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P43146

- DCC_HUMAN

UniProt

P43146 - DCC_HUMAN

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Protein

Netrin receptor DCC

Gene

DCC

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

Functioni

Receptor for netrin required for axon guidance. Mediates axon attraction of neuronal growth cones in the developing nervous system upon ligand binding. Its association with UNC5 proteins may trigger signaling for axon repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. Implicated as a tumor suppressor gene.2 Publications

GO - Molecular functioni

  1. netrin receptor activity Source: Ensembl
  2. transcription coactivator activity Source: Ensembl
  3. transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

  1. anterior/posterior axon guidance Source: Ensembl
  2. apoptotic process Source: Reactome
  3. axon guidance Source: Reactome
  4. axonogenesis Source: ProtInc
  5. dorsal/ventral axon guidance Source: Ensembl
  6. negative regulation of collateral sprouting Source: BHF-UCL
  7. negative regulation of dendrite development Source: BHF-UCL
  8. negative regulation of neuron projection development Source: BHF-UCL
  9. neuron migration Source: Ensembl
  10. positive regulation of apoptotic process Source: Reactome
  11. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  12. positive regulation of neuron projection development Source: Ensembl
  13. regulation of apoptotic process Source: Reactome
  14. response to amphetamine Source: Ensembl
  15. spinal cord ventral commissure morphogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_22128. Role of DCC in regulating apoptosis.
REACT_22228. Role of second messengers in netrin-1 signaling.
REACT_22237. Netrin-1 signaling.
REACT_22351. DCC mediated attractive signaling.
REACT_22384. Netrin mediated repulsion signals.
REACT_25299. DSCAM interactions.

Protein family/group databases

MEROPSiI43.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Netrin receptor DCC
Alternative name(s):
Colorectal cancer suppressor
Immunoglobulin superfamily DCC subclass member 1
Tumor suppressor protein DCC
Gene namesi
Name:DCC
Synonyms:IGDCC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:2701. DCC.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 10971072ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1098 – 112225HelicalSequence AnalysisAdd
BLAST
Topological domaini1123 – 1447325CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. axon Source: Ensembl
  2. cytosol Source: Reactome
  3. growth cone membrane Source: Ensembl
  4. integral component of membrane Source: UniProtKB-KW
  5. membrane raft Source: Ensembl
  6. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Mirror movements 1 (MRMV1) [MIM:157600]: A disorder characterized by contralateral involuntary movements that mirror voluntary ones. While mirror movements are occasionally found in young children, persistence beyond the age of 10 is abnormal. Mirror movements occur more commonly in the upper extremities.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1432 – 14321L → S: Abolishes interaction with MYO10. 1 Publication
Mutagenesisi1435 – 14362LM → SS: Abolishes interaction with MYO10. 1 Publication
Mutagenesisi1439 – 14391L → S: Abolishes interaction with MYO10. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

MIMi157600. phenotype.
Orphaneti238722. Familial congenital mirror movements.
PharmGKBiPA27170.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 14471422Netrin receptor DCCPRO_0000014744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi61 ↔ 117PROSITE-ProRule annotation
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi161 ↔ 212PROSITE-ProRule annotation
Disulfide bondi261 ↔ 310PROSITE-ProRule annotation
Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi318 – 3181N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi352 ↔ 400PROSITE-ProRule annotation
Glycosylationi478 – 4781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi628 – 6281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi702 – 7021N-linked (GlcNAc...)Sequence Analysis
Modified residuei1178 – 11781Phosphoserine; by MAPK1By similarity
Modified residuei1187 – 11871Phosphothreonine; by MAPK1By similarity
Modified residuei1267 – 12671Phosphoserine; by MAPK1By similarity

Post-translational modificationi

Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation.Curated

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP43146.
PRIDEiP43146.

PTM databases

PhosphoSiteiP43146.

Expressioni

Tissue specificityi

Found in axons of the central and peripheral nervous system and in differentiated cell types of the intestine. Not expressed in colorectal tumor cells that lost their capacity to differentiate into mucus producing cells.1 Publication

Gene expression databases

BgeeiP43146.
CleanExiHS_DCC.
ExpressionAtlasiP43146. baseline.
GenevestigatoriP43146.

Organism-specific databases

HPAiCAB002311.

Interactioni

Subunit structurei

Interacts with the cytoplasmic part of UNC5A, UNC5B, UNC5C and probably UNC5D. Interacts with DSCAM. Interacts with PTK2/FAK1 and MAPK1. Interacts with NTN1 (By similarity). Interacts with MYO10. Interacts with CBLN4; this interaction can be competed by NTN1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
MAZP562704EBI-1222919,EBI-1809742
MYO10Q9HD677EBI-1222919,EBI-307061
RPL28P467793EBI-1222919,EBI-366357
RPL5P467777EBI-1222919,EBI-358018
RPS23P622662EBI-1222919,EBI-353072

Protein-protein interaction databases

BioGridi107998. 41 interactions.
DIPiDIP-38423N.
IntActiP43146. 28 interactions.
STRINGi9606.ENSP00000389140.

Structurei

Secondary structure

1
1447
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi425 – 4284Combined sources
Beta strandi436 – 4405Combined sources
Beta strandi445 – 4484Combined sources
Beta strandi459 – 47012Combined sources
Beta strandi475 – 4784Combined sources
Beta strandi486 – 4894Combined sources
Beta strandi494 – 5007Combined sources
Beta strandi503 – 5086Combined sources
Beta strandi517 – 5204Combined sources
Beta strandi532 – 5376Combined sources
Beta strandi543 – 5497Combined sources
Beta strandi560 – 5678Combined sources
Turni568 – 5703Combined sources
Beta strandi573 – 5786Combined sources
Beta strandi583 – 5875Combined sources
Beta strandi593 – 6019Combined sources
Beta strandi606 – 6094Combined sources
Beta strandi613 – 6164Combined sources
Beta strandi631 – 6355Combined sources
Beta strandi638 – 6425Combined sources
Turni648 – 6503Combined sources
Beta strandi657 – 66812Combined sources
Beta strandi671 – 6744Combined sources
Beta strandi679 – 6846Combined sources
Beta strandi691 – 6944Combined sources
Beta strandi696 – 6994Combined sources
Beta strandi711 – 7144Combined sources
Beta strandi716 – 7194Combined sources
Beta strandi732 – 7365Combined sources
Beta strandi741 – 7455Combined sources
Beta strandi757 – 76610Combined sources
Beta strandi769 – 7757Combined sources
Beta strandi780 – 7834Combined sources
Beta strandi788 – 80013Combined sources
Beta strandi808 – 8103Combined sources
Beta strandi848 – 8547Combined sources
Beta strandi856 – 8583Combined sources
Beta strandi860 – 8656Combined sources
Beta strandi867 – 8693Combined sources
Beta strandi880 – 88910Combined sources
Beta strandi899 – 9079Combined sources
Beta strandi915 – 92410Combined sources
Beta strandi925 – 9273Combined sources
Beta strandi935 – 9384Combined sources
Beta strandi949 – 9557Combined sources
Beta strandi963 – 9686Combined sources
Beta strandi979 – 9868Combined sources
Beta strandi988 – 9903Combined sources
Beta strandi992 – 9954Combined sources
Beta strandi998 – 10003Combined sources
Beta strandi1005 – 10095Combined sources
Beta strandi1017 – 102610Combined sources
Beta strandi1037 – 10404Combined sources
Helixi1415 – 14217Combined sources
Helixi1425 – 144319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ED7NMR-A419-524[»]
2ED8NMR-A528-620[»]
2ED9NMR-A602-718[»]
2EDBNMR-A716-818[»]
2EDDNMR-A833-942[»]
2EDENMR-A944-1044[»]
3AU4X-ray1.90B1390-1447[»]
4URTX-ray3.10B844-1043[»]
ProteinModelPortaliP43146.
SMRiP43146. Positions 39-1047, 1414-1445.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43146.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 135110Ig-like C2-type 1Add
BLAST
Domaini139 – 22991Ig-like C2-type 2Add
BLAST
Domaini234 – 32693Ig-like C2-type 3Add
BLAST
Domaini331 – 41686Ig-like C2-type 4Add
BLAST
Domaini431 – 52494Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini530 – 62091Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini625 – 71894Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini728 – 82194Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini846 – 94297Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini947 – 104498Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1432 – 14398Interaction with MYO10

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. DCC family.Curated
Contains 6 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG249790.
GeneTreeiENSGT00770000120490.
HOGENOMiHOG000230686.
HOVERGENiHBG005455.
InParanoidiP43146.
KOiK06765.
OMAiWGPGESS.
OrthoDBiEOG7RRF65.
PhylomeDBiP43146.
TreeFamiTF321506.

Family and domain databases

Gene3Di2.60.40.10. 10 hits.
InterProiIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR010560. Neogenin_C.
[Graphical view]
PfamiPF00041. fn3. 6 hits.
PF07679. I-set. 3 hits.
PF06583. Neogenin_C. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 6 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 3 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 4 hits.
PROSITEiPS50853. FN3. 6 hits.
PS50835. IG_LIKE. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P43146-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MENSLRCVWV PKLAFVLFGA SLFSAHLQVT GFQIKAFTAL RFLSEPSDAV
60 70 80 90 100
TMRGGNVLLD CSAESDRGVP VIKWKKDGIH LALGMDERKQ QLSNGSLLIQ
110 120 130 140 150
NILHSRHHKP DEGLYQCEAS LGDSGSIISR TAKVAVAGPL RFLSQTESVT
160 170 180 190 200
AFMGDTVLLK CEVIGEPMPT IHWQKNQQDL TPIPGDSRVV VLPSGALQIS
210 220 230 240 250
RLQPGDIGIY RCSARNPASS RTGNEAEVRI LSDPGLHRQL YFLQRPSNVV
260 270 280 290 300
AIEGKDAVLE CCVSGYPPPS FTWLRGEEVI QLRSKKYSLL GGSNLLISNV
310 320 330 340 350
TDDDSGMYTC VVTYKNENIS ASAELTVLVP PWFLNHPSNL YAYESMDIEF
360 370 380 390 400
ECTVSGKPVP TVNWMKNGDV VIPSDYFQIV GGSNLRILGV VKSDEGFYQC
410 420 430 440 450
VAENEAGNAQ TSAQLIVPKP AIPSSSVLPS APRDVVPVLV SSRFVRLSWR
460 470 480 490 500
PPAEAKGNIQ TFTVFFSREG DNRERALNTT QPGSLQLTVG NLKPEAMYTF
510 520 530 540 550
RVVAYNEWGP GESSQPIKVA TQPELQVPGP VENLQAVSTS PTSILITWEP
560 570 580 590 600
PAYANGPVQG YRLFCTEVST GKEQNIEVDG LSYKLEGLKK FTEYSLRFLA
610 620 630 640 650
YNRYGPGVST DDITVVTLSD VPSAPPQNVS LEVVNSRSIK VSWLPPPSGT
660 670 680 690 700
QNGFITGYKI RHRKTTRRGE METLEPNNLW YLFTGLEKGS QYSFQVSAMT
710 720 730 740 750
VNGTGPPSNW YTAETPENDL DESQVPDQPS SLHVRPQTNC IIMSWTPPLN
760 770 780 790 800
PNIVVRGYII GYGVGSPYAE TVRVDSKQRY YSIERLESSS HYVISLKAFN
810 820 830 840 850
NAGEGVPLYE SATTRSITDP TDPVDYYPLL DDFPTSVPDL STPMLPPVGV
860 870 880 890 900
QAVALTHDAV RVSWADNSVP KNQKTSEVRL YTVRWRTSFS ASAKYKSEDT
910 920 930 940 950
TSLSYTATGL KPNTMYEFSV MVTKNRRSST WSMTAHATTY EAAPTSAPKD
960 970 980 990 1000
LTVITREGKP RAVIVSWQPP LEANGKITAY ILFYTLDKNI PIDDWIMETI
1010 1020 1030 1040 1050
SGDRLTHQIM DLNLDTMYYF RIQARNSKGV GPLSDPILFR TLKVEHPDKM
1060 1070 1080 1090 1100
ANDQGRHGDG GYWPVDTNLI DRSTLNEPPI GQMHPPHGSV TPQKNSNLLV
1110 1120 1130 1140 1150
IIVVTVGVIT VLVVVIVAVI CTRRSSAQQR KKRATHSAGK RKGSQKDLRP
1160 1170 1180 1190 1200
PDLWIHHEEM EMKNIEKPSG TDPAGRDSPI QSCQDLTPVS HSQSETQLGS
1210 1220 1230 1240 1250
KSTSHSGQDT EEAGSSMSTL ERSLAARRAP RAKLMIPMDA QSNNPAVVSA
1260 1270 1280 1290 1300
IPVPTLESAQ YPGILPSPTC GYPHPQFTLR PVPFPTLSVD RGFGAGRSQS
1310 1320 1330 1340 1350
VSEGPTTQQP PMLPPSQPEH SSSEEAPSRT IPTACVRPTH PLRSFANPLL
1360 1370 1380 1390 1400
PPPMSAIEPK VPYTPLLSQP GPTLPKTHVK TASLGLAGKA RSPLLPVSVP
1410 1420 1430 1440
TAPEVSEESH KPTEDSANVY EQDDLSEQMA SLEGLMKQLN AITGSAF
Length:1,447
Mass (Da):158,457
Last modified:May 18, 2010 - v2
Checksum:iBC17EA0E93DE8768
GO

Sequence cautioni

The sequence AAA52175.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAA52177.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAA52179.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAA52180.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti951 – 9511L → F in CAA53735. (PubMed:7926722)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231F → L.2 Publications
Corresponds to variant rs9951523 [ dbSNP | Ensembl ].
VAR_060257
Natural varianti168 – 1681M → T in a esophageal carcinoma. 1 Publication
VAR_003909
Natural varianti201 – 2011R → G.1 Publication
Corresponds to variant rs2229080 [ dbSNP | Ensembl ].
VAR_003910
Natural varianti679 – 6791L → R.
Corresponds to variant rs2271042 [ dbSNP | Ensembl ].
VAR_060258
Natural varianti759 – 7591I → M.
Corresponds to variant rs2278339 [ dbSNP | Ensembl ].
VAR_056043
Natural varianti1017 – 10171M → V.
Corresponds to variant rs984274 [ dbSNP | Ensembl ].
VAR_024495
Natural varianti1039 – 10391F → S in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035511
Natural varianti1191 – 11911H → L.
Corresponds to variant rs2270950 [ dbSNP | Ensembl ].
VAR_060259
Natural varianti1375 – 13751P → H in a colorectal carcinoma. 1 Publication
VAR_003911

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76132 mRNA. Translation: CAA53735.1.
AC011155 Genomic DNA. No translation available.
AC016383 Genomic DNA. No translation available.
AC019239 Genomic DNA. No translation available.
AC021486 Genomic DNA. No translation available.
AC027248 Genomic DNA. No translation available.
AC078999 Genomic DNA. No translation available.
AC090660 Genomic DNA. No translation available.
AC100777 Genomic DNA. No translation available.
AC103949 Genomic DNA. No translation available.
AC110591 Genomic DNA. No translation available.
AC116002 Genomic DNA. No translation available.
M32292 mRNA. Translation: AAA35751.1.
M32286 Genomic DNA. Translation: AAA52174.1.
M32288 Genomic DNA. Translation: AAA52175.1. Sequence problems.
M32290 Genomic DNA. Translation: AAA52176.1.
M63696 Genomic DNA. Translation: AAA52177.1. Different initiation.
M63700 Genomic DNA. Translation: AAA52178.1.
M63702 Genomic DNA. Translation: AAA52179.1. Different initiation.
M63718 Genomic DNA. Translation: AAA52180.1. Different initiation.
M63698 Genomic DNA. Translation: AAA52181.1.
CCDSiCCDS11952.1.
PIRiA54100.
RefSeqiNP_005206.2. NM_005215.3.
XP_005258261.1. XM_005258204.1.
UniGeneiHs.162025.

Genome annotation databases

EnsembliENST00000442544; ENSP00000389140; ENSG00000187323.
GeneIDi1630.
KEGGihsa:1630.
UCSCiuc002lfe.2. human.

Polymorphism databases

DMDMi296434474.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76132 mRNA. Translation: CAA53735.1 .
AC011155 Genomic DNA. No translation available.
AC016383 Genomic DNA. No translation available.
AC019239 Genomic DNA. No translation available.
AC021486 Genomic DNA. No translation available.
AC027248 Genomic DNA. No translation available.
AC078999 Genomic DNA. No translation available.
AC090660 Genomic DNA. No translation available.
AC100777 Genomic DNA. No translation available.
AC103949 Genomic DNA. No translation available.
AC110591 Genomic DNA. No translation available.
AC116002 Genomic DNA. No translation available.
M32292 mRNA. Translation: AAA35751.1 .
M32286 Genomic DNA. Translation: AAA52174.1 .
M32288 Genomic DNA. Translation: AAA52175.1 . Sequence problems.
M32290 Genomic DNA. Translation: AAA52176.1 .
M63696 Genomic DNA. Translation: AAA52177.1 . Different initiation.
M63700 Genomic DNA. Translation: AAA52178.1 .
M63702 Genomic DNA. Translation: AAA52179.1 . Different initiation.
M63718 Genomic DNA. Translation: AAA52180.1 . Different initiation.
M63698 Genomic DNA. Translation: AAA52181.1 .
CCDSi CCDS11952.1.
PIRi A54100.
RefSeqi NP_005206.2. NM_005215.3.
XP_005258261.1. XM_005258204.1.
UniGenei Hs.162025.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ED7 NMR - A 419-524 [» ]
2ED8 NMR - A 528-620 [» ]
2ED9 NMR - A 602-718 [» ]
2EDB NMR - A 716-818 [» ]
2EDD NMR - A 833-942 [» ]
2EDE NMR - A 944-1044 [» ]
3AU4 X-ray 1.90 B 1390-1447 [» ]
4URT X-ray 3.10 B 844-1043 [» ]
ProteinModelPortali P43146.
SMRi P43146. Positions 39-1047, 1414-1445.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107998. 41 interactions.
DIPi DIP-38423N.
IntActi P43146. 28 interactions.
STRINGi 9606.ENSP00000389140.

Protein family/group databases

MEROPSi I43.001.

PTM databases

PhosphoSitei P43146.

Polymorphism databases

DMDMi 296434474.

Proteomic databases

PaxDbi P43146.
PRIDEi P43146.

Protocols and materials databases

DNASUi 1630.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000442544 ; ENSP00000389140 ; ENSG00000187323 .
GeneIDi 1630.
KEGGi hsa:1630.
UCSCi uc002lfe.2. human.

Organism-specific databases

CTDi 1630.
GeneCardsi GC18P049802.
H-InvDB HIX0039754.
HGNCi HGNC:2701. DCC.
HPAi CAB002311.
MIMi 120470. gene.
157600. phenotype.
neXtProti NX_P43146.
Orphaneti 238722. Familial congenital mirror movements.
PharmGKBi PA27170.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG249790.
GeneTreei ENSGT00770000120490.
HOGENOMi HOG000230686.
HOVERGENi HBG005455.
InParanoidi P43146.
KOi K06765.
OMAi WGPGESS.
OrthoDBi EOG7RRF65.
PhylomeDBi P43146.
TreeFami TF321506.

Enzyme and pathway databases

Reactomei REACT_22128. Role of DCC in regulating apoptosis.
REACT_22228. Role of second messengers in netrin-1 signaling.
REACT_22237. Netrin-1 signaling.
REACT_22351. DCC mediated attractive signaling.
REACT_22384. Netrin mediated repulsion signals.
REACT_25299. DSCAM interactions.

Miscellaneous databases

ChiTaRSi DCC. human.
EvolutionaryTracei P43146.
GeneWikii Deleted_in_Colorectal_Cancer.
GenomeRNAii 1630.
NextBioi 6688.
PROi P43146.
SOURCEi Search...

Gene expression databases

Bgeei P43146.
CleanExi HS_DCC.
ExpressionAtlasi P43146. baseline.
Genevestigatori P43146.

Family and domain databases

Gene3Di 2.60.40.10. 10 hits.
InterProi IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR010560. Neogenin_C.
[Graphical view ]
Pfami PF00041. fn3. 6 hits.
PF07679. I-set. 3 hits.
PF06583. Neogenin_C. 1 hit.
[Graphical view ]
SMARTi SM00060. FN3. 6 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 3 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 4 hits.
PROSITEi PS50853. FN3. 6 hits.
PS50835. IG_LIKE. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The DCC gene product in cellular differentiation and colorectal tumorigenesis."
    Hedrick L., Cho K.R., Fearon E.R., Wu T.-C., Kinzler K.W., Vogelstein B.
    Genes Dev. 8:1174-1183(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT LEU-23.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-750, VARIANT LEU-23.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 107-472.
  5. "The DCC gene: structural analysis and mutations in colorectal carcinomas."
    Cho K.R., Oliner J.D., Simons J.W., Hedrick L., Fearon E.R., Preisinger A.C., Hedge P., Silverman G.A., Vogelstein B.
    Genomics 19:525-531(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE STRUCTURE, VARIANT HIS-1375.
  6. Cited for: FUNCTION.
  7. "Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway."
    Hu G., Zhang S., Vidal M., Baer J.L., Xu T., Fearon E.R.
    Genes Dev. 11:2701-2714(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIAH1 AND SIAH2, DEGRADATION.
  8. Cited for: INVOLVEMENT IN MRMV1.
  9. "Solution structure of the fibronectin type III domains of human netrin receptor DCC."
    RIKEN structural genomics initiative (RSGI)
    Submitted (MAR-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 419-1047.
  10. "Structural basis of cargo recognition by the myosin-X MyTH4-FERM domain."
    Hirano Y., Hatano T., Takahashi A., Toriyama M., Inagaki N., Hakoshima T.
    EMBO J. 30:2734-2747(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1390-1447 IN COMPLEX WITH MYO10, INTERACTION WITH MYO10, MUTAGENESIS OF LEU-1432; 1435-LEU-MET-1436 AND LEU-1439.
  11. "Point mutations and allelic deletion of tumor suppressor gene DCC in human esophageal squamous cell carcinomas and their relation to metastasis."
    Miyake S., Nagai K., Yoshino K., Oto M., Endo M., Yuasa Y.
    Cancer Res. 54:3007-3010(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-168 AND GLY-201, ROLE IN METASTATIC TUMOR DISSEMINATION.
  12. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-1039.

Entry informationi

Entry nameiDCC_HUMAN
AccessioniPrimary (citable) accession number: P43146
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 18, 2010
Last modified: November 26, 2014
This is version 149 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

Miscellaneous

Inactivation of DCC due to allelic deletion and/or point mutations is related to lymphatic and hematogenous metastatic tumor dissemination.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: 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

External Data

Dasty 3