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Q14031

- CO4A6_HUMAN

UniProt

Q14031 - CO4A6_HUMAN

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Protein
Collagen alpha-6(IV) chain
Gene
COL4A6
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: InterPro

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. cellular response to amino acid stimulus Source: Ensembl
  3. collagen catabolic process Source: Reactome
  4. extracellular matrix disassembly Source: Reactome
  5. extracellular matrix organization Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_118779. Extracellular matrix organization.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150268. Anchoring fibril formation.
REACT_150401. Collagen degradation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_169262. Laminin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-6(IV) chain
Gene namesi
Name:COL4A6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:2208. COL4A6.

Subcellular locationi

GO - Cellular componenti

  1. collagen type IV trimer Source: UniProtKB
  2. endoplasmic reticulum lumen Source: Reactome
  3. extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Deletions covering the N-terminal regions of COL4A5 and COL4A6, which are localized in a head-to-head manner, are found in the chromosome Xq22.3 centromeric deletion syndrome. This results in a phenotype with features of diffuse leiomyomatosis and Alport syndrome (DL-ATS).2 Publications
Deafness, X-linked, 6 (DFNX6) [MIM:300914]: A non-syndromic form of sensorineural hearing loss with prelingual onset. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti591 – 5911G → S in DFNX6. 1 Publication
VAR_070936

Keywords - Diseasei

Deafness, Disease mutation, Non-syndromic deafness

Organism-specific databases

MIMi300914. phenotype.
Orphaneti1018. X-linked diffuse leiomyomatosis - Alport syndrome.
90625. X-linked nonsyndromic sensorineural deafness type DFN.
PharmGKBiPA26723.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed prediction
Add
BLAST
Chaini23 – 16911669Collagen alpha-6(IV) chain
PRO_0000005853Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi127 – 1271N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1482 ↔ 1571Or C-1482 with C-1568 By similarity
Disulfide bondi1515 ↔ 1568Or C-1515 with C-1571 By similarity
Disulfide bondi1527 ↔ 1533 By similarity
Disulfide bondi1590 ↔ 1687Or C-1590 with C-1684 By similarity
Disulfide bondi1624 ↔ 1684Or C-1624 with C-1687 By similarity
Disulfide bondi1636 ↔ 1643 By similarity

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.
The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiQ14031.
PaxDbiQ14031.
PRIDEiQ14031.

PTM databases

PhosphoSiteiQ14031.

Miscellaneous databases

PMAP-CutDBQ5JYH8.

Expressioni

Gene expression databases

ArrayExpressiQ14031.
BgeeiQ14031.
GenevestigatoriQ14031.

Interactioni

Subunit structurei

There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network.

Protein-protein interaction databases

BioGridi107685. 2 interactions.
IntActiQ14031. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ14031.
SMRiQ14031. Positions 1466-1689.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1467 – 1691225Collagen IV NC1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 46247S domain
Add
BLAST
Regioni47 – 14631417Triple-helical region
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi515 – 5173Cell attachment site Reviewed prediction
Motifi560 – 5623Cell attachment site Reviewed prediction
Motifi986 – 9883Cell attachment site Reviewed prediction

Domaini

Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain.

Sequence similaritiesi

Belongs to the type IV collagen family.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOVERGENiHBG004933.
KOiK06237.
OrthoDBiEOG7RZ5P3.
PhylomeDBiQ14031.
TreeFamiTF344135.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view]
PfamiPF01413. C4. 2 hits.
PF01391. Collagen. 22 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[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. Align

Isoform A (identifier: Q14031-1) [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

MLINKLWLLL VTLCLTEELA AAGEKSYGKP CGGQDCSGSC QCFPEKGARG     50
RPGPIGIQGP TGPQGFTGST GLSGLKGERG FPGLLGPYGP KGDKGPMGVP 100
GFLGINGIPG HPGQPGPRGP PGLDGCNGTQ GAVGFPGPDG YPGLLGPPGL 150
PGQKGSKGDP VLAPGSFKGM KGDPGLPGLD GITGPQGAPG FPGAVGPAGP 200
PGLQGPPGPP GPLGPDGNMG LGFQGEKGVK GDVGLPGPAG PPPSTGELEF 250
MGFPKGKKGS KGEPGPKGFP GISGPPGFPG LGTTGEKGEK GEKGIPGLPG 300
PRGPMGSEGV QGPPGQQGKK GTLGFPGLNG FQGIEGQKGD IGLPGPDVFI 350
DIDGAVISGN PGDPGVPGLP GLKGDEGIQG LRGPSGVPGL PALSGVPGAL 400
GPQGFPGLKG DQGNPGRTTI GAAGLPGRDG LPGPPGPPGP PSPEFETETL 450
HNKESGFPGL RGEQGPKGNL GLKGIKGDSG FCACDGGVPN TGPPGEPGPP 500
GPWGLIGLPG LKGARGDRGS GGAQGPAGAP GLVGPLGPSG PKGKKGEPIL 550
STIQGMPGDR GDSGSQGFRG VIGEPGKDGV PGLPGLPGLP GDGGQGFPGE 600
KGLPGLPGEK GHPGPPGLPG NGLPGLPGPR GLPGDKGKDG LPGQQGLPGS 650
KGITLPCIIP GSYGPSGFPG TPGFPGPKGS RGLPGTPGQP GSSGSKGEPG 700
SPGLVHLPEL PGFPGPRGEK GLPGFPGLPG KDGLPGMIGS PGLPGSKGAT 750
GDIFGAENGA PGEQGLQGLT GHKGFLGDSG LPGLKGVHGK PGLLGPKGER 800
GSPGTPGQVG QPGTPGSSGP YGIKGKSGLP GAPGFPGISG HPGKKGTRGK 850
KGPPGSIVKK GLPGLKGLPG NPGLVGLKGS PGSPGVAGLP ALSGPKGEKG 900
SVGFVGFPGI PGLPGIPGTR GLKGIPGSTG KMGPSGRAGT PGEKGDRGNP 950
GPVGIPSPRR PMSNLWLKGD KGSQGSAGSN GFPGPRGDKG EAGRPGPPGL 1000
PGAPGLPGII KGVSGKPGPP GFMGIRGLPG LKGSSGITGF PGMPGESGSQ 1050
GIRGSPGLPG ASGLPGLKGD NGQTVEISGS PGPKGQPGES GFKGTKGRDG 1100
LIGNIGFPGN KGEDGKVGVS GDVGLPGAPG FPGVAGMRGE PGLPGSSGHQ 1150
GAIGPLGSPG LIGPKGFPGF PGLHGLNGLP GTKGTHGTPG PSITGVPGPA 1200
GLPGPKGEKG YPGIGIGAPG KPGLRGQKGD RGFPGLQGPA GLPGAPGISL 1250
PSLIAGQPGD PGRPGLDGER GRPGPAGPPG PPGPSSNQGD TGDPGFPGIP 1300
GPKGPKGDQG IPGFSGLPGE LGLKGMRGEP GFMGTPGKVG PPGDPGFPGM 1350
KGKAGPRGSS GLQGDPGQTP TAEAVQVPPG PLGLPGIDGI PGLTGDPGAQ 1400
GPVGLQGSKG LPGIPGKDGP SGLPGPPGAL GDPGLPGLQG PPGFEGAPGQ 1450
QGPFGMPGMP GQSMRVGYTL VKHSQSEQVP PCPIGMSQLW VGYSLLFVEG 1500
QEKAHNQDLG FAGSCLPRFS TMPFIYCNIN EVCHYARRND KSYWLSTTAP 1550
IPMMPVSQTQ IPQYISRCSV CEAPSQAIAV HSQDITIPQC PLGWRSLWIG 1600
YSFLMHTAAG AEGGGQSLVS PGSCLEDFRA TPFIECSGAR GTCHYFANKY 1650
SFWLTTVEER QQFGELPVSE TLKAGQLHTR VSRCQVCMKS L 1691
Length:1,691
Mass (Da):163,807
Last modified:October 17, 2006 - v3
Checksum:i9313294D4CE63067
GO
Isoform B (identifier: Q14031-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MLINK → MHPG

Show »
Length:1,690
Mass (Da):163,629
Checksum:iA311225C5FF212B9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti455 – 4551S → A.1 Publication
Corresponds to variant rs1042065 [ dbSNP | Ensembl ].
VAR_015216
Natural varianti455 – 4551S → P.
Corresponds to variant rs1042065 [ dbSNP | Ensembl ].
VAR_059242
Natural varianti591 – 5911G → S in DFNX6. 1 Publication
VAR_070936
Natural varianti1110 – 11101N → K.1 Publication
Corresponds to variant rs1042067 [ dbSNP | Ensembl ].
VAR_015217
Natural varianti1126 – 11261P → S.
Corresponds to variant rs35179844 [ dbSNP | Ensembl ].
VAR_032972
Natural varianti1130 – 11301G → E in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035748
Natural varianti1162 – 11621I → V.
Corresponds to variant rs34466065 [ dbSNP | Ensembl ].
VAR_032973
Natural varianti1362 – 13621L → P.
Corresponds to variant rs35363062 [ dbSNP | Ensembl ].
VAR_032974

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 55MLINK → MHPG in isoform B.
VSP_001174

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701M → I in AAA19569. 1 Publication
Sequence conflicti170 – 1701M → I in AAA16338. 1 Publication
Sequence conflicti272 – 2732IS → LR in AAB19038. 1 Publication
Sequence conflicti272 – 2732IS → LR in AAB19039. 1 Publication
Sequence conflicti366 – 3661V → D in AAB19038. 1 Publication
Sequence conflicti366 – 3661V → D in AAB19039. 1 Publication
Sequence conflicti518 – 5181R → Q in AAB19038. 1 Publication
Sequence conflicti518 – 5181R → Q in AAB19039. 1 Publication
Sequence conflicti917 – 9171P → S in BAA04809. 1 Publication
Sequence conflicti917 – 9171P → S in AAB19038. 1 Publication
Sequence conflicti917 – 9171P → S in AAB19039. 1 Publication
Sequence conflicti1302 – 131312Missing in BAA04809. 1 Publication
Add
BLAST
Sequence conflicti1356 – 13561P → A in BAA04809. 1 Publication
Sequence conflicti1365 – 13651D → H in AAB19038. 1 Publication
Sequence conflicti1365 – 13651D → H in AAB19039. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D21337 mRNA. Translation: BAA04809.1.
U04845 mRNA. Translation: AAA19569.2.
U47004
, U46959, U46961, U46962, U46963, U46964, U46965, U46966, U46967, U46968, U46969, U46970, U46971, U46972, U46973, U46974, U46975, U46976, U46977, U46978, U46979, U46980, U46981, U46982, U46983, U46984, U46985, U46986, U46987, U46988, U46989, U46990, U46991, U46992, U46993, U46994, U46995, U46996, U46997, U46998, U46999, U47000, U47001, U47002, U47003 Genomic DNA. Translation: AAB19038.1.
U47004
, U46960, U46961, U46962, U46963, U46964, U46965, U46966, U46967, U46968, U46969, U46970, U46971, U46972, U46973, U46974, U46975, U46976, U46977, U46978, U46979, U46980, U46981, U46982, U46983, U46984, U46985, U46986, U46987, U46988, U46989, U46990, U46991, U46992, U46993, U46994, U46995, U46996, U46997, U46998, U46999, U47000, U47001, U47002, U47003 Genomic DNA. Translation: AAB19039.1.
AL136080
, AL031177, AL034369, AL109943 Genomic DNA. Translation: CAI40756.1.
AL136080
, AL031177, AL034369, AL109943 Genomic DNA. Translation: CAI40758.1.
AL034369
, AL031177, AL109943, AL136080 Genomic DNA. Translation: CAI42045.1.
AL034369
, AL031177, AL109943, AL136080 Genomic DNA. Translation: CAI42047.1.
AL109943
, AL031177, AL034369, AL136080 Genomic DNA. Translation: CAI42993.1.
AL109943
, AL031177, AL034369, AL136080 Genomic DNA. Translation: CAI42995.1.
AL031177
, AL034369, AL109943, AL136080 Genomic DNA. Translation: CAI43139.1.
AL031177
, AL034369, AL109943, AL136080 Genomic DNA. Translation: CAI43140.1.
CH471120 Genomic DNA. Translation: EAX02688.1.
L22763 mRNA. Translation: AAA16338.1.
CCDSiCCDS14541.1. [Q14031-1]
CCDS14542.1. [Q14031-2]
PIRiA54122. CGHU6B.
RefSeqiNP_001274689.1. NM_001287760.1.
NP_001838.2. NM_001847.3. [Q14031-1]
NP_378667.1. NM_033641.3. [Q14031-2]
UniGeneiHs.145586.

Genome annotation databases

EnsembliENST00000334504; ENSP00000334733; ENSG00000197565. [Q14031-2]
ENST00000372216; ENSP00000361290; ENSG00000197565. [Q14031-1]
GeneIDi1288.
KEGGihsa:1288.
UCSCiuc004env.4. human. [Q14031-2]
uc004enw.4. human. [Q14031-1]

Polymorphism databases

DMDMi116241307.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D21337 mRNA. Translation: BAA04809.1 .
U04845 mRNA. Translation: AAA19569.2 .
U47004
, U46959 , U46961 , U46962 , U46963 , U46964 , U46965 , U46966 , U46967 , U46968 , U46969 , U46970 , U46971 , U46972 , U46973 , U46974 , U46975 , U46976 , U46977 , U46978 , U46979 , U46980 , U46981 , U46982 , U46983 , U46984 , U46985 , U46986 , U46987 , U46988 , U46989 , U46990 , U46991 , U46992 , U46993 , U46994 , U46995 , U46996 , U46997 , U46998 , U46999 , U47000 , U47001 , U47002 , U47003 Genomic DNA. Translation: AAB19038.1 .
U47004
, U46960 , U46961 , U46962 , U46963 , U46964 , U46965 , U46966 , U46967 , U46968 , U46969 , U46970 , U46971 , U46972 , U46973 , U46974 , U46975 , U46976 , U46977 , U46978 , U46979 , U46980 , U46981 , U46982 , U46983 , U46984 , U46985 , U46986 , U46987 , U46988 , U46989 , U46990 , U46991 , U46992 , U46993 , U46994 , U46995 , U46996 , U46997 , U46998 , U46999 , U47000 , U47001 , U47002 , U47003 Genomic DNA. Translation: AAB19039.1 .
AL136080
, AL031177 , AL034369 , AL109943 Genomic DNA. Translation: CAI40756.1 .
AL136080
, AL031177 , AL034369 , AL109943 Genomic DNA. Translation: CAI40758.1 .
AL034369
, AL031177 , AL109943 , AL136080 Genomic DNA. Translation: CAI42045.1 .
AL034369
, AL031177 , AL109943 , AL136080 Genomic DNA. Translation: CAI42047.1 .
AL109943
, AL031177 , AL034369 , AL136080 Genomic DNA. Translation: CAI42993.1 .
AL109943
, AL031177 , AL034369 , AL136080 Genomic DNA. Translation: CAI42995.1 .
AL031177
, AL034369 , AL109943 , AL136080 Genomic DNA. Translation: CAI43139.1 .
AL031177
, AL034369 , AL109943 , AL136080 Genomic DNA. Translation: CAI43140.1 .
CH471120 Genomic DNA. Translation: EAX02688.1 .
L22763 mRNA. Translation: AAA16338.1 .
CCDSi CCDS14541.1. [Q14031-1 ]
CCDS14542.1. [Q14031-2 ]
PIRi A54122. CGHU6B.
RefSeqi NP_001274689.1. NM_001287760.1.
NP_001838.2. NM_001847.3. [Q14031-1 ]
NP_378667.1. NM_033641.3. [Q14031-2 ]
UniGenei Hs.145586.

3D structure databases

ProteinModelPortali Q14031.
SMRi Q14031. Positions 1466-1689.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107685. 2 interactions.
IntActi Q14031. 1 interaction.

Chemistry

ChEMBLi CHEMBL2364188.

PTM databases

PhosphoSitei Q14031.

Polymorphism databases

DMDMi 116241307.

Proteomic databases

MaxQBi Q14031.
PaxDbi Q14031.
PRIDEi Q14031.

Protocols and materials databases

DNASUi 1288.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000334504 ; ENSP00000334733 ; ENSG00000197565 . [Q14031-2 ]
ENST00000372216 ; ENSP00000361290 ; ENSG00000197565 . [Q14031-1 ]
GeneIDi 1288.
KEGGi hsa:1288.
UCSCi uc004env.4. human. [Q14031-2 ]
uc004enw.4. human. [Q14031-1 ]

Organism-specific databases

CTDi 1288.
GeneCardsi GC0XM107386.
H-InvDB HIX0056214.
HGNCi HGNC:2208. COL4A6.
MIMi 300914. phenotype.
303631. gene.
neXtProti NX_Q14031.
Orphaneti 1018. X-linked diffuse leiomyomatosis - Alport syndrome.
90625. X-linked nonsyndromic sensorineural deafness type DFN.
PharmGKBi PA26723.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOVERGENi HBG004933.
KOi K06237.
OrthoDBi EOG7RZ5P3.
PhylomeDBi Q14031.
TreeFami TF344135.

Enzyme and pathway databases

Reactomei REACT_118779. Extracellular matrix organization.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150268. Anchoring fibril formation.
REACT_150401. Collagen degradation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_169262. Laminin interactions.

Miscellaneous databases

GeneWikii COL4A6.
GenomeRNAii 1288.
NextBioi 5213.
PMAP-CutDB Q5JYH8.
PROi Q14031.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14031.
Bgeei Q14031.
Genevestigatori Q14031.

Family and domain databases

Gene3Di 2.170.240.10. 1 hit.
InterProi IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view ]
Pfami PF01413. C4. 2 hits.
PF01391. Collagen. 22 hits.
[Graphical view ]
SMARTi SM00111. C4. 2 hits.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 2 hits.
PROSITEi PS51403. NC1_IV. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a new collagen IV chain, alpha 6(IV), by cDNA isolation and assignment of the gene to chromosome Xq22, which is the same locus for COL4A5."
    Oohashi T., Sugimoto M., Mattei M.-G., Ninomiya Y.
    J. Biol. Chem. 269:7520-7526(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
    Tissue: Eye and Kidney.
  2. "Complete primary structure of the sixth chain of human basement membrane collagen, alpha 6(IV). Isolation of the cDNAs for alpha 6(IV) and comparison with five other type IV collagen chains."
    Zhou J., Ding M., Zhao Z., Reeders S.T.
    J. Biol. Chem. 269:13193-13199(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
  3. "Structure of the human type IV collagen COL4A6 gene, which is mutated in Alport syndrome-associated leiomyomatosis."
    Zhang X., Zhou J., Reeders S.T., Tryggvason K.
    Genomics 33:473-479(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B), VARIANTS ALA-455 AND LYS-1110.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Deletion of the paired alpha 5(IV) and alpha 6(IV) collagen genes in inherited smooth muscle tumors."
    Zhou J., Mochizuki T., Smeets H., Antignac C., Laurila P., de Paepe A., Tryggvason K., Reeders S.T.
    Science 261:1167-1169(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-542 (ISOFORM A), INVOLVEMENT IN DL-ATS.
  7. Cited for: INVOLVEMENT IN DL-ATS.
  8. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-1130.
  9. "Novel form of X-linked nonsyndromic hearing loss with cochlear malformation caused by a mutation in the type IV collagen gene COL4A6."
    Rost S., Bach E., Neuner C., Nanda I., Dysek S., Bittner R.E., Keller A., Bartsch O., Mlynski R., Haaf T., Mueller C.R., Kunstmann E.
    Eur. J. Hum. Genet. 22:208-215(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DFNX6 SER-591.

Entry informationi

Entry nameiCO4A6_HUMAN
AccessioniPrimary (citable) accession number: Q14031
Secondary accession number(s): Q12823
, Q14053, Q5JYH6, Q5JYH8, Q9NQM5, Q9NTX3, Q9UJ76, Q9UMG6, Q9Y4L4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: September 3, 2014
This is version 151 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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