TXND9_HUMAN - dbPTM
TXND9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TXND9_HUMAN
UniProt AC O14530
Protein Name Thioredoxin domain-containing protein 9
Gene Name TXNDC9
Organism Homo sapiens (Human).
Sequence Length 226
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Midbody . Co-localizes with beta-tubulin in the centrosome.
Protein Description Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin..
Protein Sequence MEADASVDMFSKVLEHQLLQTTKLVEEHLDSEIQKLDQMDEDELERLKEKRLQALRKAQQQKQEWLSKGHGEYREIPSERDFFQEVKESENVVCHFYRDSTFRCKILDRHLAILSKKHLETKFLKLNVEKAPFLCERLHIKVIPTLALLKDGKTQDYVVGFTDLGNTDDFTTETLEWRLGSSDILNYSGNLMEPPFQNQKKFGTNFTKLEKKTIRGKKYDSDSDDD
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
21PhosphorylationLEHQLLQTTKLVEEH
HHHHHHHHHHHHHHH		26.3528555341
22PhosphorylationEHQLLQTTKLVEEHL
HHHHHHHHHHHHHHH		14.9328555341
23UbiquitinationHQLLQTTKLVEEHLD
HHHHHHHHHHHHHHH		54.6532015554
35UbiquitinationHLDSEIQKLDQMDED
HHHHHHHHHHCCCHH		60.74-
48UbiquitinationEDELERLKEKRLQAL
HHHHHHHHHHHHHHH		68.3729967540
57UbiquitinationKRLQALRKAQQQKQE
HHHHHHHHHHHHHHH		51.9322817900
62UbiquitinationLRKAQQQKQEWLSKG
HHHHHHHHHHHHHCC		45.9421890473
62UbiquitinationLRKAQQQKQEWLSKG
HHHHHHHHHHHHHCC		45.9421906983
68UbiquitinationQKQEWLSKGHGEYRE
HHHHHHHCCCCCCCC		53.4029967540
78PhosphorylationGEYREIPSERDFFQE
CCCCCCCCCCCHHHH		51.4224719451
87UbiquitinationRDFFQEVKESENVVC
CCHHHHHHHHCCEEE		55.5621963094
116UbiquitinationRHLAILSKKHLETKF
HHHHHHCHHHHHHHC		40.5429967540
116AcetylationRHLAILSKKHLETKF
HHHHHHCHHHHHHHC		40.5426210075
117UbiquitinationHLAILSKKHLETKFL
HHHHHCHHHHHHHCC		50.47-
122AcetylationSKKHLETKFLKLNVE
CHHHHHHHCCCCCHH		39.0527452117
125UbiquitinationHLETKFLKLNVEKAP
HHHHHCCCCCHHHHH		40.9429967540
130UbiquitinationFLKLNVEKAPFLCER
CCCCCHHHHHHHHHH		58.0129967540
141UbiquitinationLCERLHIKVIPTLAL
HHHHHCCEEEEEEEE		24.3022817900
145PhosphorylationLHIKVIPTLALLKDG
HCCEEEEEEEECCCC		17.3421406692
150UbiquitinationIPTLALLKDGKTQDY
EEEEEECCCCCCCEE		66.3429967540
153UbiquitinationLALLKDGKTQDYVVG
EEECCCCCCCEEEEE		53.82-
181PhosphorylationTLEWRLGSSDILNYS
CEEECCCCCCCCCCC		29.4528102081
182PhosphorylationLEWRLGSSDILNYSG
EEECCCCCCCCCCCC		27.2028102081
187PhosphorylationGSSDILNYSGNLMEP
CCCCCCCCCCCCCCC		17.9521712546
188PhosphorylationSSDILNYSGNLMEPP
CCCCCCCCCCCCCCC		21.8225159151
201UbiquitinationPPFQNQKKFGTNFTK
CCCCCCCCCCCCCCH		38.9829967540
204PhosphorylationQNQKKFGTNFTKLEK
CCCCCCCCCCCHHCC		30.2328555341
208UbiquitinationKFGTNFTKLEKKTIR
CCCCCCCHHCCCCCC		50.9733845483
208AcetylationKFGTNFTKLEKKTIR
CCCCCCCHHCCCCCC		50.9725953088
219PhosphorylationKTIRGKKYDSDSDDD
CCCCCCCCCCCCCCC		24.9424275569
221PhosphorylationIRGKKYDSDSDDD--
CCCCCCCCCCCCC--		35.6026055452
223PhosphorylationGKKYDSDSDDD----
CCCCCCCCCCC----		47.0626055452
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 TXND9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TXND9_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 TXND9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GIT1_HUMANGIT1physical
16169070
FEZ1_HUMANFEZ1physical
16169070
ELP1_HUMANIKBKAPphysical
16169070
MIC60_HUMANIMMTphysical
16169070
PTN_HUMANPTNphysical
16169070
CHD3_HUMANCHD3physical
16169070
CE126_HUMANKIAA1377physical
16169070
SETB1_HUMANSETDB1physical
16169070
ZCHC8_HUMANZCCHC8physical
22939629
U3IP2_HUMANRRP9physical
22939629
WASF1_HUMANWASF1physical
22939629
VPS53_HUMANVPS53physical
22939629
VIP1_HUMANPPIP5K1physical
22939629
ZPR1_HUMANZPR1physical
22939629
UBR7_HUMANUBR7physical
22939629
ABRX2_HUMANFAM175Bphysical
22863883
HUWE1_HUMANHUWE1physical
22863883
WDHD1_HUMANWDHD1physical
22863883
EXOS8_HUMANEXOSC8physical
25416956
CEP76_HUMANCEP76physical
25416956
CA094_HUMANC1orf94physical
25416956
DYDC1_HUMANDYDC1physical
25416956
CC172_HUMANCCDC172physical
25416956
CC062_HUMANC3orf62physical
25416956
TCPH_HUMANCCT7physical
26186194
TCPG_HUMANCCT3physical
26186194
TCPW_HUMANCCT6Bphysical
26186194
TCPD_HUMANCCT4physical
26186194
TBAL3_HUMANTUBAL3physical
26186194
TBB2A_HUMANTUBB2Aphysical
26186194
ARFP1_HUMANARFIP1physical
26344197
BAG1_HUMANBAG1physical
26344197
TCPW_HUMANCCT6Bphysical
26344197
CPSF6_HUMANCPSF6physical
26344197
CPSF5_HUMANNUDT21physical
26344197
PCF11_HUMANPCF11physical
26344197
1433T_HUMANYWHAQphysical
26344197
MAGA6_HUMANMAGEA6physical
21516116
SMYD2_HUMANSMYD2physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
TCPG_HUMANCCT3physical
28514442
TCPH_HUMANCCT7physical
28514442
TBA1C_HUMANTUBA1Cphysical
28514442
TBA1A_HUMANTUBA1Aphysical
28514442
TBAL3_HUMANTUBAL3physical
28514442
TCPB_HUMANCCT2physical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
GBB2_HUMANGNB2physical
28514442
TCPA_HUMANTCP1physical
28514442
TCPE_HUMANCCT5physical
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 TXND9_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASSSPECTROMETRY.

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