.6026437602
233 (in isoform 1)Acetylation-26.73-
233AcetylationNPITGKRTVSRVSHP
CCCCCCCCHHCCCCC
26.7319608861
235 (in isoform 1)Phosphorylation-26.7625693802
236 (in isoform 1)Phosphorylation-29.6226437602
240 (in isoform 1)Phosphorylation-25.2725693802
244 (in isoform 1)Phosphorylation-19.7525693802
245 (in isoform 5)Phosphorylation-56.6126437602
248 (in isoform 1)Phosphorylation-44.3925693802
249AcetylationSKARKPPVCHGKRLP
HHCCCCCCCCCCCCC
5.2319608861
251 (in isoform 5)Phosphorylation-45.0725693802
252 (in isoform 5)Phosphorylation-16.2026437602
256 (in isoform 1)Phosphorylation-27.6026657352
256 (in isoform 5)Phosphorylation-27.6025693802
258 (in isoform 4)Phosphorylation-25.1426437602
260 (in isoform 5)Phosphorylation-3.6525693802
262AcetylationLPLTLFPSANLRGRH
CCEEECCCCCCCCCC
23.5819608861
264 (in isoform 5)Phosphorylation-34.3125693802
264 (in isoform 4)Phosphorylation-34.3125693802
265 (in isoform 4)Phosphorylation-6.5026437602
269 (in isoform 4)Phosphorylation-28.3425693802
272 (in isoform 1)Phosphorylation-26.18-
272 (in isoform 5)Phosphorylation-26.1826657352
273 (in isoform 4)Phosphorylation-51.2125693802
277 (in isoform 4)Phosphorylation-30.5225693802
285 (in isoform 4)Phosphorylation-26.1326657352
288 (in isoform 5)Phosphorylation-35.76-
301 (in isoform 4)Phosphorylation-9.08-
318PhosphorylationPGTTTASTAKNAP--
CCCCCCCCCCCCC--
38.9124719451

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
149YPhosphorylationKinaseSRCP12931
PSP
272YPhosphorylationKinaseSRCP12931
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FHL1_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 FHL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKA12_HUMANAKAP12physical
21900206
DREB_HUMANDBN1physical
21900206
MYOME_HUMANPDE4DIPphysical
21900206
DEAF1_HUMANDEAF1physical
21900206
HES1_HUMANHES1physical
21900206
EED_HUMANEEDphysical
21900206
TXNIP_HUMANTXNIPphysical
21900206
UBP15_HUMANUSP15physical
21219870
RING1_HUMANRING1physical
14999091
SUH_HUMANRBPJphysical
14999091
ZEP3_HUMANHIVEP3physical
14999091
NRIP1_HUMANNRIP1physical
19401155
ESR1_HUMANESR1physical
19401155
SMAD2_HUMANSMAD2physical
19139564
SMAD3_HUMANSMAD3physical
19139564
SMAD4_HUMANSMAD4physical
19139564
KC1D_HUMANCSNK1Dphysical
19139564
SRF_HUMANSRFphysical
15610731
EP300_HUMANEP300physical
22219185
CBP_HUMANCREBBPphysical
22219185
TITIN_HUMANTTNphysical
22778266
MYPC1_HUMANMYBPC1physical
16407297
ESR1_HUMANESR1physical
22094188
AKT1_HUMANAKT1physical
22094188

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FHL1_HUMAN

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Related Literatures of Post-Translational Modification

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