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Q5VV43 (K0319_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dyslexia-associated protein KIAA0319
Gene names
Name:KIAA0319
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1072 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in neuronal migration during development of the cerebral neocortex. May function in a cell autonomous and a non-cell autonomous manner and play a role in appropriate adhesion between migrating neurons and radial glial fibers. May also regulate growth and differentiation of dendrites. Ref.11

Subunit structure

Homodimer. Interacts with AP2M1; required for clathrin-mediated endocytosis. Ref.9 Ref.10

Subcellular location

Cell membrane; Single-pass type I membrane protein. Early endosome membrane; Single-pass type I membrane protein. Note: Low-abundance isoforms lacking the transmembrane domain have been described; these are secreted. Ref.9 Ref.10

Tissue specificity

Detected in adult brain cortex and fetal frontal lobe (at protein level). Highly expressed in brain cortex, putamen, amygdala, hippocampus and cerebellum. Ref.6 Ref.8

Developmental stage

Expressed in the developing cerebral neocortex and glanglionic eminence in 57 days post-fertilization fetal brain. Ref.7

Post-translational modification

N-glycosylated. Ref.9

O-glycosylated. Ref.9

Shedding of the extracellular domain and intramembrane cleavage produce several proteolytic products. The intramembrane cleavage releases a soluble cytoplasmic polypeptide that translocates to the nucleolus.

Involvement in disease

Dyslexia 2 (DYX2) [MIM:600202]: A relatively common, complex cognitive disorder characterized by an impairment of reading performance despite adequate motivational, educational and intellectual opportunities. It is a multifactorial trait, with evidence for familial clustering and heritability.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.7

Sequence similarities

Contains 1 MANSC domain.

Contains 5 PKD domains.

Sequence caution

The sequence BAA20777.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q5VV43-1)

Also known as: A;

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 2 (identifier: Q5VV43-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MAPPTGVLSSLLLLVTIAG → MTRLGWPSPC
Isoform 3 (identifier: Q5VV43-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.
Isoform 4 (identifier: Q5VV43-4)

The sequence of this isoform differs from the canonical sequence as follows:
     953-1013: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 10721052Dyslexia-associated protein KIAA0319
PRO_0000042946

Regions

Topological domain21 – 955935Extracellular Potential
Transmembrane956 – 97621Helical; Potential
Topological domain977 – 107296Cytoplasmic Potential
Domain21 – 9979MANSC
Domain341 – 42787PKD 1
Domain435 – 52490PKD 2
Domain530 – 62091PKD 3
Domain621 – 71494PKD 4
Domain720 – 81192PKD 5
Motif995 – 9984Endocytosis signal

Amino acid modifications

Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation2621N-linked (GlcNAc...) Potential
Glycosylation3941N-linked (GlcNAc...) Potential
Glycosylation4211N-linked (GlcNAc...) Potential
Glycosylation4981N-linked (GlcNAc...) Potential
Glycosylation5131N-linked (GlcNAc...) Potential
Glycosylation5361N-linked (GlcNAc...) Potential
Glycosylation5511N-linked (GlcNAc...) Potential
Glycosylation7331N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 4545Missing in isoform 3.
VSP_036234
Alternative sequence1 – 1919MAPPT…VTIAG → MTRLGWPSPC in isoform 2.
VSP_036235
Alternative sequence953 – 101361Missing in isoform 4.
VSP_044971
Natural variant1421T → P. Ref.1 Ref.3 Ref.5
Corresponds to variant rs4576240 [ dbSNP | Ensembl ].
VAR_023837
Natural variant3111A → T May be associated with susceptibility to dyslexia. Ref.3 Ref.5 Ref.14
Corresponds to variant rs4504469 [ dbSNP | Ensembl ].
VAR_023838
Natural variant5671G → S.
Corresponds to variant rs2744559 [ dbSNP | Ensembl ].
VAR_049505
Natural variant7731S → G.
Corresponds to variant rs2744550 [ dbSNP | Ensembl ].
VAR_049506
Natural variant7741V → A.
Corresponds to variant rs2817191 [ dbSNP | Ensembl ].
VAR_049507
Natural variant9191G → A.
Corresponds to variant rs10946705 [ dbSNP | Ensembl ].
VAR_034032
Natural variant10131Y → C.
Corresponds to variant rs807534 [ dbSNP | Ensembl ].
VAR_049508

