HEM1_HUMAN - dbPTM
HEM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HEM1_HUMAN
UniProt AC P13196
Protein Name 5-aminolevulinate synthase, nonspecific, mitochondrial
Gene Name ALAS1
Organism Homo sapiens (Human).
Sequence Length 640
Subcellular Localization Mitochondrion matrix.
Protein Description
Protein Sequence MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKETPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGSSVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPERVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLITKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLELKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA
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
29PhosphorylationAGKSLLFYAQNCPKM
HHHHHHHCCCCCHHH
13.7729496907
42UbiquitinationKMMEVGAKPAPRALS
HHHHCCCCCCCCHHH
35.47-
55PhosphorylationLSTAAVHYQQIKETP
HHHHHHHHHHHHCCC
8.7727642862
74UbiquitinationKDKTAKAKVQQTPDG
CCCCCHHHEEECCCC
39.61-
78PhosphorylationAKAKVQQTPDGSQQS
CHHHEEECCCCCCCC
13.2728450419
82PhosphorylationVQQTPDGSQQSPDGT
EEECCCCCCCCCCCC
32.2128450419
85PhosphorylationTPDGSQQSPDGTQLP
CCCCCCCCCCCCCCC
19.8128450419
89PhosphorylationSQQSPDGTQLPSGHP
CCCCCCCCCCCCCCC
34.0228450419
93PhosphorylationPDGTQLPSGHPLPAT
CCCCCCCCCCCCCCC
59.3228450419
107UbiquitinationTSQGTASKCPFLAAQ
CCCCHHHCCHHHHHH
43.38-
142UbiquitinationQEMNAVRKEVAETSA
HHHHHHHHHHHHCCC
50.36-
147PhosphorylationVRKEVAETSAGPSVV
HHHHHHHCCCCCEEE
17.7123312004
148PhosphorylationRKEVAETSAGPSVVS
HHHHHHCCCCCEEEE
23.8023312004
152PhosphorylationAETSAGPSVVSVKTD
HHCCCCCEEEEEEEC
33.9423312004
155PhosphorylationSAGPSVVSVKTDGGD
CCCCEEEEEEECCCC
18.7523312004
157UbiquitinationGPSVVSVKTDGGDPS
CCEEEEEEECCCCCC
33.1321906983
158PhosphorylationPSVVSVKTDGGDPSG
CEEEEEEECCCCCCH
37.4123312004
164PhosphorylationKTDGGDPSGLLKNFQ
EECCCCCCHHHHHHH
46.9823312004
168UbiquitinationGDPSGLLKNFQDIMQ
CCCCHHHHHHHHHHH
61.8421906983
174 (in isoform 1)Ubiquitination-5.6821906983
176AcetylationNFQDIMQKQRPERVS
HHHHHHHHHCHHHHH
30.787482707
176UbiquitinationNFQDIMQKQRPERVS
HHHHHHHHHCHHHHH
30.78-
185 (in isoform 1)Ubiquitination-3.4221906983
192UbiquitinationLLQDNLPKSVSTFQY
HHHHCCCCCCCHHHH
67.66-
210AcetylationFEKKIDEKKNDHTYR
HHHHCCCCCCCHHHE
53.8023749302
216PhosphorylationEKKNDHTYRVFKTVN
CCCCCHHHEEEHHHC
11.0222817900
220UbiquitinationDHTYRVFKTVNRRAH
CHHHEEEHHHCCCCC
49.02-
242UbiquitinationYSDSLITKKQVSVWC
CCCCCCCHHHEEEEE
33.932190698
243UbiquitinationSDSLITKKQVSVWCS
CCCCCCHHHEEEEEC
47.48-
259 (in isoform 1)Ubiquitination-13.7621906983
269PhosphorylationVCGAVMDTLKQHGAG
HHHHHHHHHHHCCCC
20.1218767875
271UbiquitinationGAVMDTLKQHGAGAG
HHHHHHHHHCCCCCC
42.20-
280PhosphorylationHGAGAGGTRNISGTS
CCCCCCCCCCCCCCC
21.4512300637
284PhosphorylationAGGTRNISGTSKFHV
CCCCCCCCCCCEEEE
39.3012300647
287PhosphorylationTRNISGTSKFHVDLE
CCCCCCCCEEEEEHH
36.5312300657
288UbiquitinationRNISGTSKFHVDLER
CCCCCCCEEEEEHHH
39.05-
353UbiquitinationIRNSRVPKYIFRHND
HHCCCCCCCHHCCCC
48.39-
371PhosphorylationLRELLQRSDPSVPKI
HHHHHHCCCCCCCEE
40.69113305975
435UbiquitinationDRDGVMPKMDIISGT
CCCCCCCCHHEECCH
30.98-
445OtherIISGTLGKAFGCVGG
EECCHHHHHHCCHHH
43.59-
445N6-(pyridoxal phosphate)lysineIISGTLGKAFGCVGG
EECCHHHHHHCCHHH
43.59-
488PhosphorylationLLAGALESVRILKSA
HHHHHHHHHHHHHHC
19.97108417771
539UbiquitinationVRVADAAKNTEVCDE
CHHHHHHCCHHHHHH
67.15-
548SulfoxidationTEVCDELMSRHNIYV
HHHHHHHHHHCCEEE
2.8821406390
602UbiquitinationKQVGLELKPHSSAEC
HHHCCEECCCCCCCC
31.17-
626UbiquitinationEVMSEREKSYFSGLS
HHCCHHHHHHHHHHH
57.59-
628PhosphorylationMSEREKSYFSGLSKL
CCHHHHHHHHHHHHH
16.906885281
630PhosphorylationEREKSYFSGLSKLVS
HHHHHHHHHHHHHHH
30.5025690035
634UbiquitinationSYFSGLSKLVSAQA-
HHHHHHHHHHHCCC-
58.93-

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 HEM1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HEM1_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 HEM1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VHL_HUMANVHLphysical
16234850
UROK_HUMANPLAUphysical
21988832
HEM1_HUMANALAS1physical
25416956
BCL7A_HUMANBCL7Aphysical
25416956
PEPL_HUMANPPLphysical
25416956
TCEA2_HUMANTCEA2physical
25416956
TYB4_HUMANTMSB4Xphysical
25416956
WIPF1_HUMANWIPF1physical
25416956
ZN175_HUMANZNF175physical
25416956
TYB10_HUMANTMSB10physical
25416956
UBP20_HUMANUSP20physical
25416956
ZFY26_HUMANZFYVE26physical
25416956
PDIP2_HUMANPOLDIP2physical
25416956
CCHCR_HUMANCCHCR1physical
25416956
GNL3L_HUMANGNL3Lphysical
25416956
CB042_HUMANC2orf42physical
25416956
EP400_HUMANEP400physical
25416956
SH24A_HUMANSH2D4Aphysical
25416956
CERK1_HUMANCERKphysical
25416956
TTC23_HUMANTTC23physical
25416956
CDC73_HUMANCDC73physical
25416956
ZMAT1_HUMANZMAT1physical
25416956
LONF1_HUMANLONRF1physical
25416956
MTFR2_HUMANMTFR2physical
25416956
SNX20_HUMANSNX20physical
25416956
DUS19_HUMANDUSP19physical
25416956
TEKT4_HUMANTEKT4physical
25416956
ZN564_HUMANZNF564physical
25416956
KLH35_HUMANKLHL35physical
25416956
RTL8B_HUMANFAM127Cphysical
25416956
PDIP2_HUMANPOLDIP2physical
21516116
EP400_HUMANEP400physical
21516116
TYB10_HUMANTMSB10physical
21516116

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
DB00145Glycine
Regulatory Network of HEM1_HUMAN

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Related Literatures of Post-Translational Modification

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