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Q13303

- KCAB2_HUMAN

UniProt

Q13303 - KCAB2_HUMAN

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Protein
Voltage-gated potassium channel subunit beta-2
Gene
KCNAB2, KCNA2B, KCNK2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters functional properties of Kv1.4.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631NADP
Binding sitei85 – 851NADP
Binding sitei90 – 901NADP
Binding sitei214 – 2141NADP
Binding sitei254 – 2541NADP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi56 – 572NADP
Nucleotide bindingi188 – 1892NADP
Nucleotide bindingi243 – 2486NADP
Nucleotide bindingi323 – 3297NADP

GO - Molecular functioni

  1. potassium channel regulator activity Source: ProtInc
  2. voltage-gated potassium channel activity Source: InterPro

GO - Biological processi

  1. protein heterooligomerization Source: Ensembl
  2. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

NADP, Potassium

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-2009-MONOMER.
ReactomeiREACT_75770. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-gated potassium channel subunit beta-2
Alternative name(s):
K(+) channel subunit beta-2
Kv-beta-2
Short name:
hKvbeta2
Gene namesi
Name:KCNAB2
Synonyms:KCNA2B, KCNK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6229. KCNAB2.

Subcellular locationi

Cytoplasm Reviewed prediction

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. integral component of membrane Source: InterPro
  3. juxtaparanode region of axon Source: BHF-UCL
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

Orphaneti1606. 1p36 deletion syndrome.
PharmGKBiPA373.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Voltage-gated potassium channel subunit beta-2
PRO_0000148746Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine1 Publication
Modified residuei124 – 1241N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated by PRKCZ; may be regulated by incorporation in a complex composed of PRKCZ and SQSTM1 By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13303.
PaxDbiQ13303.
PRIDEiQ13303.

PTM databases

PhosphoSiteiQ13303.

Expressioni

Gene expression databases

ArrayExpressiQ13303.
BgeeiQ13303.
CleanExiHS_KCNAB2.
HS_KCNK2.
GenevestigatoriQ13303.

Organism-specific databases

HPAiCAB001975.
HPA030185.

Interactioni

Subunit structurei

Forms heteromultimeric complex with alpha subunits. Forms a ternary complex with SQSTM1 and PRKCZ By similarity.

Protein-protein interaction databases

BioGridi114086. 10 interactions.
IntActiQ13303. 1 interaction.
MINTiMINT-2865320.
STRINGi9606.ENSP00000164247.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 424
Beta strandi48 – 558
Helixi59 – 635
Helixi66 – 7813
Beta strandi83 – 853
Helixi90 – 934
Helixi94 – 10613
Helixi110 – 1123
Beta strandi114 – 1218
Helixi126 – 1283
Beta strandi129 – 1313
Helixi133 – 14715
Beta strandi152 – 1598
Helixi166 – 17813
Beta strandi181 – 1899
Helixi192 – 20514
Beta strandi212 – 2165
Helixi223 – 2264
Helixi228 – 2369
Beta strandi239 – 2435
Helixi247 – 2526
Turni253 – 2575
Helixi264 – 2663
Helixi271 – 2777
Helixi280 – 29920
Helixi303 – 31311
Beta strandi317 – 3226
Helixi327 – 3348
Helixi336 – 3394
Helixi340 – 3423
Helixi345 – 35511

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZSXX-ray1.90A39-360[»]
ProteinModelPortaliQ13303.
SMRiQ13303. Positions 37-359.

Miscellaneous databases

EvolutionaryTraceiQ13303.

Family & Domainsi

Domaini

Alteration of functional properties of alpha subunit is mediated through N-terminal domain of beta subunit Inferred.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0667.
HOVERGENiHBG052216.
KOiK04883.
OMAiAIGFIEV.
PhylomeDBiQ13303.
TreeFamiTF324563.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR005983. K_chnl_volt-dep_bsu_KCNAB.
IPR005399. K_chnl_volt-dep_bsu_KCNAB-rel.
IPR005401. K_chnl_volt-dep_bsu_KCNAB2.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR01579. KCNAB2CHANEL.
PR01577. KCNABCHANNEL.
SUPFAMiSSF51430. SSF51430. 1 hit.
TIGRFAMsiTIGR01293. Kv_beta. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13303-1) [UniParc]FASTAAdd to Basket

Also known as: KvB2.1

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.

« Hide

MYPESTTGSP ARLSLRQTGS PGMIYSTRYG SPKRQLQFYR NLGKSGLRVS    50
CLGLGTWVTF GGQITDEMAE QLMTLAYDNG INLFDTAEVY AAGKAEVVLG 100
NIIKKKGWRR SSLVITTKIF WGGKAETERG LSRKHIIEGL KASLERLQLE 150
YVDVVFANRP DPNTPMEETV RAMTHVINQG MAMYWGTSRW SSMEIMEAYS 200
VARQFNLTPP ICEQAEYHMF QREKVEVQLP ELFHKIGVGA MTWSPLACGI 250
VSGKYDSGIP PYSRASLKGY QWLKDKILSE EGRRQQAKLK ELQAIAERLG 300
CTLPQLAIAW CLRNEGVSSV LLGASNADQL MENIGAIQVL PKLSSSIIHE 350
IDSILGNKPY SKKDYRS 367
Length:367
Mass (Da):41,000
Last modified:January 1, 1998 - v2
Checksum:i91A673F8992140DA
GO
Isoform 2 (identifier: Q13303-2) [UniParc]FASTAAdd to Basket

Also known as: KvB2.2

The sequence of this isoform differs from the canonical sequence as follows:
     26-39: Missing.

