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Q14031 (CO4A6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-6(IV) chain
Gene names
Name:COL4A6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1691 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane.

Domain

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.

Post-translational modification

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.

Involvement in disease

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). Ref.6 Ref.7

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. Ref.9

Sequence similarities

Belongs to the type IV collagen family.

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q14031-1)

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.
Isoform B (identifier: Q14031-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 16911669Collagen alpha-6(IV) chain
PRO_0000005853

Regions

Domain1467 – 1691225Collagen IV NC1
Region23 – 46247S domain
Region47 – 14631417Triple-helical region
Motif515 – 5173Cell attachment site Potential
Motif560 – 5623Cell attachment site Potential
Motif986 – 9883Cell attachment site Potential

Amino acid modifications

Glycosylation1271N-linked (GlcNAc...) Potential
Disulfide bond1482 ↔ 1571Or C-1482 with C-1568 By similarity
Disulfide bond1515 ↔ 1568Or C-1515 with C-1571 By similarity
Disulfide bond1527 ↔ 1533 By similarity
Disulfide bond1590 ↔ 1687Or C-1590 with C-1684 By similarity
Disulfide bond1624 ↔ 1684Or C-1624 with C-1687 By similarity
Disulfide bond1636 ↔ 1643 By similarity

Natural variations

Alternative sequence1 – 55MLINK → MHPG in isoform B.
VSP_001174
Natural variant4551S → A. Ref.3
Corresponds to variant rs1042065 [ dbSNP | Ensembl ].
VAR_015216
Natural variant4551S → P.
Corresponds to variant rs1042065 [ dbSNP | Ensembl ].
VAR_059242
Natural variant5911G → S in DFNX6. Ref.9
VAR_070936
Natural variant11101N → K. Ref.3
Corresponds to variant rs1042067 [ dbSNP | Ensembl ].
VAR_015217
Natural variant11261P → S.
Corresponds to variant rs35179844 [ dbSNP | Ensembl ].
VAR_032972
Natural variant11301G → E in a colorectal cancer sample; somatic mutation. Ref.8
VAR_035748
Natural variant11621I → V.
Corresponds to variant rs34466065 [ dbSNP | Ensembl ].
VAR_032973
Natural variant13621L → P.
Corresponds to variant rs35363062 [ dbSNP | Ensembl ].
VAR_032974

Experimental info

Sequence conflict1701M → I in AAA19569. Ref.2
Sequence conflict1701M → I in AAA16338. Ref.5
Sequence conflict272 – 2732IS → LR in AAB19038. Ref.3
Sequence conflict272 – 2732IS → LR in AAB19039. Ref.3
Sequence conflict3661V → D in AAB19038. Ref.3
Sequence conflict3661V → D in AAB19039. Ref.3
Sequence conflict5181R → Q in AAB19038. Ref.3
Sequence conflict5181R → Q in AAB19039. Ref.3
Sequence conflict9171P → S in BAA04809. Ref.1
Sequence conflict9171P → S in AAB19038. Ref.3
Sequence conflict9171P → S in AAB19039. Ref.3
Sequence conflict1302 – 131312Missing in BAA04809. Ref.1
Sequence conflict13561P → A in BAA04809. Ref.1
Sequence conflict13651D → H in AAB19038. Ref.3
Sequence conflict13651D → H in AAB19039. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 9313294D4CE63067

FASTA1,691163,807
        10         20         30         40         50         60 
MLINKLWLLL VTLCLTEELA AAGEKSYGKP CGGQDCSGSC QCFPEKGARG RPGPIGIQGP 

        70         80         90        100        110        120 
TGPQGFTGST GLSGLKGERG FPGLLGPYGP KGDKGPMGVP GFLGINGIPG HPGQPGPRGP 

       130        140        150        160        170        180 
PGLDGCNGTQ GAVGFPGPDG YPGLLGPPGL PGQKGSKGDP VLAPGSFKGM KGDPGLPGLD 

       190        200        210        220        230        240 
GITGPQGAPG FPGAVGPAGP PGLQGPPGPP GPLGPDGNMG LGFQGEKGVK GDVGLPGPAG 

       250        260        270        280        290        300 
PPPSTGELEF MGFPKGKKGS KGEPGPKGFP GISGPPGFPG LGTTGEKGEK GEKGIPGLPG 

