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Protein

Dixin

Gene

DIXDC1

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

Functioni

Positive effector of the Wnt signaling pathway; activates WNT3A signaling via DVL2. Regulates JNK activation by AXIN1 and DVL2.2 Publications

GO - Molecular functioni

  • gamma-tubulin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Dixin
Alternative name(s):
Coiled-coil protein DIX1
Short name:
Coiled-coil-DIX1
DIX domain-containing protein 1
Gene namesi
Name:DIXDC1
Synonyms:CCD1, KIAA1735
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:23695. DIXDC1.

Subcellular locationi

Isoform 1 :

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB
  • focal adhesion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi648 – 6481D → A: Loss of interaction with DVL2. Abolishes activation of Wnt signaling. 1 Publication
Mutagenesisi651 – 6511F → A: Loss of interaction with DVL2. Abolishes activation of Wnt signaling. 1 Publication
Mutagenesisi655 – 6551K → A: Loss of interaction with DVL2. Abolishes activation of Wnt signaling. 1 Publication

Organism-specific databases

PharmGKBiPA134988674.

Polymorphism and mutation databases

DMDMi147641721.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 683683DixinPRO_0000287223Add
BLAST
Isoform 2 (identifier: Q155Q3-2)
Initiator methionineiRemoved

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei186 – 1861PhosphoserineBy similarity
Modified residuei231 – 2311PhosphoserineBy similarity
Modified residuei590 – 5901PhosphoserineCombined sources
Isoform 2 (identifier: Q155Q3-2)
Lipidationi2 – 21N-myristoyl glycine

Post-translational modificationi

Phosphorylated on tyrosine and serine residues.1 Publication
Polyubiquitinated, leading to its proteasomal degradation. WNT3A signaling increases DIXDC1 protein levels by inhibiting its ubiquitination and subsequent degradation.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ155Q3.
MaxQBiQ155Q3.
PaxDbiQ155Q3.
PRIDEiQ155Q3.

PTM databases

iPTMnetiQ155Q3.
PhosphoSiteiQ155Q3.

Expressioni

Tissue specificityi

Ubiquitously expressed with higher expression in cardiac and skeletal muscles.1 Publication

Gene expression databases

BgeeiQ155Q3.
CleanExiHS_DIXDC1.
ExpressionAtlasiQ155Q3. baseline and differential.
GenevisibleiQ155Q3. HS.

Interactioni

Subunit structurei

Isoform 1 but not isoform 2 binds filamentous actin. Interacts with the complex composed of DVL2 and Rac. Interacts with AXIN1; competes with MAP3K1. Interacts with MAP3K4 preventing MAP3K4 interaction with AXIN1. Directly interacts (via DIX domain) with DVL2 (via DIX domain). Interacts with gamma-tubulin.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DVL2O146412EBI-1104700,EBI-740850
Dvl2Q608384EBI-1104700,EBI-641940From a different organism.

GO - Molecular functioni

  • gamma-tubulin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi124542. 19 interactions.
IntActiQ155Q3. 20 interactions.
MINTiMINT-8080298.
STRINGi9606.ENSP00000394352.

Structurei

Secondary structure

1
683
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi601 – 6066Combined sources
Beta strandi614 – 6207Combined sources
Helixi627 – 6348Combined sources
Beta strandi640 – 6489Combined sources
Turni649 – 6513Combined sources
Beta strandi652 – 6587Combined sources
Beta strandi671 – 6788Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PZ7X-ray2.44A597-683[»]
ProteinModelPortaliQ155Q3.
SMRiQ155Q3. Positions 20-125, 594-679.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 127108CHPROSITE-ProRule annotationAdd
BLAST
Domaini600 – 68081DIXPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni127 – 300174Actin-bindingAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili279 – 452174Sequence analysisAdd
BLAST

Domaini

The coiled-coil domain mediates interaction with MAP3K4 and inhibition of AXIN1-mediated JNK activation through MAP3K4.1 Publication
The DIX domain mediates interaction with AXIN1 and inhibition of AXIN1-mediated JNK activation through MAP3K1. Mediates interaction with DVL2; this interaction is required for activation of Wnt signaling.1 Publication

