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Reviewed, UniProtKB/Swiss-Prot Q9BWU0 (NADAP_HUMAN)

Last modified July 7, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Kanadaptin
Alternative name(s):
    Kidney anion exchanger adapter protein
    Solute carrier family 4 anion exchanger member 1 adapter protein
    Human lung cancer oncogene 3 protein
      Short name=HLC-3
Gene names
Name: SLC4A1AP
ORF Names: HLC3
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length796 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Subcellular location

Nucleus. Cytoplasm. Note: Mainly nuclear. Small amounts are found in the cytoplasm. Ref.1

Tissue specificity

Ubiquitously expressed. Ref.1

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.8 Ref.9 Ref.10

Sequence similarities

Contains 1 FHA domain.

Caution

Ref.1 initially suggested a role in targeting SLC4A1 (kidney anion exchanger 1) to the plasma membrane; it does not seem to do so as it does not interact with SLC4A1 and has no effect on SLC4A1 trafficking.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondouble-stranded RNA binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ILKQ134185EBI-1999704,EBI-747644

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 796796Kanadaptin
PRO_0000076268

Regions

Domain189 – 24961FHA
Coiled coil497 – 53034 Potential
Compositional bias644 – 71572Glu-rich

Amino acid modifications

Modified residue3121Phosphoserine Ref.8 Ref.10
Modified residue4661Phosphoserine Ref.7 Ref.8 Ref.10
Modified residue5241Phosphoserine Ref.9
Modified residue5301Phosphoserine Ref.7 Ref.10
Modified residue5321Phosphoserine Ref.9
Modified residue7091Phosphoserine Ref.9
Modified residue7121Phosphoserine Ref.9

Natural variations

Natural variant1391P → T: dbSNP rs9678851. Ref.2 Ref.5
VAR_024748
Natural variant1811R → C: dbSNP rs9679004.
VAR_051219

Experimental info

Sequence conflict111 – 1155SNSGE → PIAKP in AAN12269. Ref.6
Sequence conflict3091G → R in AAK29177. Ref.2
Sequence conflict3591Q → R in AAH98358. Ref.5
Sequence conflict3731A → V in AAK29177. Ref.2
Sequence conflict4441L → I in AAN12269. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9BWU0-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: EE0F560648DA39EF

FASTA79688,814
        10         20         30         40         50         60 
MLAPLRNAPG REGATSPSPP TDATGSLGEW DVDRNVKTEG WVSKERISKL HRLRMADILS 

        70         80         90        100        110        120 
QSETLASQDL SGDFKKPALP VSPAARSKAP ASSSSNPEEV QKEGPTALQD SNSGEPDIPP 

       130        140        150        160        170        180 
PQPDCGDFRS LQEEQSRPPT AVSSPGGPAR APPYQEPPWG GPATAPYSLE TLKGGTILGT 

       190        200        210        220        230        240 
RSLKGTSYCL FGRLSGCDVC LEHPSVSRYH AVLQHRASGP DGECDSNGPG FYLYDLGSTH 

       250        260        270        280        290        300 
GTFLNKTRIP PRTYCRVHVG HVVRFGGSTR LFILQGPEED REAESELTVT QLKELRKQQQ 

       310        320        330        340        350        360 
ILLEKKMLGE DSDEEEEMDT SERKINAGSQ DDEMGCTWGM GEDAVEDDAE ENPIVLEFQQ 

       370        380        390        400        410        420 
EREAFYIKDP KKALQGFFDR EGEELEYEFD EQGHSTWLCR VRLPVDDSTG KQLVAEAIHS 

       430        440        450        460        470        480 
GKKKEAMIQC SLEACRILDT LGLLRQEAVS RKRKAKNWED EDFYDSDDDT FLDRTGLIEK 

       490        500        510        520        530        540 
KRLNRMKKAG KIDEKPETFE SLVAKLNDAE RELSEISERL KASSQVLSES PSQDSLDAFM 

