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Protein

TRAF-type zinc finger domain-containing protein 1

Gene

TRAFD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Negative feedback regulator that controls excessive innate immune responses. Regulates both Toll-like receptor 4 (TLR4) and DDX58/RIG1-like helicases (RLH) pathways. May inhibit the LTR pathway by direct interaction with TRAF6 and attenuation of NF-kappa-B activation. May negatively regulate the RLH pathway downstream from MAVS and upstream of NF-kappa-B and IRF3 (By similarity).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri27 – 10377TRAF-typeAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
TRAF-type zinc finger domain-containing protein 1
Alternative name(s):
Protein FLN29
Gene namesi
Name:TRAFD1
Synonyms:FLN29
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:24808. TRAFD1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670704.

Polymorphism and mutation databases

BioMutaiTRAFD1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 582581TRAF-type zinc finger domain-containing protein 1PRO_0000278457Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei320 – 3201PhosphoserineCombined sources
Modified residuei326 – 3261PhosphoserineCombined sources
Modified residuei327 – 3271PhosphoserineCombined sources
Modified residuei409 – 4091PhosphoserineCombined sources
Modified residuei415 – 4151PhosphoserineCombined sources
Modified residuei470 – 4701PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO14545.
MaxQBiO14545.
PaxDbiO14545.
PeptideAtlasiO14545.
PRIDEiO14545.

PTM databases

iPTMnetiO14545.
PhosphoSiteiO14545.

Expressioni

Gene expression databases

BgeeiO14545.
CleanExiHS_TRAFD1.
ExpressionAtlasiO14545. baseline and differential.
GenevisibleiO14545. HS.

Organism-specific databases

HPAiHPA039254.
HPA039266.

Interactioni

Subunit structurei

Interacts with MAVS, TICAM1, TRAF1, TRAF2, TRAF3 (By similarity). Interacts with TRAF6.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HTTP428585EBI-1396921,EBI-466029
NGLY1Q96IV03EBI-1396921,EBI-6165879

Protein-protein interaction databases

BioGridi116112. 20 interactions.
IntActiO14545. 15 interactions.
STRINGi9606.ENSP00000257604.

Structurei

Secondary structure

1
582
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi91 – 933Combined sources
Helixi99 – 11113Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi117 – 1193Combined sources
Beta strandi122 – 1243Combined sources
Helixi127 – 1293Combined sources
Helixi131 – 1344Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9KNMR-A78-139[»]
ProteinModelPortaliO14545.
SMRiO14545. Positions 30-65, 78-139.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14545.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi577 – 5826Poly-Glu

Sequence similaritiesi

Contains 1 TRAF-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri27 – 10377TRAF-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IGBJ. Eukaryota.
ENOG4111IF3. LUCA.
GeneTreeiENSGT00530000063869.
HOGENOMiHOG000154674.
HOVERGENiHBG094084.
InParanoidiO14545.
OMAiAEQDFWR.
OrthoDBiEOG76473W.
PhylomeDBiO14545.
TreeFamiTF331416.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O14545-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEFLDDQET RLCDNCKKEI PVFNFTIHEI HCQRNIGMCP TCKEPFPKSD
60 70 80 90 100
METHMAAEHC QVTCKCNKKL EKRLLKKHEE TECPLRLAVC QHCDLELSIL
110 120 130 140 150
KLKEHEDYCG ARTELCGNCG RNVLVKDLKT HPEVCGREGE EKRNEVAIPP
160 170 180 190 200
NAYDESWGQD GIWIASQLLR QIEALDPPMR LPRRPLRAFE SDVFHNRTTN
210 220 230 240 250
QRNITAQVSI QNNLFEEQER QERNRGQQPP KEGGEESANL DFMLALSLQN
260 270 280 290 300
EGQASSVAEQ DFWRAVCEAD QSHGGPRSLS DIKGAADEIM LPCEFCEELY
310 320 330 340 350
PEELLIDHQT SCNPSRALPS LNTGSSSPRG VEEPDVIFQN FLQQAASNQL
360 370 380 390 400
DSLMGLSNSH PVEESIIIPC EFCGVQLEEE VLFHHQDQCD QRPATATNHV
410 420 430 440 450
TEGIPRLDSQ PQETSPELPR RRVRHQGDLS SGYLDDTKQE TANGPTSCLP
460 470 480 490 500
PSRPINNMTA TYNQLSRSTS GPRPGCQPSS PCVPKLSNSD SQDIQGRNRD
510 520 530 540 550
SQNGAIAPGH VSVIRPPQNL YPENIVPSFS PGPSGRYGAS GRSEGGRNSR
560 570 580
VTPAAANYRS RTAKAKPSKQ QGAGDAEEEE EE
Length:582
Mass (Da):64,841
Last modified:January 1, 1998 - v1
Checksum:i4937682988851AC0
GO
Isoform 2 (identifier: O14545-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     134-164: VCGREGEEKRNEVAIPPNAYDESWGQDGIWI → LKNKRGRKGIEANSPPKRVVKRVQTWTSCWP
     165-582: Missing.

Note: No experimental confirmation available.
Show »
Length:164
Mass (Da):19,034
Checksum:iADEC71EC3A43B28E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381E → V in BAF84020 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei134 – 16431VCGRE…DGIWI → LKNKRGRKGIEANSPPKRVV KRVQTWTSCWP in isoform 2. 1 PublicationVSP_056085Add
BLAST
Alternative sequencei165 – 582418Missing in isoform 2. 1 PublicationVSP_056086Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007447 mRNA. Translation: BAA22541.1.
AK291331 mRNA. Translation: BAF84020.1.
AK295474 mRNA. Translation: BAG58401.1.
AC073575 Genomic DNA. No translation available.
BC003553 mRNA. Translation: AAH03553.1.
CCDSiCCDS9160.1. [O14545-1]
RefSeqiNP_001137378.1. NM_001143906.1. [O14545-1]
NP_006691.1. NM_006700.2. [O14545-1]
UniGeneiHs.5148.

Genome annotation databases

EnsembliENST00000257604; ENSP00000257604; ENSG00000135148. [O14545-1]
ENST00000412615; ENSP00000396526; ENSG00000135148. [O14545-1]
ENST00000552890; ENSP00000447340; ENSG00000135148. [O14545-2]
GeneIDi10906.
KEGGihsa:10906.
UCSCiuc001tto.4. human. [O14545-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007447 mRNA. Translation: BAA22541.1.
AK291331 mRNA. Translation: BAF84020.1.
AK295474 mRNA. Translation: BAG58401.1.
AC073575 Genomic DNA. No translation available.
BC003553 mRNA. Translation: AAH03553.1.
CCDSiCCDS9160.1. [O14545-1]
RefSeqiNP_001137378.1. NM_001143906.1. [O14545-1]
NP_006691.1. NM_006700.2. [O14545-1]
UniGeneiHs.5148.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9KNMR-A78-139[»]
ProteinModelPortaliO14545.
SMRiO14545. Positions 30-65, 78-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116112. 20 interactions.
IntActiO14545. 15 interactions.
STRINGi9606.ENSP00000257604.

PTM databases

iPTMnetiO14545.
PhosphoSiteiO14545.

Polymorphism and mutation databases

BioMutaiTRAFD1.

Proteomic databases

EPDiO14545.
MaxQBiO14545.
PaxDbiO14545.
PeptideAtlasiO14545.
PRIDEiO14545.

Protocols and materials databases

DNASUi10906.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257604; ENSP00000257604; ENSG00000135148. [O14545-1]
ENST00000412615; ENSP00000396526; ENSG00000135148. [O14545-1]
ENST00000552890; ENSP00000447340; ENSG00000135148. [O14545-2]
GeneIDi10906.
KEGGihsa:10906.
UCSCiuc001tto.4. human. [O14545-1]

Organism-specific databases

CTDi10906.
GeneCardsiTRAFD1.
HGNCiHGNC:24808. TRAFD1.
HPAiHPA039254.
HPA039266.
MIMi613197. gene.
neXtProtiNX_O14545.
PharmGKBiPA142670704.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGBJ. Eukaryota.
ENOG4111IF3. LUCA.
GeneTreeiENSGT00530000063869.
HOGENOMiHOG000154674.
HOVERGENiHBG094084.
InParanoidiO14545.
OMAiAEQDFWR.
OrthoDBiEOG76473W.
PhylomeDBiO14545.
TreeFamiTF331416.

Miscellaneous databases

ChiTaRSiTRAFD1. human.
EvolutionaryTraceiO14545.
GeneWikiiTRAFD1.
GenomeRNAii10906.
PROiO14545.
SOURCEiSearch...

Gene expression databases

BgeeiO14545.
CleanExiHS_TRAFD1.
ExpressionAtlasiO14545. baseline and differential.
GenevisibleiO14545. HS.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "TRAF interacting Zn finger protein."
    Nezu J.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Hippocampus and Tongue.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skin.
  5. "FLN29, a novel interferon- and LPS-inducible gene acting as a negative regulator of toll-like receptor signaling."
    Mashima R., Saeki K., Aki D., Minoda Y., Takaki H., Sanada T., Kobayashi T., Aburatani H., Yamanashi Y., Yoshimura A.
    J. Biol. Chem. 280:41289-41297(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRAF6.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327; SER-415 AND SER-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-327 AND SER-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-327; SER-409 AND SER-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Solution structure of the ZF-TRAF domain of FLN29 gene product."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 78-139 IN COMPLEX WITH ZINC IONS.

Entry informationi

Entry nameiTRAD1_HUMAN
AccessioniPrimary (citable) accession number: O14545
Secondary accession number(s): A8K5L6, B4DI89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.