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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).
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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 non-syndromic sensorineural deafness type DFN.
PharmGKBiPA26723.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 16911669Collagen alpha-6(IV) chainPRO_0000005853Add
BLAST

Amino acid modifications

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

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

BgeeiQ14031.
ExpressionAtlasiQ14031. baseline and differential.
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. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ14031.
SMRiQ14031. Positions 1466-1689.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1467 – 1691225Collagen IV NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 46247S domainAdd
BLAST
Regioni47 – 14631417Triple-helical regionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi515 – 5173Cell attachment siteSequence Analysis
Motifi560 – 5623Cell attachment siteSequence Analysis
Motifi986 – 9883Cell attachment siteSequence Analysis

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.PROSITE-ProRule annotation
Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000118776.
HOVERGENiHBG004933.
InParanoidiQ14031.
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

        10         20         30         40         50
MLINKLWLLL VTLCLTEELA AAGEKSYGKP CGGQDCSGSC QCFPEKGARG
60 70 80 90 100
RPGPIGIQGP TGPQGFTGST GLSGLKGERG FPGLLGPYGP KGDKGPMGVP
110 120 130 140 150
GFLGINGIPG HPGQPGPRGP PGLDGCNGTQ GAVGFPGPDG YPGLLGPPGL
160 170 180 190 200
PGQKGSKGDP VLAPGSFKGM KGDPGLPGLD GITGPQGAPG FPGAVGPAGP
210 220 230 240 250
PGLQGPPGPP GPLGPDGNMG LGFQGEKGVK GDVGLPGPAG PPPSTGELEF
260 270 280 290 300
MGFPKGKKGS KGEPGPKGFP GISGPPGFPG LGTTGEKGEK GEKGIPGLPG
310 320 330 340 350
PRGPMGSEGV QGPPGQQGKK GTLGFPGLNG FQGIEGQKGD IGLPGPDVFI
360 370 380 390 400
DIDGAVISGN PGDPGVPGLP GLKGDEGIQG LRGPSGVPGL PALSGVPGAL
410 420 430 440 450
GPQGFPGLKG DQGNPGRTTI GAAGLPGRDG LPGPPGPPGP PSPEFETETL
460 470 480 490 500
HNKESGFPGL RGEQGPKGNL GLKGIKGDSG FCACDGGVPN TGPPGEPGPP
510 520 530 540 550
GPWGLIGLPG LKGARGDRGS GGAQGPAGAP GLVGPLGPSG PKGKKGEPIL
560 570 580 590 600
STIQGMPGDR GDSGSQGFRG VIGEPGKDGV PGLPGLPGLP GDGGQGFPGE
610 620 630 640 650
KGLPGLPGEK GHPGPPGLPG NGLPGLPGPR GLPGDKGKDG LPGQQGLPGS
660 670 680 690 700
KGITLPCIIP GSYGPSGFPG TPGFPGPKGS RGLPGTPGQP GSSGSKGEPG
710 720 730 740 750
SPGLVHLPEL PGFPGPRGEK GLPGFPGLPG KDGLPGMIGS PGLPGSKGAT
760 770 780 790 800
GDIFGAENGA PGEQGLQGLT GHKGFLGDSG LPGLKGVHGK PGLLGPKGER
810 820 830 840 850
GSPGTPGQVG QPGTPGSSGP YGIKGKSGLP GAPGFPGISG HPGKKGTRGK
860 870 880 890 900
KGPPGSIVKK GLPGLKGLPG NPGLVGLKGS PGSPGVAGLP ALSGPKGEKG
910 920 930 940 950
SVGFVGFPGI PGLPGIPGTR GLKGIPGSTG KMGPSGRAGT PGEKGDRGNP
960 970 980 990 1000