Sequence similaritiesi

Belongs to the DIXDC1 family.Curated
Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
Contains 1 DIX domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFNC. Eukaryota.
ENOG410XPPR. LUCA.
GeneTreeiENSGT00390000013552.
HOVERGENiHBG107812.
InParanoidiQ155Q3.
OMAiETSWEEQ.
PhylomeDBiQ155Q3.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR001158. DIX.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00307. CH. 1 hit.
PF00778. DIX. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 1 hit.
SM00021. DAX. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50021. CH. 1 hit.
PS50841. DIX. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q155Q3-1) [UniParc]FASTAAdd to basket

Also known as: l-DIXDC1

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
MLACLTRGNL LDVLQEGFNE QQLQAYVAWV NAQLKKRPAV KPVQDLRQDL
60 70 80 90 100
RDGVILAYLI EIVAGEKLSG VQLSPGNQQE MKNNVEKVLQ FVASKKIRMH
110 120 130 140 150
QTSAKDIVDG NLKSIMRLVL ALAAHFKPGS SRTVNQGRDS RAPLQSHRPH
160 170 180 190 200
CATAVAQGAA AALADVCHDM SRSGRDVFRY RQRNSSMDEE IENPYWSVRA
210 220 230 240 250
LVQQYEGQQR SPSESSCSSL TSPSPIHSAK SESIITQSEE KADFVIIPAE
260 270 280 290 300
GIENRTEGTD SPLSRDWRPG SPGTYLETSW EEQLLEQQEY LEKEMEEAKK
310 320 330 340 350
MISGLQALLL NGSLPEDEQE RPLALCEPGV NPEEQLIIIQ SRLDQSMEEN
360 370 380 390 400
QDLKKELLKC KQEARNLQGI KDALQQRLTQ QDTSVLQLKQ ELLRANMDKD
410 420 430 440 450
ELHNQNVDLQ RKLDERNRLL GEYKKELGQK DRLLQQHQAK LEEALRKLSD
460 470 480 490 500
VSYHQVDLER ELEHKDVLLA HCMKREADEA TNYNSHNSQS NGFLLPTAGK
510 520 530 540 550
GATSVSNRGT SDLQLVRDAL RSLRNSFSGH DPQHHTIDSL EQGISSLMER
560 570 580 590 600
LHVMETQKKQ ERKVRVKSPR TQVGSEYRES WPPNSKLPHS QSSPTVSSTC
610 620 630 640 650
TKVLYFTDRS LTPFMVNIPK RLEEVTLKDF KAAIDREGNH RYHFKALDPE
660 670 680
FGTVKEEIFH DDDAIPGWEG KIVAWVEEDH GEN
Note: Major isoform. Ubiquitously expressed.
Length:683
Mass (Da):77,478
Last modified:May 15, 2007 - v2
Checksum:iE643D1A69B00238C
GO
Isoform 2 (identifier: Q155Q3-2) [UniParc]FASTAAdd to basket

Also known as: s-DIXDC1

The sequence of this isoform differs from the canonical sequence as follows:
     1-211: Missing.
     212-219: PSESSCSS → MGGTQVKC

Note: Major isoform. Preferentially expressed in cardiac and skeletal muscles.
Show »
Length:472
Mass (Da):53,942
Checksum:i70C4312A59CAAF47
GO
Isoform 3 (identifier: Q155Q3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-219: S → R
     220-683: Missing.

Note: No experimental confirmation available.
Show »
Length:219
Mass (Da):24,428
Checksum:iF27E0386517E1EAB
GO
Isoform 4 (identifier: Q155Q3-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MLACLTRGNLLDVLQEGFNE → MGTQVVMRFNNSLLPTEPS
     219-219: S → R
     220-683: Missing.

Note: No experimental confirmation available.
Show »
Length:218
Mass (Da):24,313
Checksum:i7EC65502524E280C
GO

Sequence cautioni

The sequence AAH35509.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH64479.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAB21826.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB71039.1 differs from that shown.Probable cloning artifact.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 1401S → P in ABG25914 (PubMed:16814745).Curated
Sequence conflicti144 – 1441L → R in ABG25914 (PubMed:16814745).Curated
Sequence conflicti168 – 1681H → Q in ABG25914 (PubMed:16814745).Curated
Sequence conflicti378 – 3781L → S in BAB71039 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti300 – 3001K → R.
Corresponds to variant rs34575249 [ dbSNP | Ensembl ].
VAR_032294

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 211211Missing in isoform 2. 2 PublicationsVSP_025378Add
BLAST
Alternative sequencei1 – 2020MLACL…EGFNE → MGTQVVMRFNNSLLPTEPS in isoform 4. 1 PublicationVSP_054565Add
BLAST
Alternative sequencei212 – 2198PSESSCSS → MGGTQVKC in isoform 2. 2 PublicationsVSP_025379
Alternative sequencei219 – 2191S → R in isoform 3 and isoform 4. 1 PublicationVSP_025380
Alternative sequencei220 – 683464Missing in isoform 3 and isoform 4. 1 PublicationVSP_025381Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ642016 mRNA. Translation: ABG25914.1.
AB051522 mRNA. Translation: BAB21826.1. Different initiation.
AP000907 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67171.1.
BC033034 mRNA. Translation: AAH33034.1.
BC035509 mRNA. Translation: AAH35509.1. Sequence problems.
BC041626 mRNA. Translation: AAH41626.2.
BC048294 mRNA. Translation: AAH48294.1.
BC064479 mRNA. Translation: AAH64479.1. Sequence problems.
BC128600 mRNA. Translation: AAI28601.1.
AK055899 mRNA. Translation: BAB71039.1. Sequence problems.
CCDSiCCDS60957.1. [Q155Q3-5]
CCDS73381.1. [Q155Q3-1]
CCDS73382.1. [Q155Q3-2]
RefSeqiNP_001033043.1. NM_001037954.3. [Q155Q3-1]
NP_001265471.1. NM_001278542.1. [Q155Q3-5]
NP_219493.1. NM_033425.4. [Q155Q3-2]
UniGeneiHs.655626.

Genome annotation databases

EnsembliENST00000440460; ENSP00000394352; ENSG00000150764. [Q155Q3-1]
ENST00000529225; ENSP00000434130; ENSG00000150764. [Q155Q3-5]
ENST00000615255; ENSP00000480808; ENSG00000150764. [Q155Q3-2]
GeneIDi85458.
KEGGihsa:85458.
UCSCiuc001pmj.4. human. [Q155Q3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ642016 mRNA. Translation: ABG25914.1.
AB051522 mRNA. Translation: BAB21826.1. Different initiation.
AP000907 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67171.1.
BC033034 mRNA. Translation: AAH33034.1.
BC035509 mRNA. Translation: AAH35509.1. Sequence problems.
BC041626 mRNA. Translation: AAH41626.2.
BC048294 mRNA. Translation: AAH48294.1.
BC064479 mRNA. Translation: AAH64479.1. Sequence problems.
BC128600 mRNA. Translation: AAI28601.1.
AK055899 mRNA. Translation: BAB71039.1. Sequence problems.
CCDSiCCDS60957.1. [Q155Q3-5]
CCDS73381.1. [Q155Q3-1]
CCDS73382.1. [Q155Q3-2]
RefSeqiNP_001033043.1. NM_001037954.3. [Q155Q3-1]
NP_001265471.1. NM_001278542.1. [Q155Q3-5]
NP_219493.1. NM_033425.4. [Q155Q3-2]
UniGeneiHs.655626.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PZ7X-ray2.44A597-683[»]
ProteinModelPortaliQ155Q3.
SMRiQ155Q3. Positions 20-125, 594-679.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124542. 19 interactions.
IntActiQ155Q3. 20 interactions.
MINTiMINT-8080298.
STRINGi9606.ENSP00000394352.

PTM databases

iPTMnetiQ155Q3.
PhosphoSiteiQ155Q3.

Polymorphism and mutation databases

DMDMi147641721.

Proteomic databases

EPDiQ155Q3.
MaxQBiQ155Q3.
PaxDbiQ155Q3.
PRIDEiQ155Q3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000440460; ENSP00000394352; ENSG00000150764. [Q155Q3-1]
ENST00000529225; ENSP00000434130; ENSG00000150764. [Q155Q3-5]
ENST00000615255; ENSP00000480808; ENSG00000150764. [Q155Q3-2]
GeneIDi85458.
KEGGihsa:85458.
UCSCiuc001pmj.4. human. [Q155Q3-1]

Organism-specific databases

CTDi85458.
GeneCardsiDIXDC1.
HGNCiHGNC:23695. DIXDC1.
MIMi610493. gene.
neXtProtiNX_Q155Q3.
PharmGKBiPA134988674.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFNC. Eukaryota.
ENOG410XPPR. LUCA.
GeneTreeiENSGT00390000013552.
HOVERGENiHBG107812.
InParanoidiQ155Q3.
OMAiETSWEEQ.
PhylomeDBiQ155Q3.

Miscellaneous databases

ChiTaRSiDIXDC1. human.
GeneWikiiDIXDC1.
GenomeRNAii85458.
NextBioi35504789.
PROiQ155Q3.
SOURCEiSearch...

Gene expression databases

BgeeiQ155Q3.
CleanExiHS_DIXDC1.
ExpressionAtlasiQ155Q3. baseline and differential.
GenevisibleiQ155Q3. HS.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR001158. DIX.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00307. CH. 1 hit.
PF00778. DIX. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 1 hit.
SM00021. DAX. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50021. CH. 1 hit.
PS50841. DIX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DIXDC1 isoform, l-DIXDC1, is a novel filamentous actin-binding protein."
    Wang X., Zheng L., Zeng Z., Zhou G., Chien J., Qian C., Vasmatzis G., Shridhar V., Chen L., Liu W.
    Biochem. Biophys. Res. Commun. 347:22-30(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH ACTIN.
  2. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "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] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-293 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-218 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 327-683 (ISOFORMS 1/2).
    Tissue: Brain and Uterus.
  4. "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] OF 257-683 (ISOFORMS 1/2).
    Tissue: Mammary gland.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal kinase activation by Axin and dishevelled through distinct mechanisms."
    Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.
    J. Biol. Chem. 279:39366-39373(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AXIN1; DVL2; MAP3K4 AND RAC.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "DIXDC1 co-localizes and interacts with gamma-tubulin in HEK293 cells."
    Wu Y., Jing X., Ma X., Wu Y., Ding X., Fan W., Fan M.
    Cell Biol. Int. 33:697-701(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH GAMMA TUBULIN.
  10. "Wnt signaling stabilizes the DIXDC1 protein through decreased ubiquitin-dependent degradation."
    Wang L., Li H., Chen Q., Zhu T., Zhu H., Zheng L.
    Cancer Sci. 101:700-706(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION, UBIQUITINATION.
  11. "Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
    Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
    Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2 (ISOFORM 2).
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Molecular basis of Wnt activation via the DIX-domain protein Ccd1."
    Liu Y.T., Dan Q.J., Wang J., Feng Y., Chen L., Liang J., Li Q., Lin S.C., Wang Z.X., Wu J.W.
    J. Biol. Chem. 286:8597-8608(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 597-683, FUNCTION, MUTAGENESIS OF ASP-648; PHE-651 AND LYS-655, DOMAIN, INTERACTION WITH DVL2.

Entry informationi

Entry nameiDIXC1_HUMAN
AccessioniPrimary (citable) accession number: Q155Q3
Secondary accession number(s): A1A5D8
, E9PRV4, Q6P2J8, Q6PIK4, Q86SR7, Q8IVY4, Q96N69, Q9C0C8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: May 11, 2016
This is version 97 of the entry and version 2 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.