Experimental info

Mutagenesis9951Y → A: Loss of interaction with AP2M1 and impaired endocytosis. Ref.10
Sequence conflict971R → S in BAG58068. Ref.3
Sequence conflict1571S → A in BAA20777. Ref.1
Sequence conflict1571S → A in AAI52461. Ref.5
Sequence conflict2561L → H in BAG59087. Ref.3
Sequence conflict9261L → I in AAI44629. Ref.5

Secondary structure

..................... 1072
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 94F33B03E7FE8C0F

FASTA1,072117,763
        10         20         30         40         50         60 
MAPPTGVLSS LLLLVTIAGC ARKQCSEGRT YSNAVISPNL ETTRIMRVSH TFPVVDCTAA 

        70         80         90        100        110        120 
CCDLSSCDLA WWFEGRCYLV SCPHKENCEP KKMGPIRSYL TFVLRPVQRP AQLLDYGDMM 

       130        140        150        160        170        180 
LNRGSPSGIW GDSPEDIRKD LTFLGKDWGL EEMSEYSDDY RELEKDLLQP SGKQEPRGSA 

       190        200        210        220        230        240 
EYTDWGLLPG SEGAFNSSVG DSPAVPAETQ QDPELHYLNE SASTPAPKLP ERSVLLPLPT 

       250        260        270        280        290        300 
TPSSGEVLEK EKASQLQEQS SNSSGKEVLM PSHSLPPASL ELSSVTVEKS PVLTVTPGST 

       310        320        330        340        350        360 
EHSIPTPPTS AAPSESTPSE LPISPTTAPR TVKELTVSAG DNLIITLPDN EVELKAFVAP 

       370        380        390        400        410        420 
APPVETTYNY EWNLISHPTD YQGEIKQGHK QTLNLSQLSV GLYVFKVTVS SENAFGEGFV 

       430        440        450        460        470        480 
NVTVKPARRV NLPPVAVVSP QLQELTLPLT SALIDGSQST DDTEIVSYHW EEINGPFIEE 

       490        500        510        520        530        540 
KTSVDSPVLR LSNLDPGNYS FRLTVTDSDG ATNSTTAALI VNNAVDYPPV ANAGPNHTIT 

       550        560        570        580        590        600 
LPQNSITLNG NQSSDDHQIV LYEWSLGPGS EGKHVVMQGV QTPYLHLSAM QEGDYTFQLK 

       610        620        630        640        650        660 
VTDSSRQQST AVVTVIVQPE NNRPPVAVAG PDKELIFPVE SATLDGSSSS DDHGIVFYHW 

       670        680        690        700        710        720 
EHVRGPSAVE MENIDKAIAT VTGLQVGTYH FRLTVKDQQG LSSTSTLTVA VKKENNSPPR 

       730        740        750        760        770        780 
ARAGGRHVLV LPNNSITLDG SRSTDDQRIV SYLWIRDGQS PAAGDVIDGS DHSVALQLTN 

       790        800        810        820        830        840 
LVEGVYTFHL RVTDSQGASD TDTATVEVQP DPRKSGLVEL TLQVGVGQLT EQRKDTLVRQ 

       850        860        870        880        890        900 
LAVLLNVLDS DIKVQKIRAH SDLSTVIVFY VQSRPPFKVL KAAEVARNLH MRLSKEKADF 

       910        920        930        940        950        960 
LLFKVLRVDT AGCLLKCSGH GHCDPLTKRC ICSHLWMENL IQRYIWDGES NCEWSIFYVT 

       970        980        990       1000       1010       1020 
VLAFTLIVLT GGFTWLCICC CKRQKRTKIR KKTKYTILDN MDEQERMELR PKYGIKHRST 

      1030       1040       1050       1060       1070 
EHNSSLMVSE SEFDSDQDTI FSREKMERGN PKVSMNGSIR NGASFSYCSK DR 

« Hide

Isoform 2 [UniParc].

Checksum: 144EC867C3FD7CD5
Show »

FASTA1,063117,057
Isoform 3 [UniParc].

Checksum: 27D81BD05C976D80
Show »

FASTA1,027113,047
Isoform 4 [UniParc].

Checksum: 6B875CD6ED56D253
Show »

FASTA1,011110,370

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PRO-142.
Tissue: Brain.
[2]Ohara O., Nagase T., Kikuno R., Nomura N.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), VARIANTS PRO-142 AND THR-311.
Tissue: Brain and Thalamus.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS PRO-142 AND THR-311.
Tissue: Brain.
[6]"A transcription map of the 6p22.3 reading disability locus identifying candidate genes."
Londin E.R., Meng H., Gruen J.R.
BMC Genomics 4:25-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"The chromosome 6p22 haplotype associated with dyslexia reduces the expression of KIAA0319, a novel gene involved in neuronal migration."
Paracchini S., Thomas A., Castro S., Lai C., Paramasivam M., Wang Y., Keating B.J., Taylor J.M., Hacking D.F., Scerri T., Francks C., Richardson A.J., Wade-Martins R., Stein J.F., Knight J.C., Copp A.J., Loturco J., Monaco A.P.
Hum. Mol. Genet. 15:1659-1666(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN DYX2, DEVELOPMENTAL STAGE.
[8]"Alternative splicing in the dyslexia-associated gene KIAA0319."
Velayos-Baeza A., Toma C., da Roza S., Paracchini S., Monaco A.P.
Mamm. Genome 18:627-634(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[9]"The dyslexia-associated gene KIAA0319 encodes highly N- and O-glycosylated plasma membrane and secreted isoforms."
Velayos-Baeza A., Toma C., Paracchini S., Monaco A.P.
Hum. Mol. Genet. 17:859-871(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, SUBUNIT.
[10]"The dyslexia-associated protein KIAA0319 interacts with adaptor protein 2 and follows the classical clathrin-mediated endocytosis pathway."
Levecque C., Velayos-Baeza A., Holloway Z.G., Monaco A.P.
Am. J. Physiol. 297:C160-C168(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-995, ENDOCYTOSIS SIGNAL, INTERACTION WITH AP2M1.
[11]"The effect of variation in expression of the candidate dyslexia susceptibility gene homolog Kiaa0319 on neuronal migration and dendritic morphology in the rat."
Peschansky V.J., Burbridge T.J., Volz A.J., Fiondella C., Wissner-Gross Z., Galaburda A.M., Lo Turco J.J., Rosen G.D.
Cereb. Cortex 20:884-897(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"The dyslexia-associated KIAA0319 protein undergoes proteolytic processing with {gamma}-secretase-independent intramembrane cleavage."
Velayos-Baeza A., Levecque C., Kobayashi K., Holloway Z.G., Monaco A.P.
J. Biol. Chem. 285:40148-40162(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[13]"Solution structure of the PKD domain (329-428) from human KIAA0319."
RIKEN structural genomics initiative (RSGI)
Submitted (JUL-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 324-428.
[14]"Strong evidence that KIAA0319 on chromosome 6p is a susceptibility gene for developmental dyslexia."
Cope N., Harold D., Hill G., Moskvina V., Stevenson J., Holmans P., Owen M.J., O'Donovan M.C., Williams J.
Am. J. Hum. Genet. 76:581-591(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-311.
+Additional computationally mapped references.

Web resources

Protein Spotlight

The twisted way of things - Issue 125 of January 2011

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB002317 mRNA. Translation: BAA20777.2. Different initiation.
AK295008 mRNA. Translation: BAG58068.1.
AK296310 mRNA. Translation: BAG59008.1.
AK296426 mRNA. Translation: BAG59087.1.
AL512385, AL031230 Genomic DNA. Translation: CAH71730.1.
AL031230, AL512385 Genomic DNA. Translation: CAI22601.1.
BC140821 mRNA. Translation: AAI40822.1.
BC144628 mRNA. Translation: AAI44629.1.
BC152460 mRNA. Translation: AAI52461.1.
RefSeqNP_001161846.1. NM_001168374.1.
NP_001161847.1. NM_001168375.1.
NP_001161848.1. NM_001168376.1.
NP_001161849.1. NM_001168377.1.
NP_055624.2. NM_014809.3.
UniGeneHs.26441.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E7MNMR-A329-428[»]
ProteinModelPortalQ5VV43.
SMRQ5VV43. Positions 324-428, 443-521, 531-621, 627-811.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115190. 2 interactions.
IntActQ5VV43. 3 interactions.
STRING9606.ENSP00000367459.

PTM databases

PhosphoSiteQ5VV43.

Polymorphism databases

DMDM74747200.

Proteomic databases

PaxDbQ5VV43.
PRIDEQ5VV43.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378214; ENSP00000367459; ENSG00000137261. [Q5VV43-1]
ENST00000430948; ENSP00000401086; ENSG00000137261. [Q5VV43-3]
ENST00000535378; ENSP00000442403; ENSG00000137261. [Q5VV43-2]
ENST00000537886; ENSP00000439700; ENSG00000137261. [Q5VV43-4]
ENST00000543707; ENSP00000437656; ENSG00000137261. [Q5VV43-1]
GeneID9856.
KEGGhsa:9856.
UCSCuc003neh.1. human. [Q5VV43-1]
uc011djq.1. human. [Q5VV43-2]

Organism-specific databases

CTD9856.
GeneCardsGC06M024493.
HGNCHGNC:21580. KIAA0319.
HPAHPA015607.
MIM600202. phenotype.
609269. gene.
neXtProtNX_Q5VV43.
PharmGKBPA134936721.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000043880.
HOVERGENHBG057130.
InParanoidQ5VV43.
OMANYEWSLI.
OrthoDBEOG79PJNJ.
PhylomeDBQ5VV43.
TreeFamTF323356.

Gene expression databases

BgeeQ5VV43.
CleanExHS_KIAA0319.
GenevestigatorQ5VV43.

Family and domain databases

Gene3D2.60.40.670. 3 hits.
InterProIPR003961. Fibronectin_type3.
IPR013980. MANSC.
IPR011106. MANSC_N.
IPR022409. PKD/Chitinase_dom.
IPR002859. PKD/REJ-like.
IPR000601. PKD_dom.
[Graphical view]
PfamPF02010. REJ. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 4 hits.
SM00765. MANEC. 1 hit.
SM00089. PKD. 5 hits.
[Graphical view]
SUPFAMSSF49299. SSF49299. 4 hits.
PROSITEPS50986. MANSC. 1 hit.
PS50093. PKD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKIAA0319. human.
EvolutionaryTraceQ5VV43.
GeneWikiKIAA0319.
GenomeRNAi9856.
NextBio37146.
SOURCESearch...

Entry information

Entry nameK0319_HUMAN
AccessionPrimary (citable) accession number: Q5VV43
Secondary accession number(s): A7MD37 expand/collapse secondary AC list , B2RTU7, B4DHA7, B4DK75, B7ZML3, F5H123, Q9UJC8, Q9Y4G7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: December 7, 2004
Last modified: April 16, 2014
This is version 100 of the entry and version 1 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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 6

Human chromosome 6: entries, gene names and cross-references to MIM