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Protein

Down syndrome cell adhesion molecule-like protein 1

Gene

DSCAML1

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

Functioni

Cell adhesion molecule that plays a role in neuronal self-avoidance (PubMed:11453658). Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Promotes both isoneuronal self-avoidance for creating an orderly neurite arborization in retinal rod bipolar cells and heteroneuronal self-avoidance to maintain mosaic spacing between AII amacrine cells (By similarity). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity).By similarity1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • axonogenesis Source: UniProtKB
  • brain development Source: UniProtKB
  • cell fate determination Source: UniProtKB
  • central nervous system development Source: UniProtKB
  • dorsal/ventral pattern formation Source: UniProtKB
  • embryonic skeletal system morphogenesis Source: UniProtKB
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Neurogenesis

Enzyme and pathway databases

ReactomeiR-HSA-376172. DSCAM interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Down syndrome cell adhesion molecule-like protein 1
Alternative name(s):
Down syndrome cell adhesion molecule 2
Gene namesi
Name:DSCAML1
Synonyms:DSCAM2, KIAA11321 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:14656. DSCAML1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 15911573ExtracellularSequence analysisAdd
BLAST
Transmembranei1592 – 161221HelicalSequence analysisAdd
BLAST
Topological domaini1613 – 2053441CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cell surface Source: UniProtKB
  • extracellular space Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: Reactome
  • synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38384.

Polymorphism and mutation databases

BioMutaiDSCAML1.
DMDMi73620825.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 20532035Down syndrome cell adhesion molecule-like protein 1PRO_0000014748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi29 – 291N-linked (GlcNAc...)Sequence analysis
Disulfide bondi47 ↔ 103PROSITE-ProRule annotation
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence analysis
Disulfide bondi146 ↔ 198PROSITE-ProRule annotation
Disulfide bondi247 ↔ 294PROSITE-ProRule annotation
Disulfide bondi336 ↔ 386PROSITE-ProRule annotation
Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence analysis
Disulfide bondi429 ↔ 485PROSITE-ProRule annotation
Glycosylationi471 – 4711N-linked (GlcNAc...)Sequence analysis
Glycosylationi513 – 5131N-linked (GlcNAc...)Sequence analysis
Disulfide bondi526 ↔ 575PROSITE-ProRule annotation
Glycosylationi556 – 5561N-linked (GlcNAc...)Sequence analysis
Disulfide bondi617 ↔ 669PROSITE-ProRule annotation
Glycosylationi666 – 6661N-linked (GlcNAc...)Sequence analysis
Glycosylationi710 – 7101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi711 ↔ 767PROSITE-ProRule annotation
Glycosylationi749 – 7491N-linked (GlcNAc...)Sequence analysis
Glycosylationi796 – 7961N-linked (GlcNAc...)Sequence analysis
Glycosylationi809 – 8091N-linked (GlcNAc...)Sequence analysis
Disulfide bondi810 ↔ 867PROSITE-ProRule annotation
Glycosylationi926 – 9261N-linked (GlcNAc...)Sequence analysis
Glycosylationi1082 – 10821N-linked (GlcNAc...)Sequence analysis
Glycosylationi1144 – 11441N-linked (GlcNAc...)Sequence analysis
Glycosylationi1162 – 11621N-linked (GlcNAc...)Sequence analysis
Glycosylationi1275 – 12751N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1311 ↔ 1363PROSITE-ProRule annotation
Glycosylationi1345 – 13451N-linked (GlcNAc...)Sequence analysis
Glycosylationi1492 – 14921N-linked (GlcNAc...)Sequence analysis
Glycosylationi1531 – 15311N-linked (GlcNAc...)Sequence analysis
Glycosylationi1561 – 15611N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ8TD84.
PaxDbiQ8TD84.
PeptideAtlasiQ8TD84.
PRIDEiQ8TD84.

PTM databases

iPTMnetiQ8TD84.

Expressioni

Tissue specificityi

Detected in heart, liver, pancreas, skeletal muscle, kidney and in brain, in particular in the amygdala, caudate nucleus, corpus callosum, hippocampus, substantia nigra, thalamus and subthalamus.2 Publications

Gene expression databases

BgeeiQ8TD84.
CleanExiHS_DSCAML1.
ExpressionAtlasiQ8TD84. baseline and differential.
GenevisibleiQ8TD84. HS.

Organism-specific databases

HPAiCAB025540.

Interactioni

Subunit structurei

Homodimer; mediates homophilic interactions to promote cell adhesion.By similarity

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi121525. 3 interactions.
IntActiQ8TD84. 3 interactions.
STRINGi9606.ENSP00000315465.

Structurei

Secondary structure

1
2053
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi991 – 9977Combined sources
Beta strandi999 – 100810Combined sources
Beta strandi1021 – 103010Combined sources
Beta strandi1046 – 105510Combined sources
Beta strandi1062 – 10709Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VA9NMR-A979-1087[»]
ProteinModelPortaliQ8TD84.
SMRiQ8TD84. Positions 981-1091.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TD84.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 119101Ig-like C2-type 1Add
BLAST
Domaini115 – 217103Ig-like C2-type 2Add
BLAST
Domaini226 – 30681Ig-like C2-type 3Add
BLAST
Domaini314 – 40289Ig-like C2-type 4Add
BLAST
Domaini408 – 50194Ig-like C2-type 5Add
BLAST
Domaini506 – 58681Ig-like C2-type 6Add
BLAST
Domaini596 – 68590Ig-like C2-type 7Add
BLAST
Domaini690 – 78495Ig-like C2-type 8Add
BLAST
Domaini788 – 88598Ig-like C2-type 9Add
BLAST
Domaini887 – 98498Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini989 – 1088100Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini1093 – 118997Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini1193 – 128896Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini1278 – 1377100Ig-like C2-type 10Add
BLAST
Domaini1383 – 147795Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini1478 – 1578101Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1956 – 201661Pro-richAdd
BLAST

Sequence similaritiesi

Contains 6 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IQJM. Eukaryota.
ENOG410XQX7. LUCA.
HOGENOMiHOG000112277.
HOVERGENiHBG051409.
InParanoidiQ8TD84.
KOiK06768.
PhylomeDBiQ8TD84.
TreeFamiTF316846.

Family and domain databases

Gene3Di2.60.40.10. 16 hits.
InterProiIPR033029. DSCAML1.
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PANTHERiPTHR10489:SF171. PTHR10489:SF171. 1 hit.
PfamiPF00041. fn3. 5 hits.
PF07679. I-set. 4 hits.
[Graphical view]
SMARTiSM00060. FN3. 6 hits.
SM00409. IG. 10 hits.
SM00408. IGc2. 9 hits.
SM00406. IGv. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 10 hits.
SSF49265. SSF49265. 3 hits.
PROSITEiPS50853. FN3. 6 hits.
PS50835. IG_LIKE. 9 hits.
[Graphical view]

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: Q8TD84-1) [UniParc]FASTAAdd to basket

Also known as: 1a

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
MWLVTFLLLL DSLHKARPED VGTSLYFVND SLQQVTFSSS VGVVVPCPAA
60 70 80 90 100
GSPSAALRWY LATGDDIYDV PHIRHVHANG TLQLYPFSPS AFNSFIHDND
110 120 130 140 150
YFCTAENAAG KIRSPNIRVK AVFREPYTVR VEDQRSMRGN VAVFKCLIPS
160 170 180 190 200
SVQEYVSVVS WEKDTVSIIP EHRFFITYHG GLYISDVQKE DALSTYRCIT
210 220 230 240 250
KHKYSGETRQ SNGARLSVTD PAESIPTILD GFHSQEVWAG HTVELPCTAS
260 270 280 290 300
GYPIPAIRWL KDGRPLPADS RWTKRITGLT ISDLRTEDSG TYICEVTNTF
310 320 330 340 350
GSAEATGILM VIDPLHVTLT PKKLKTGIGS TVILSCALTG SPEFTIRWYR
360 370 380 390 400
NTELVLPDEA ISIRGLSNET LLITSAQKSH SGAYQCFATR KAQTAQDFAI
410 420 430 440 450
IALEDGTPRI VSSFSEKVVN PGEQFSLMCA AKGAPPPTVT WALDDEPIVR
460 470 480 490 500
DGSHRTNQYT MSDGTTISHM NVTGPQIRDG GVYRCTARNL VGSAEYQARI
510 520 530 540 550
NVRGPPSIRA MRNITAVAGR DTLINCRVIG YPYYSIKWYK DALLLPDNHR
560 570 580 590 600
QVVFENGTLK LTDVQKGMDE GEYLCSVLIQ PQLSISQSVH VAVKVPPLIQ
610 620 630 640 650
PFEFPPASIG QLLYIPCVVS SGDMPIRITW RKDGQVIISG SGVTIESKEF
660 670 680 690 700
MSSLQISSVS LKHNGNYTCI ASNAAATVSR ERQLIVRVPP RFVVQPNNQD
710 720 730 740 750
GIYGKAGVLN CSVDGYPPPK VMWKHAKGSG NPQQYHPVPL TGRIQILPNS
760 770 780 790 800
SLLIRHVLEE DIGYYLCQAS NGVGTDISKS MFLTVKIPAM ITSHPNTTIA
810 820 830 840 850
IKGHAKELNC TARGERPIII RWEKGDTVID PDRVMRYAIA TKDNGDEVVS
860 870 880 890 900
TLKLKPADRG DSVFFSCHAI NSYGEDRGLI QLTVQEPPDP PELEIREVKA
910 920 930 940 950
RSMNLRWTQR FDGNSIITGF DIEYKNKSDS WDFKQSTRNI SPTINQANIV
960 970 980 990 1000
DLHPASVYSI RMYSFNKIGR SEPSKELTIS TEEAAPDGPP MDVTLQPVTS
1010 1020 1030 1040 1050
QSIQVTWKAP KKELQNGVIR GYQIGYRENS PGSNGQYSIV EMKATGDSEV
1060 1070 1080 1090 1100
YTLDNLKKFA QYGVVVQAFN RAGTGPSSSE INATTLEDVP SQPPENVRAL
1110 1120 1130 1140 1150
SITSDVAVIS WSEPPRSTLN GVLKGYRVIF WSLYVDGEWG EMQNITTTRE
1160 1170 1180 1190 1200
RVELRGMEKF TNYSVQVLAY TQAGDGVRSS VLYIQTKEDV PGPPAGIKAV
1210 1220 1230 1240 1250
PSSASSVVVS WLPPTKPNGV IRKYTIFCSS PGSGQPAPSE YETSPEQLFY
1260 1270 1280 1290 1300
RIAHLNRGQQ YLLWVAAVTS AGRGNSSEKV TIEPAGKAPA KIISFGGTVT
1310 1320 1330 1340 1350
TPWMKDVRLP CNSVGDPAPA VKWTKDSEDS AIPVSMDGHR LIHTNGTLLL
1360 1370 1380 1390 1400
RAVKAEDSGY YTCTATNTGG FDTIIVNLLV QVPPDQPRLT VSKTSASSIT
1410 1420 1430 1440 1450
LTWIPGDNGG SSIRGFVLQY SVDNSEEWKD VFISSSERSF KLDSLKCGTW
1460 1470 1480 1490 1500
YKVKLAAKNS VGSGRISEII EAKTHGREPS FSKDQHLFTH INSTHARLNL
1510 1520 1530 1540 1550
QGWNNGGCPI TAIVLEYRPK GTWAWQGLRA NSSGEVFLTE LREATWYELR
1560 1570 1580 1590 1600
MRACNSAGCG NETAQFATLD YDGSTIPPIK SAQGEGDDVK KLFTIGCPVI
1610 1620 1630 1640 1650
LATLGVALLF IVRKKRKEKR LKRLRDAKSL AEMLISKNNR SFDTPVKGPP
1660 1670 1680 1690 1700
QGPRLHIDIP RVQLLIEDKE GIKQLGDDKA TIPVTDAEFS QAVNPQSFCT
1710 1720 1730 1740 1750
GVSLHHPTLI QSTGPLIDMS DIRPGTNPVS RKNVKSAHST RNRYSSQWTL
1760 1770 1780 1790 1800
TKCQASTPAR TLTSDWRTVG SQHGVTVTES DSYSASLSQD TDKGRNSMVS
1810 1820 1830 1840 1850
TESASSTYEE LARAYEHAKL EEQLQHAKFE ITECFISDSS SDQMTTGTNE
1860 1870 1880 1890 1900
NADSMTSMST PSEPGICRFT ASPPKPQDAD RGKNVAVPIP HRANKSDYCN
1910 1920 1930 1940 1950
LPLYAKSEAF FRKADGREPC PVVPPREASI RNLARTYHTQ ARHLTLDPAS
1960 1970 1980 1990 2000
KSLGLPHPGA PAAASTATLP QRTLAMPAPP AGTAPPAPGP TPAEPPTAPS
2010 2020 2030 2040 2050
AAPPAPSTEP PRAGGPHTKM GGSRDSLLEM STSGVGRSQK QGAGAYSKSY

TLV
Length:2,053
Mass (Da):224,463
Last modified:August 16, 2005 - v2
Checksum:i9CC9644214FF19C4
GO
Isoform 2 (identifier: Q8TD84-2) [UniParc]FASTAAdd to basket

Also known as: 1b

The sequence of this isoform differs from the canonical sequence as follows:
     34-244: Missing.

Show »
Length:1,842
Mass (Da):200,982
Checksum:i238314CA48D908D2
GO

Sequence cautioni

The sequence AAM09558.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA86446.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41V → L in AAN32613 (Ref. 3) Curated
Sequence conflicti4 – 41V → L in AAN32614 (Ref. 3) Curated
Sequence conflicti150 – 1523SSV → FLG in AAN32613 (Ref. 3) Curated
Sequence conflicti172 – 1721H → N in AAL57166 (PubMed:11453658).Curated
Sequence conflicti172 – 1721H → N in BAA86446 (PubMed:10574461).Curated
Sequence conflicti250 – 2501S → P in AAN32614 (Ref. 3) Curated
Sequence conflicti469 – 4691H → Y in AAN32613 (Ref. 3) Curated
Sequence conflicti667 – 6671Y → D in AAN32613 (Ref. 3) Curated
Sequence conflicti667 – 6671Y → D in AAN32614 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti659 – 6591V → I in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035512
Natural varianti1702 – 17021V → I in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035513

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei34 – 244211Missing in isoform 2. 1 PublicationVSP_014978Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF334384 mRNA. Translation: AAL57166.1.
AF491813 mRNA. Translation: AAM09558.1. Different initiation.
AF304304 mRNA. Translation: AAN32613.1.
AF304305 mRNA. Translation: AAN32614.1.
AB032958 mRNA. Translation: BAA86446.2. Different initiation.
AP000711 Genomic DNA. No translation available.
AP000757 Genomic DNA. No translation available.
AP001554 Genomic DNA. No translation available.
AP002342 Genomic DNA. No translation available.
RefSeqiNP_065744.2. NM_020693.3.
UniGeneiHs.659513.

Genome annotation databases

EnsembliENST00000321322; ENSP00000315465; ENSG00000177103.
GeneIDi57453.
KEGGihsa:57453.
UCSCiuc001prh.1. human. [Q8TD84-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF334384 mRNA. Translation: AAL57166.1.
AF491813 mRNA. Translation: AAM09558.1. Different initiation.
AF304304 mRNA. Translation: AAN32613.1.
AF304305 mRNA. Translation: AAN32614.1.
AB032958 mRNA. Translation: BAA86446.2. Different initiation.
AP000711 Genomic DNA. No translation available.
AP000757 Genomic DNA. No translation available.
AP001554 Genomic DNA. No translation available.
AP002342 Genomic DNA. No translation available.
RefSeqiNP_065744.2. NM_020693.3.
UniGeneiHs.659513.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VA9NMR-A979-1087[»]
ProteinModelPortaliQ8TD84.
SMRiQ8TD84. Positions 981-1091.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121525. 3 interactions.
IntActiQ8TD84. 3 interactions.
STRINGi9606.ENSP00000315465.

PTM databases

iPTMnetiQ8TD84.

Polymorphism and mutation databases

BioMutaiDSCAML1.
DMDMi73620825.

Proteomic databases

EPDiQ8TD84.
PaxDbiQ8TD84.
PeptideAtlasiQ8TD84.
PRIDEiQ8TD84.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321322; ENSP00000315465; ENSG00000177103.
GeneIDi57453.
KEGGihsa:57453.
UCSCiuc001prh.1. human. [Q8TD84-1]

Organism-specific databases

CTDi57453.
GeneCardsiDSCAML1.
HGNCiHGNC:14656. DSCAML1.
HPAiCAB025540.
MIMi611782. gene.
neXtProtiNX_Q8TD84.
PharmGKBiPA38384.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQJM. Eukaryota.
ENOG410XQX7. LUCA.
HOGENOMiHOG000112277.
HOVERGENiHBG051409.
InParanoidiQ8TD84.
KOiK06768.
PhylomeDBiQ8TD84.
TreeFamiTF316846.

Enzyme and pathway databases

ReactomeiR-HSA-376172. DSCAM interactions.

Miscellaneous databases

ChiTaRSiDSCAML1. human.
EvolutionaryTraceiQ8TD84.
GenomeRNAii57453.
PROiQ8TD84.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TD84.
CleanExiHS_DSCAML1.
ExpressionAtlasiQ8TD84. baseline and differential.
GenevisibleiQ8TD84. HS.

Family and domain databases

Gene3Di2.60.40.10. 16 hits.
InterProiIPR033029. DSCAML1.
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PANTHERiPTHR10489:SF171. PTHR10489:SF171. 1 hit.
PfamiPF00041. fn3. 5 hits.
PF07679. I-set. 4 hits.
[Graphical view]
SMARTiSM00060. FN3. 6 hits.
SM00409. IG. 10 hits.
SM00408. IGc2. 9 hits.
SM00406. IGv. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 10 hits.
SSF49265. SSF49265. 3 hits.
PROSITEiPS50853. FN3. 6 hits.
PS50835. IG_LIKE. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional characterization of DSCAML1, a novel DSCAM-like cell adhesion molecule that mediates homophilic intercellular adhesion."
    Agarwala K.L., Ganesh S., Tsutsumi Y., Suzuki T., Amano K., Yamakawa K.
    Biochem. Biophys. Res. Commun. 285:760-772(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  2. "Mammalian DSCAMs: roles in the development of the spinal cord, cortex, and cerebellum?"
    Barlow G.M., Micales B., Chen X.-N., Lyons G.E., Korenberg J.R.
    Biochem. Biophys. Res. Commun. 293:881-891(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  3. "DSCAML1, a novel member of the immunoglobulin superfamily."
    Lin S., Wang Z., Ying K., Xie Y., Mao Y.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Fetal brain.
  4. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
    Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
    DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Solution structure of the second FNIII domain of DSCAML1 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 979-1087.
  8. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-659 AND ILE-1702.

Entry informationi

Entry nameiDSCL1_HUMAN
AccessioniPrimary (citable) accession number: Q8TD84
Secondary accession number(s): Q76MU9
, Q8IZY3, Q8IZY4, Q8WXU7, Q9ULT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: July 6, 2016
This is version 131 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.