CHSTF_HUMAN - dbPTM
CHSTF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHSTF_HUMAN
UniProt AC Q7LFX5
Protein Name Carbohydrate sulfotransferase 15
Gene Name CHST15
Organism Homo sapiens (Human).
Sequence Length 561
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein . A small fraction may also be present at the cell surface, where it acts as a B-cell receptor.
Protein Description Sulfotransferase that transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4)) repeating units. It also transfers sulfate to a unique non-reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. May also act as a B-cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and/or regulation of B-cell-specific RAG expression; however such results are unclear in vivo..
Protein Sequence MRHCINCCIQLLPDGAHKQQVNCQGGPHHGHQACPTCKGENKILFRVDSKQMNLLAVLEVRTEGNENWGGFLRFKKGKRCSLVFGLIIMTLVMASYILSGAHQELLISSPFHYGGFPSNPSLMDSENPSDTKEHHHQSSVNNISYMKDYPSIKLIINSITTRIEFTTRQLPDLEDLKKQELHMFSVIPNKFLPNSKSPCWYEEFSGQNTTDPYLTNSYVLYSKRFRSTFDALRKAFWGHLAHAHGKHFRLRCLPHFYIIGQPKCGTTDLYDRLRLHPEVKFSAIKEPHWWTRKRFGIVRLRDGLRDRYPVEDYLDLFDLAAHQIHQGLQASSAKEQSKMNTIIIGEASASTMWDNNAWTFFYDNSTDGEPPFLTQDFIHAFQPNARLIVMLRDPVERLYSDYLYFASSNKSADDFHEKVTEALQLFENCMLDYSLRACVYNNTLNNAMPVRLQVGLYAVYLLDWLSVFDKQQFLILRLEDHASNVKYTMHKVFQFLNLGPLSEKQEALMTKSPASNARRPEDRNLGPMWPITQKILRDFYRPFNARLAQVLADEAFAWKTT
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
49PhosphorylationKILFRVDSKQMNLLA
EEEEEECCCCCEEEE
23.1729514088
118O-linked_GlycosylationFHYGGFPSNPSLMDS
CCCCCCCCCHHHCCC
60.14OGP
160PhosphorylationKLIINSITTRIEFTT
EEHHHHHHHCCEEEC
15.16-
161PhosphorylationLIINSITTRIEFTTR
EHHHHHHHCCEEECC
28.16-
201PhosphorylationNSKSPCWYEEFSGQN
CCCCCCCCCCCCCCC
16.58-
213PhosphorylationGQNTTDPYLTNSYVL
CCCCCCCCCCCEEEE
29.03-
217PhosphorylationTDPYLTNSYVLYSKR
CCCCCCCEEEEEEHH
16.0417081983
218PhosphorylationDPYLTNSYVLYSKRF
CCCCCCEEEEEEHHH
9.1322817900
221PhosphorylationLTNSYVLYSKRFRST
CCCEEEEEEHHHHHH
11.3417081983
222PhosphorylationTNSYVLYSKRFRSTF
CCEEEEEEHHHHHHH
17.1317081983
364N-linked_GlycosylationAWTFFYDNSTDGEPP
CEEEEECCCCCCCCC
35.12UniProtKB CARBOHYD
434PhosphorylationENCMLDYSLRACVYN
HHHHHCHHHHHHHHC
15.8524719451
443PhosphorylationRACVYNNTLNNAMPV
HHHHHCCCCCCCCCC
27.5024719451
504UbiquitinationNLGPLSEKQEALMTK
CCCCCCHHHHHHHCC
50.4921906983
504 (in isoform 1)Ubiquitination-50.4921906983
510PhosphorylationEKQEALMTKSPASNA
HHHHHHHCCCCCCCC
29.2622210691
511UbiquitinationKQEALMTKSPASNAR
HHHHHHCCCCCCCCC
40.242190698
511 (in isoform 1)Ubiquitination-40.2421906983

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 CHSTF_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHSTF_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 CHSTF_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HCK_HUMANHCKphysical
10749872
CALX_HUMANCANXphysical
26496610
CCNB1_HUMANCCNB1physical
26496610
IF5A1_HUMANEIF5Aphysical
26496610
ZEP1_HUMANHIVEP1physical
26496610
LGAT1_HUMANLPGAT1physical
26496610
CEPT1_HUMANCEPT1physical
26496610
SYFM_HUMANFARS2physical
26496610
CASC3_HUMANCASC3physical
26496610
RB6I2_HUMANERC1physical
26496610
KLDC2_HUMANKLHDC2physical
26496610
S43A3_HUMANSLC43A3physical
26496610
RABL6_HUMANRABL6physical
26496610
PKHG1_HUMANPLEKHG1physical
26496610
TPC_HUMANSLC25A19physical
26496610
S35E1_HUMANSLC35E1physical
26496610
ILKAP_HUMANILKAPphysical
26496610
PHF5A_HUMANPHF5Aphysical
26496610
NDUF2_HUMANNDUFAF2physical
26496610
TJAP1_HUMANTJAP1physical
26496610
CALX_HUMANCANXphysical
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 CHSTF_HUMAN

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Related Literatures of Post-Translational Modification

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