       550        560        570        580        590        600 
SEMKSGSTLD GVSRKKLHLR TFELRKEQQR LKGLIKIVKP AEIPELKKTE TQTTGAENKA 

       610        620        630        640        650        660 
KKLTLPLFGA MKGGSKFKLK TGTVGKLPPK RPELPPTLMR MKDEPEVEEE EEEEEEEEKE 

       670        680        690        700        710        720 
KEEHEKKKLE DGSLSRPQPE IEPEAAVQEM RPPTDLTHFK ETQTHENMSQ LSEEEQNKDY 

       730        740        750        760        770        780 
QDCSKTTSLC AGPSASKNEY EKSRGELKKK KTPGPGKLPP TLSSKYPEDD PDYCVWVPPE 

       790 
GQSGDGRTHL NDKYGY 

« Hide

References

« Hide 'large scale' references
[1]"Human kanadaptin and kidney anion exchanger 1 (kAE1) do not interact in transfected HEK 293 cells."
Kittanakom S., Keskanokwong T., Akkarapatumwong V., Yenchitsomanus P.-T., Reithmeier R.A.F.
Mol. Membr. Biol. 21:395-402(2004) [PubMed: 15764369] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-139.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-139.
[6]"Identification of a new oncogene in human lung cancer."
Kim J.W.
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-796.
[7]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466 AND SER-530, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND SER-466, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524; SER-532; SER-709 AND SER-712, MASS SPECTROMETRY.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; SER-466 AND SER-530, MASS SPECTROMETRY.
[11]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Web resources

Wikipedia

Band 3 entry

Cross-references

Sequence databases

AY028435 mRNA. Translation: AAK29177.1.
AK001486 mRNA. Translation: BAA91718.1.
AC074091 Genomic DNA. Translation: AAX93203.1.
CH471053 Genomic DNA. Translation: EAX00555.1.
BC098302 mRNA. Translation: AAH98302.1.
BC098358 mRNA. Translation: AAH98358.1.
BC099711 mRNA. Translation: AAH99711.1.
BC099739 mRNA. Translation: AAH99739.1.
AY117688 mRNA. Translation: AAN12269.1. Different initiation.
IPIIPI00306749.
RefSeqNP_060628.2.
UniGeneHs.306000

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9BWU0. 2 interactions.

PTM databases

PhosphoSiteQ9BWU0.

Proteomic databases

PRIDEQ9BWU0.

Genome annotation databases

EnsemblENSG00000163798. Homo sapiens. [Contig view]
GeneID22950.
KEGGhsa:22950.
UCSCuc002rlk.2. human.

Organism-specific databases

GeneCardsGC02P027797.
H-InvDBHIX0001931.
HGNCHGNC:13813. SLC4A1AP.
MIM602655. gene.
PharmGKBPA37811.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9BWU0.
OMAQ9BWU0. PPTLMRM.

Gene expression databases

ArrayExpressQ9BWU0.
BgeeQ9BWU0.
CleanExHS_SLC4A1AP.
GermOnlineENSG00000163798. Homo sapiens.

Family and domain databases

InterProIPR001159. Ds-RNA_bd.
IPR000253. FHA.
[Graphical view]
Gene3DG3DSA:2.60.200.20. FHA. 1 hit.
PfamPF00035. dsrm. 1 hit.
PF00498. FHA. 1 hit.
[Graphical view]
SMARTSM00358. DSRM. 1 hit.
SM00240. FHA. 1 hit.
[Graphical view]
PROSITEPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio43719.
SOURCESearch...

Entry information

Entry nameNADAP_HUMAN
AccessionPrimary (citable) accession number: Q9BWU0
Secondary accession number(s): A6NJ39 expand/collapse secondary AC list , Q4KMT1, Q4KMX0, Q7Z5Q9, Q9NVN2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 1, 2001
Last modified: July 7, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents