HMBX1_HUMAN - dbPTM
HMBX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HMBX1_HUMAN
UniProt AC Q6NT76
Protein Name Homeobox-containing protein 1
Gene Name HMBOX1
Organism Homo sapiens (Human).
Sequence Length 420
Subcellular Localization Nucleus . Cytoplasm . Predominantly detected in cytoplasm.
Isoform 5: Nucleus . Cytoplasm .
Protein Description Transcription factor. Isoform 1 acts as a transcriptional repressor. Isoform 4 has very low activity as a transcriptional repressor..
Protein Sequence MLSSFPVVLLETMSHYTDEPRFTIEQIDLLQRLRRTGMTKHEILHALETLDRLDQEHSDKFGRRSSYGGSSYGNSTNNVPASSSTATASTQTQHSGMSPSPSNSYDTSPQPCTTNQNGRENNERLSTSNGKMSPTRYHANSMGQRSYSFEASEEDLDVDDKVEELMRRDSSVIKEEIKAFLANRRISQAVVAQVTGISQSRISHWLLQQGSDLSEQKKRAFYRWYQLEKTNPGATLSMRPAPIPIEDPEWRQTPPPVSATSGTFRLRRGSRFTWRKECLAVMESYFNENQYPDEAKREEIANACNAVIQKPGKKLSDLERVTSLKVYNWFANRRKEIKRRANIEAAILESHGIDVQSPGGHSNSDDVDGNDYSEQDDSTSHSDHQDPISLAVEMAAVNHTILALARQGANEIKTEALDDD
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
3Phosphorylation-----MLSSFPVVLL
-----CCCCCCEEEE
28.7426074081
4Phosphorylation----MLSSFPVVLLE
----CCCCCCEEEEE
29.6126074081
12PhosphorylationFPVVLLETMSHYTDE
CCEEEEECCCCCCCC
24.7626074081
14PhosphorylationVVLLETMSHYTDEPR
EEEEECCCCCCCCCC
22.2926074081
16PhosphorylationLLETMSHYTDEPRFT
EEECCCCCCCCCCCC
14.4726074081
17PhosphorylationLETMSHYTDEPRFTI
EECCCCCCCCCCCCH
28.5826074081
23PhosphorylationYTDEPRFTIEQIDLL
CCCCCCCCHHHHHHH
25.5326074081
60SumoylationLDQEHSDKFGRRSSY
HCHHHHHHCCCCCCC
53.3728112733
126PhosphorylationRENNERLSTSNGKMS
CCCCCCCCCCCCCCC
35.6921712546
127PhosphorylationENNERLSTSNGKMSP
CCCCCCCCCCCCCCC
30.7023898821
128PhosphorylationNNERLSTSNGKMSPT
CCCCCCCCCCCCCCC
39.9621712546
131SumoylationRLSTSNGKMSPTRYH
CCCCCCCCCCCCHHC
40.2228112733
133PhosphorylationSTSNGKMSPTRYHAN
CCCCCCCCCCHHCCC
26.9723927012
135PhosphorylationSNGKMSPTRYHANSM
CCCCCCCCHHCCCCC
36.2323403867
137PhosphorylationGKMSPTRYHANSMGQ
CCCCCCHHCCCCCCC
14.0427251275
141PhosphorylationPTRYHANSMGQRSYS
CCHHCCCCCCCCCCC
25.6928348404
146PhosphorylationANSMGQRSYSFEASE
CCCCCCCCCCEECCH
19.7630266825
147PhosphorylationNSMGQRSYSFEASEE
CCCCCCCCCEECCHH
21.4028387310
148PhosphorylationSMGQRSYSFEASEED
CCCCCCCCEECCHHH
20.1830266825
152PhosphorylationRSYSFEASEEDLDVD
CCCCEECCHHHCCHH
34.0330266825
161SumoylationEDLDVDDKVEELMRR
HHCCHHHHHHHHHHC
47.2728112733
170PhosphorylationEELMRRDSSVIKEEI
HHHHHCCCHHHHHHH
25.3726055452
171PhosphorylationELMRRDSSVIKEEIK
HHHHCCCHHHHHHHH
31.9528102081
174SumoylationRRDSSVIKEEIKAFL
HCCCHHHHHHHHHHH
47.3328112733
187PhosphorylationFLANRRISQAVVAQV
HHHCCCHHHHHHHHH
15.4123312004
214PhosphorylationLQQGSDLSEQKKRAF
HHCCCCCCHHHHHHH
42.8628555341
217SumoylationGSDLSEQKKRAFYRW
CCCCCHHHHHHHHHH
39.9328112733
217AcetylationGSDLSEQKKRAFYRW
CCCCCHHHHHHHHHH
39.9325953088
235PhosphorylationEKTNPGATLSMRPAP
CCCCCCCCEECEECC
25.8627251275
237PhosphorylationTNPGATLSMRPAPIP
CCCCCCEECEECCCC
14.3727251275
253PhosphorylationEDPEWRQTPPPVSAT
CCCHHHCCCCCCCCC
29.2325850435
258PhosphorylationRQTPPPVSATSGTFR
HCCCCCCCCCCCEEE
31.4425850435
260PhosphorylationTPPPVSATSGTFRLR
CCCCCCCCCCEEEEC
21.8625850435
261PhosphorylationPPPVSATSGTFRLRR
CCCCCCCCCEEEECC
35.2425850435
263PhosphorylationPVSATSGTFRLRRGS
CCCCCCCEEEECCCC
12.8325850435
310SumoylationACNAVIQKPGKKLSD
HHHHHHCCCCCCHHH
44.6128112733
310UbiquitinationACNAVIQKPGKKLSD
HHHHHHCCCCCCHHH
44.61-
314UbiquitinationVIQKPGKKLSDLERV
HHCCCCCCHHHHHHH
60.17-
316PhosphorylationQKPGKKLSDLERVTS
CCCCCCHHHHHHHHH
49.37-
322PhosphorylationLSDLERVTSLKVYNW
HHHHHHHHHHHHHHH
34.2623312004
323PhosphorylationSDLERVTSLKVYNWF
HHHHHHHHHHHHHHH
24.2823312004
325UbiquitinationLERVTSLKVYNWFAN
HHHHHHHHHHHHHHH
42.30-
356 (in isoform 2)Phosphorylation-39.9125921289
356 (in isoform 5)Phosphorylation-39.9125921289
361 (in isoform 2)Phosphorylation-29.7125921289
361 (in isoform 5)Phosphorylation-29.7125921289
363 (in isoform 2)Phosphorylation-43.7325921289
363 (in isoform 5)Phosphorylation-43.7325921289
389 (in isoform 2)Phosphorylation-18.7025159151
390 (in isoform 2)Phosphorylation-6.8325159151
413SumoylationRQGANEIKTEALDDD
HCCHHHHHHHCCCCC
33.8525114211
413SumoylationRQGANEIKTEALDDD
HCCHHHHHHHCCCCC
33.85-

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 HMBX1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HMBX1_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 HMBX1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
HMBX1_HUMANHMBOX1physical
25416956
SP30L_HUMANSAP30Lphysical
25416956
F161A_HUMANFAM161Aphysical
25416956
LNX1_HUMANLNX1physical
25416956
ZN587_HUMANZNF587physical
25416956
REEP6_HUMANREEP6physical
25416956
SFR1_HUMANSFR1physical
25416956
AEBP2_HUMANAEBP2physical
25416956
FRMD6_HUMANFRMD6physical
25416956
ASB7_HUMANASB7physical
25416956
DYL2_HUMANDYNLL2physical
25416956
ZN417_HUMANZNF417physical
25416956
ZMAT2_HUMANZMAT2physical
25416956
TEANC_HUMANTCEANCphysical
25416956
FA13C_HUMANFAM13Cphysical
25416956
REQU_HUMANDPF2physical
26496610
DCC1_HUMANDSCC1physical
26496610
AMOL1_HUMANAMOTL1physical
27173435
CDAC1_HUMANCDADC1physical
27173435

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 HMBX1_HUMAN

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Related Literatures of Post-Translational Modification

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