GPVGIPSPRR PMSNLWLKGD KGSQGSAGSN GFPGPRGDKG EAGRPGPPGL
1010 1020 1030 1040 1050
PGAPGLPGII KGVSGKPGPP GFMGIRGLPG LKGSSGITGF PGMPGESGSQ
1060 1070 1080 1090 1100
GIRGSPGLPG ASGLPGLKGD NGQTVEISGS PGPKGQPGES GFKGTKGRDG
1110 1120 1130 1140 1150
LIGNIGFPGN KGEDGKVGVS GDVGLPGAPG FPGVAGMRGE PGLPGSSGHQ
1160 1170 1180 1190 1200
GAIGPLGSPG LIGPKGFPGF PGLHGLNGLP GTKGTHGTPG PSITGVPGPA
1210 1220 1230 1240 1250
GLPGPKGEKG YPGIGIGAPG KPGLRGQKGD RGFPGLQGPA GLPGAPGISL
1260 1270 1280 1290 1300
PSLIAGQPGD PGRPGLDGER GRPGPAGPPG PPGPSSNQGD TGDPGFPGIP
1310 1320 1330 1340 1350
GPKGPKGDQG IPGFSGLPGE LGLKGMRGEP GFMGTPGKVG PPGDPGFPGM
1360 1370 1380 1390 1400
KGKAGPRGSS GLQGDPGQTP TAEAVQVPPG PLGLPGIDGI PGLTGDPGAQ
1410 1420 1430 1440 1450
GPVGLQGSKG LPGIPGKDGP SGLPGPPGAL GDPGLPGLQG PPGFEGAPGQ
1460 1470 1480 1490 1500
QGPFGMPGMP GQSMRVGYTL VKHSQSEQVP PCPIGMSQLW VGYSLLFVEG
1510 1520 1530 1540 1550
QEKAHNQDLG FAGSCLPRFS TMPFIYCNIN EVCHYARRND KSYWLSTTAP
1560 1570 1580 1590 1600
IPMMPVSQTQ IPQYISRCSV CEAPSQAIAV HSQDITIPQC PLGWRSLWIG
1610 1620 1630 1640 1650
YSFLMHTAAG AEGGGQSLVS PGSCLEDFRA TPFIECSGAR GTCHYFANKY
1660 1670 1680 1690
SFWLTTVEER QQFGELPVSE TLKAGQLHTR VSRCQVCMKS L
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701M → I in AAA19569. (PubMed:8175748)Curated
Sequence conflicti170 – 1701M → I in AAA16338. 1 PublicationCurated
Sequence conflicti272 – 2732IS → LR in AAB19038. (PubMed:8661006)Curated
Sequence conflicti272 – 2732IS → LR in AAB19039. (PubMed:8661006)Curated
Sequence conflicti366 – 3661V → D in AAB19038. (PubMed:8661006)Curated
Sequence conflicti366 – 3661V → D in AAB19039. (PubMed:8661006)Curated
Sequence conflicti518 – 5181R → Q in AAB19038. (PubMed:8661006)Curated
Sequence conflicti518 – 5181R → Q in AAB19039. (PubMed:8661006)Curated
Sequence conflicti917 – 9171P → S in BAA04809. (PubMed:8125972)Curated
Sequence conflicti917 – 9171P → S in AAB19038. (PubMed:8661006)Curated
Sequence conflicti917 – 9171P → S in AAB19039. (PubMed:8661006)Curated
Sequence conflicti1302 – 131312Missing in BAA04809. (PubMed:8125972)CuratedAdd
BLAST
Sequence conflicti1356 – 13561P → A in BAA04809. (PubMed:8125972)Curated
Sequence conflicti1365 – 13651D → H in AAB19038. (PubMed:8661006)Curated
Sequence conflicti1365 – 13651D → H in AAB19039. (PubMed:8661006)Curated

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. 1 PublicationVSP_001174

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. 2 interactions.

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 non-syndromic sensorineural deafness type DFN.
PharmGKBi PA26723.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118776.
HOVERGENi HBG004933.
InParanoidi Q14031.
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

Bgeei Q14031.
ExpressionAtlasi Q14031. baseline and differential.
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: October 29, 2014
This is version 153 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