       310        320        330        340        350        360 
PRGPMGSEGV QGPPGQQGKK GTLGFPGLNG FQGIEGQKGD IGLPGPDVFI DIDGAVISGN 

       370        380        390        400        410        420 
PGDPGVPGLP GLKGDEGIQG LRGPSGVPGL PALSGVPGAL GPQGFPGLKG DQGNPGRTTI 

       430        440        450        460        470        480 
GAAGLPGRDG LPGPPGPPGP PSPEFETETL HNKESGFPGL RGEQGPKGNL GLKGIKGDSG 

       490        500        510        520        530        540 
FCACDGGVPN TGPPGEPGPP GPWGLIGLPG LKGARGDRGS GGAQGPAGAP GLVGPLGPSG 

       550        560        570        580        590        600 
PKGKKGEPIL STIQGMPGDR GDSGSQGFRG VIGEPGKDGV PGLPGLPGLP GDGGQGFPGE 

       610        620        630        640        650        660 
KGLPGLPGEK GHPGPPGLPG NGLPGLPGPR GLPGDKGKDG LPGQQGLPGS KGITLPCIIP 

       670        680        690        700        710        720 
GSYGPSGFPG TPGFPGPKGS RGLPGTPGQP GSSGSKGEPG SPGLVHLPEL PGFPGPRGEK 

       730        740        750        760        770        780 
GLPGFPGLPG KDGLPGMIGS PGLPGSKGAT GDIFGAENGA PGEQGLQGLT GHKGFLGDSG 

       790        800        810        820        830        840 
LPGLKGVHGK PGLLGPKGER GSPGTPGQVG QPGTPGSSGP YGIKGKSGLP GAPGFPGISG 

       850        860        870        880        890        900 
HPGKKGTRGK KGPPGSIVKK GLPGLKGLPG NPGLVGLKGS PGSPGVAGLP ALSGPKGEKG 

       910        920        930        940        950        960 
SVGFVGFPGI PGLPGIPGTR GLKGIPGSTG KMGPSGRAGT PGEKGDRGNP GPVGIPSPRR 

       970        980        990       1000       1010       1020 
PMSNLWLKGD KGSQGSAGSN GFPGPRGDKG EAGRPGPPGL PGAPGLPGII KGVSGKPGPP 

      1030       1040       1050       1060       1070       1080 
GFMGIRGLPG LKGSSGITGF PGMPGESGSQ GIRGSPGLPG ASGLPGLKGD NGQTVEISGS 

      1090       1100       1110       1120       1130       1140 
PGPKGQPGES GFKGTKGRDG LIGNIGFPGN KGEDGKVGVS GDVGLPGAPG FPGVAGMRGE 

      1150       1160       1170       1180       1190       1200 
PGLPGSSGHQ GAIGPLGSPG LIGPKGFPGF PGLHGLNGLP GTKGTHGTPG PSITGVPGPA 

      1210       1220       1230       1240       1250       1260 
GLPGPKGEKG YPGIGIGAPG KPGLRGQKGD RGFPGLQGPA GLPGAPGISL PSLIAGQPGD 

      1270       1280       1290       1300       1310       1320 
PGRPGLDGER GRPGPAGPPG PPGPSSNQGD TGDPGFPGIP GPKGPKGDQG IPGFSGLPGE 

      1330       1340       1350       1360       1370       1380 
LGLKGMRGEP GFMGTPGKVG PPGDPGFPGM KGKAGPRGSS GLQGDPGQTP TAEAVQVPPG 

      1390       1400       1410       1420       1430       1440 
PLGLPGIDGI PGLTGDPGAQ GPVGLQGSKG LPGIPGKDGP SGLPGPPGAL GDPGLPGLQG 

      1450       1460       1470       1480       1490       1500 
PPGFEGAPGQ QGPFGMPGMP GQSMRVGYTL VKHSQSEQVP PCPIGMSQLW VGYSLLFVEG 

      1510       1520       1530       1540       1550       1560 
QEKAHNQDLG FAGSCLPRFS TMPFIYCNIN EVCHYARRND KSYWLSTTAP IPMMPVSQTQ 

      1570       1580       1590       1600       1610       1620 
IPQYISRCSV CEAPSQAIAV HSQDITIPQC PLGWRSLWIG YSFLMHTAAG AEGGGQSLVS 

      1630       1640       1650       1660       1670       1680 
PGSCLEDFRA TPFIECSGAR GTCHYFANKY SFWLTTVEER QQFGELPVSE TLKAGQLHTR 

      1690 
VSRCQVCMKS L 

« Hide

Isoform B [UniParc].

Checksum: A311225C5FF212B9
Show »

FASTA1,690163,629

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Alport syndrome with diffuse leiomyomatosis."
Anker M.C., Arnemann J., Neumann K., Ahrens P., Schmidt H., Koenig R.
Am. J. Med. Genet. A 119:381-385(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN DL-ATS.
[8]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D21337 mRNA. Translation: BAA04809.1.
U04845 mRNA. Translation: AAA19569.2.
U47004 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , AL031177, AL034369, AL109943 Genomic DNA. Translation: CAI40756.1.
AL136080 expand/collapse EMBL AC list , AL031177, AL034369, AL109943 Genomic DNA. Translation: CAI40758.1.
AL034369 expand/collapse EMBL AC list , AL031177, AL109943, AL136080 Genomic DNA. Translation: CAI42045.1.
AL034369 expand/collapse EMBL AC list , AL031177, AL109943, AL136080 Genomic DNA. Translation: CAI42047.1.
AL109943 expand/collapse EMBL AC list , AL031177, AL034369, AL136080 Genomic DNA. Translation: CAI42993.1.
AL109943 expand/collapse EMBL AC list , AL031177, AL034369, AL136080 Genomic DNA. Translation: CAI42995.1.
AL031177 expand/collapse EMBL AC list , AL034369, AL109943, AL136080 Genomic DNA. Translation: CAI43139.1.
AL031177 expand/collapse EMBL AC list , AL034369, AL109943, AL136080 Genomic DNA. Translation: CAI43140.1.
CH471120 Genomic DNA. Translation: EAX02688.1.
L22763 mRNA. Translation: AAA16338.1.
CCDSCCDS14541.1. [Q14031-1]
CCDS14542.1. [Q14031-2]
PIRCGHU6B. A54122.
RefSeqNP_001274689.1. NM_001287760.1.
NP_001838.2. NM_001847.3. [Q14031-1]
NP_378667.1. NM_033641.3. [Q14031-2]
UniGeneHs.145586.

3D structure databases

ProteinModelPortalQ14031.
SMRQ14031. Positions 1466-1689.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107685. 2 interactions.
IntActQ14031. 1 interaction.

Chemistry

ChEMBLCHEMBL2364188.

PTM databases

PhosphoSiteQ14031.

Polymorphism databases

DMDM116241307.

Proteomic databases

MaxQBQ14031.
PaxDbQ14031.
PRIDEQ14031.

Protocols and materials databases

DNASU1288.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334504; ENSP00000334733; ENSG00000197565. [Q14031-2]
ENST00000372216; ENSP00000361290; ENSG00000197565. [Q14031-1]
GeneID1288.
KEGGhsa:1288.
UCSCuc004env.4. human. [Q14031-2]
uc004enw.4. human. [Q14031-1]

Organism-specific databases

CTD1288.
GeneCardsGC0XM107386.
H-InvDBHIX0056214.
HGNCHGNC:2208. COL4A6.
MIM300914. phenotype.
303631. gene.
neXtProtNX_Q14031.
Orphanet1018. X-linked diffuse leiomyomatosis - Alport syndrome.
90625. X-linked nonsyndromic sensorineural deafness type DFN.
PharmGKBPA26723.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG004933.
KOK06237.
OrthoDBEOG7RZ5P3.
PhylomeDBQ14031.
TreeFamTF344135.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ14031.
BgeeQ14031.
GenevestigatorQ14031.

Family and domain databases

Gene3D2.170.240.10. 1 hit.
InterProIPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view]
PfamPF01413. C4. 2 hits.
PF01391. Collagen. 22 hits.
[Graphical view]
SMARTSM00111. C4. 2 hits.
[Graphical view]
SUPFAMSSF56436. SSF56436. 2 hits.
PROSITEPS51403. NC1_IV. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCOL4A6.
GenomeRNAi1288.
NextBio5213.
PMAP-CutDBQ5JYH8.
PROQ14031.
SOURCESearch...

Entry information

Entry nameCO4A6_HUMAN
AccessionPrimary (citable) accession number: Q14031
Secondary accession number(s): Q12823 expand/collapse secondary AC list , Q14053, Q5JYH6, Q5JYH8, Q9NQM5, Q9NTX3, Q9UJ76, Q9UMG6, Q9Y4L4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM