| Tag | Content |
|---|
| CPLM ID | CPLM-015335 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Thioredoxin domain-containing protein 11 |
Protein Synonyms/Alias | EF-hand-binding protein 1 |
Gene Name | TXNDC11 |
Gene Synonyms/Alias | EFP1 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 566 | VAFSSLEKKCEVDAP | ubiquitination | [1] |
|
Reference | [1] Systematic and quantitative assessment of the ubiquitin-modified proteome. Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP. Mol Cell. 2011 Oct 21;44(2):325-40. [ PMID: 21906983] |
Functional Description | May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H(2)O(2) generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H(2)O(2) generation. |
Sequence Annotation | DOMAIN 92 214 Thioredoxin 1.
DOMAIN 649 799 Thioredoxin 2.
MOD_RES 828 828 Phosphoserine.
DISULFID 469 472 Redox-active (By similarity).
DISULFID 719 722 Redox-active (By similarity). |
Keyword | Alternative splicing; Coiled coil; Complete proteome; Disulfide bond; Endoplasmic reticulum; Membrane; Phosphoprotein; Polymorphism; Redox-active center; Reference proteome; Repeat; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 985 AA |
Protein Sequence | MSECGGRGGG SSSSEDAEDE GGGGGGPAGS DCLSSSPTLA TASSAGRLRR GLRGAFLMAR 60
QRPELLCGAV ALGCALLLAL KFTCSRAKDV IIPAKPPVSF FSLRSPVLDL FQGQLDYAEY 120
VRRDSEVVLL FFYAPWCGQS IAARAEIEQA ASRLSDQVLF VAINCWWNQG KCRKQKHFFY 180
FPVIYLYHRS FGPIEYKGPM SAVYIEKFVR RVMKPLLYIP SQSELLDFLS NYEPGVLGYF 240
EFSGSPQPPG YLTFFTSALH SLKKALESTS SPRALVSFTG EWHLETKIYV LDYLGTVRFG 300
VITNKHLAKL VSLVHSGSVY LHRHFNTSLV FPREVLNYTA ENICKWALEN QETLFRWLRP 360
HGGKSLLLNN ELKKGPALFL FIPFNPLAES HPLIDEITEV ALEYNNCHGD QVVERLLQHL 420
RRVDAPVLES LALEVPAQLP DPPTITASPC CNTVVLPQWH SFSRTHNVCE LCVNQTSGGM 480
KPSSVSVPQC SFFEMAAALD SFYLKEQTFY HVASDSIECS NFLTSYSPFS YYTACCRTIS 540
RGVSGFIDSE QGVFEAPTVA FSSLEKKCEV DAPSSVPHIE ENRYLFPEVD MTSTNFTGLS 600
CRTNKTLNIY LLDSNLFWLY AERLGAPSST QVKEFAAIVD VKEESHYILD PKQALMKLTL 660
ESFIQNFSVL YSPLKRHLIG SGSAQFPSQH LITEVTTDTF WEVVLQKQDV LLLYYAPWCG 720
FCPSLNHIFI QLARNLPMDT FTVARIDVSQ NDLPWEFMVD RLPTVLFFPC NRKDLSVKYP 780
EDVPITLPNL LRFILHHSDP ASSPQNVANS PTKECLQSEA VLQRGHISHL EREIQKLRAE 840
ISSLQRAQVQ VESQLSSARR DEHRLRQQQR ALEEQHSLLH AHSEQLQALY EQKTRELQEL 900
ARKLQELADA SENLLTENTW LKILVATMER KLEGRDGAES LAAQREVHPK QPEPSATPQL 960
PGSSPPPANV SATLVSERNK ENRTD 985 |
Gene Ontology | GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0045454; P:cell redox homeostasis; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |