H1T_HUMAN - dbPTM
H1T_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H1T_HUMAN
UniProt AC P22492
Protein Name Histone H1t
Gene Name HIST1H1T
Organism Homo sapiens (Human).
Sequence Length 207
Subcellular Localization Nucleus . Chromosome .
Protein Description Testis-specific histone H1 that forms less compacted chromatin compared to other H1 histone subtypes. [PubMed: 26757249 Formation of more relaxed chromatin may be required to promote chromatin architecture required for proper chromosome regulation during meiosis, such as homologous recombination]
Protein Sequence MSETVPAASASAGVAAMEKLPTKKRGRKPAGLISASRKVPNLSVSKLITEALSVSQERVGMSLVALKKALAAAGYDVEKNNSRIKLSLKSLVNKGILVQTRGTGASGSFKLSKKVIPKSTRSKAKKSVSAKTKKLVLSRDSKSPKTAKTNKRAKKPRATTPKTVRSGRKAKGAKGKQQQKSPVKARASKSKLTQHHEVNVRKATSKK
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
2Phosphorylation------MSETVPAAS
------CCCCCCHHH
41.8125693802
4Phosphorylation----MSETVPAASAS
----CCCCCCHHHHH
25.2025693802
9PhosphorylationSETVPAASASAGVAA
CCCCCHHHHHHCHHH
25.5130387612
11PhosphorylationTVPAASASAGVAAME
CCCHHHHHHCHHHHH
24.0625693802
22PhosphorylationAAMEKLPTKKRGRKP
HHHHHCCCCCCCCCC
60.6822964224
43PhosphorylationSRKVPNLSVSKLITE
CCCCCCCCHHHHHHH
30.8724719451
45PhosphorylationKVPNLSVSKLITEAL
CCCCCCHHHHHHHHH
20.5427282143
53PhosphorylationKLITEALSVSQERVG
HHHHHHHHCCHHHHH
27.1126699800
55PhosphorylationITEALSVSQERVGMS
HHHHHHCCHHHHHHH
23.9726699800
58CitrullinationALSVSQERVGMSLVA
HHHCCHHHHHHHHHH
23.74-
58CitrullinationALSVSQERVGMSLVA
HHHCCHHHHHHHHHH
23.74-
62PhosphorylationSQERVGMSLVALKKA
CHHHHHHHHHHHHHH
17.4826074081
67UbiquitinationGMSLVALKKALAAAG
HHHHHHHHHHHHHCC
26.6822817900
68SumoylationMSLVALKKALAAAGY
HHHHHHHHHHHHCCC
49.86-
68SumoylationMSLVALKKALAAAGY
HHHHHHHHHHHHCCC
49.86-
68UbiquitinationMSLVALKKALAAAGY
HHHHHHHHHHHHCCC
49.8622053931
75PhosphorylationKALAAAGYDVEKNNS
HHHHHCCCCCHHCCC
16.4628152594
79AcetylationAAGYDVEKNNSRIKL
HCCCCCHHCCCEEEE
62.37158563
79UbiquitinationAAGYDVEKNNSRIKL
HCCCCCHHCCCEEEE
62.3723000965
82PhosphorylationYDVEKNNSRIKLSLK
CCCHHCCCEEEEEHH
44.7923401153
82UbiquitinationYDVEKNNSRIKLSLK
CCCHHCCCEEEEEHH
44.7921890473
85UbiquitinationEKNNSRIKLSLKSLV
HHCCCEEEEEHHHHH
30.8023000965
87PhosphorylationNNSRIKLSLKSLVNK
CCCEEEEEHHHHHHC
28.8422210691
93UbiquitinationLSLKSLVNKGILVQT
EEHHHHHHCCEEEEE
41.9721890473
103PhosphorylationILVQTRGTGASGSFK
EEEEECCCCCCCCCC
26.7026657352
106PhosphorylationQTRGTGASGSFKLSK
EECCCCCCCCCCCCC
35.9925849741
108PhosphorylationRGTGASGSFKLSKKV
CCCCCCCCCCCCCCC
19.4030266825
110AcetylationTGASGSFKLSKKVIP
CCCCCCCCCCCCCCC
54.257428721
113AcetylationSGSFKLSKKVIPKST
CCCCCCCCCCCCCCC
62.597428731
138PhosphorylationKTKKLVLSRDSKSPK
HHHHHHCCCCCCCCC
26.9424719451
141PhosphorylationKLVLSRDSKSPKTAK
HHHCCCCCCCCCHHH
33.6425159151
143PhosphorylationVLSRDSKSPKTAKTN
HCCCCCCCCCHHHCC
35.26-
148UbiquitinationSKSPKTAKTNKRAKK
CCCCCHHHCCCCCCC
58.8424816145
149PhosphorylationKSPKTAKTNKRAKKP
CCCCHHHCCCCCCCC
43.43-
159PhosphorylationRAKKPRATTPKTVRS
CCCCCCCCCCCCHHC
44.9320068231
160PhosphorylationAKKPRATTPKTVRSG
CCCCCCCCCCCHHCC
23.0820068231
162AcetylationKPRATTPKTVRSGRK
CCCCCCCCCHHCCCC
58.5230585545
166PhosphorylationTTPKTVRSGRKAKGA
CCCCCHHCCCCCCCC
38.32-
171AcetylationVRSGRKAKGAKGKQQ
HHCCCCCCCCCCCCC
63.5412634851
181PhosphorylationKGKQQQKSPVKARAS
CCCCCCCCCHHHHHC
30.50-
190PhosphorylationVKARASKSKLTQHHE
HHHHHCCCHHHHHHH
30.33-
191AcetylationKARASKSKLTQHHEV
HHHHCCCHHHHHHHH
60.3325953088

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 H1T_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
58RCitrullination

-

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 H1T_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZCCHV_HUMANZC3HAV1physical
28514442
H14_HUMANHIST1H1Ephysical
28514442
YBOX2_HUMANYBX2physical
28514442
RL30_HUMANRPL30physical
28514442
ELAV2_HUMANELAVL2physical
28514442
RL36L_HUMANRPL36ALphysical
28514442
SRS12_HUMANSRSF12physical
28514442
DHX57_HUMANDHX57physical
28514442
BUD13_HUMANBUD13physical
28514442
ZNF92_HUMANZNF92physical
28514442
DHX8_HUMANDHX8physical
28514442
ZC3H8_HUMANZC3H8physical
28514442
RBM19_HUMANRBM19physical
28514442
CMS1_HUMANCMSS1physical
28514442
ZCRB1_HUMANZCRB1physical
28514442
PURB_HUMANPURBphysical
28514442
NO40_HUMANZCCHC17physical
28514442
TPM2_HUMANTPM2physical
28514442
KRR1_HUMANKRR1physical
28514442
GPT11_HUMANGPATCH11physical
28514442
RL26L_HUMANRPL26L1physical
28514442
SREK1_HUMANSREK1physical
28514442
SFR19_HUMANSCAF1physical
28514442
DKC1_HUMANDKC1physical
28514442
NAT10_HUMANNAT10physical
28514442
DDX52_HUMANDDX52physical
28514442
UTP23_HUMANUTP23physical
28514442
RSBN1_HUMANRSBN1physical
28514442
NGDN_HUMANNGDNphysical
28514442
RRP12_HUMANRRP12physical
28514442
PUM3_HUMANKIAA0020physical
28514442
RENT1_HUMANUPF1physical
28514442
DDX54_HUMANDDX54physical
28514442
ZCHC7_HUMANZCCHC7physical
28514442
NOG2_HUMANGNL2physical
28514442
CC137_HUMANCCDC137physical
28514442
SR140_HUMANU2SURPphysical
28514442
TOE1_HUMANTOE1physical
28514442
DDX27_HUMANDDX27physical
28514442
SRRM1_HUMANSRRM1physical
28514442
PRP4B_HUMANPRPF4Bphysical
28514442
TTF1_HUMANTTF1physical
28514442
RS15_HUMANRPS15physical
28514442
ZN771_HUMANZNF771physical
28514442
KRI1_HUMANKRI1physical
28514442
ZCHC9_HUMANZCCHC9physical
28514442
MPP10_HUMANMPHOSPH10physical
28514442
MOV10_HUMANMOV10physical
28514442
SYFM_HUMANFARS2physical
28514442
NOG1_HUMANGTPBP4physical
28514442
BRX1_HUMANBRIX1physical
28514442
CHERP_HUMANCHERPphysical
28514442
ZN668_HUMANZNF668physical
28514442
DDX21_HUMANDDX21physical
28514442
H2A2B_HUMANHIST2H2ABphysical
28514442
DDX10_HUMANDDX10physical
28514442
RRP8_HUMANRRP8physical
28514442
RRS1_HUMANRRS1physical
28514442
NOL12_HUMANNOL12physical
28514442
RS3A_HUMANRPS3Aphysical
28514442
RS5_HUMANRPS5physical
28514442
PRD10_HUMANPRDM10physical
28514442
RPF2_HUMANRPF2physical
28514442
NOC4L_HUMANNOC4Lphysical
28514442
DDX56_HUMANDDX56physical
28514442
CI114_HUMANC9orf114physical
28514442
RS3_HUMANRPS3physical
28514442
NKAP_HUMANNKAPphysical
28514442
YTDC1_HUMANYTHDC1physical
28514442
RL10A_HUMANRPL10Aphysical
28514442
RS10_HUMANRPS10physical
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 H1T_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 THR-159 AND THR-160, ANDMASS SPECTROMETRY.

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