Show »
Length:353
Mass (Da):39,287
Checksum:i7D59C8203AC5606F
GO
Isoform 3 (identifier: Q13303-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MYPESTTGSP...YGSPKRQLQF → MLSMTYSESL...GCTAQRTGMK
     167-167: E → EGDPFSSSKSRTFIIE

Show »
Length:415
Mass (Da):46,527
Checksum:i3AD46E32E4B200AF
GO
Isoform 4 (identifier: Q13303-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-67: Missing.

Show »
Length:300
Mass (Da):33,657
Checksum:i3ADDAAE15216B737
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti88 – 881E → K.
Corresponds to variant rs2229003 [ dbSNP | Ensembl ].
VAR_048747

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6767Missing in isoform 4.
VSP_044311Add
BLAST
Alternative sequencei1 – 3838MYPES…RQLQF → MLSMTYSESLRSVSSRCHSE WALHPVRQTDTLELQRLREV RAAAQARNMESFLRMHGLSL DGCTAQRTGMK in isoform 3.
VSP_041189Add
BLAST
Alternative sequencei26 – 3914Missing in isoform 2.
VSP_001054Add
BLAST
Alternative sequencei167 – 1671E → EGDPFSSSKSRTFIIE in isoform 3.
VSP_041190

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33429 mRNA. Translation: AAC50955.1.
AF029749 mRNA. Translation: AAB84170.1.
AF044253 mRNA. Translation: AAB99859.1.
AK124696 mRNA. Translation: BAG54071.1.
AK131252 mRNA. Translation: BAD18431.1.
AK289819 mRNA. Translation: BAF82508.1.
AK315858 mRNA. Translation: BAF98749.1.
AL035406 Genomic DNA. Translation: CAC08512.1.
AL035406 Genomic DNA. Translation: CAI19885.1.
BC126424 mRNA. Translation: AAI26425.1.
BC130413 mRNA. Translation: AAI30414.1.
CCDSiCCDS55.1. [Q13303-1]
CCDS55570.1. [Q13303-3]
CCDS55571.1. [Q13303-4]
CCDS56.1. [Q13303-2]
PIRiS66502.
RefSeqiNP_001186789.1. NM_001199860.1. [Q13303-1]
NP_001186790.1. NM_001199861.1. [Q13303-1]
NP_001186791.1. NM_001199862.1. [Q13303-3]
NP_001186792.1. NM_001199863.1. [Q13303-4]
NP_003627.1. NM_003636.3. [Q13303-1]
NP_742128.1. NM_172130.2. [Q13303-2]
XP_005263571.1. XM_005263514.1. [Q13303-2]
UniGeneiHs.440497.
Hs.735032.

Genome annotation databases

EnsembliENST00000164247; ENSP00000164247; ENSG00000069424. [Q13303-1]
ENST00000341524; ENSP00000340824; ENSG00000069424. [Q13303-1]
ENST00000352527; ENSP00000318772; ENSG00000069424. [Q13303-2]
ENST00000378083; ENSP00000367323; ENSG00000069424. [Q13303-3]
ENST00000378092; ENSP00000367332; ENSG00000069424. [Q13303-2]
ENST00000378097; ENSP00000367337; ENSG00000069424. [Q13303-1]
ENST00000458166; ENSP00000396167; ENSG00000069424. [Q13303-4]
GeneIDi8514.
KEGGihsa:8514.
UCSCiuc001alv.2. human. [Q13303-1]
uc001alw.2. human. [Q13303-2]
uc001aly.2. human. [Q13303-3]

Polymorphism databases

DMDMi18202496.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33429 mRNA. Translation: AAC50955.1 .
AF029749 mRNA. Translation: AAB84170.1 .
AF044253 mRNA. Translation: AAB99859.1 .
AK124696 mRNA. Translation: BAG54071.1 .
AK131252 mRNA. Translation: BAD18431.1 .
AK289819 mRNA. Translation: BAF82508.1 .
AK315858 mRNA. Translation: BAF98749.1 .
AL035406 Genomic DNA. Translation: CAC08512.1 .
AL035406 Genomic DNA. Translation: CAI19885.1 .
BC126424 mRNA. Translation: AAI26425.1 .
BC130413 mRNA. Translation: AAI30414.1 .
CCDSi CCDS55.1. [Q13303-1 ]
CCDS55570.1. [Q13303-3 ]
CCDS55571.1. [Q13303-4 ]
CCDS56.1. [Q13303-2 ]
PIRi S66502.
RefSeqi NP_001186789.1. NM_001199860.1. [Q13303-1 ]
NP_001186790.1. NM_001199861.1. [Q13303-1 ]
NP_001186791.1. NM_001199862.1. [Q13303-3 ]
NP_001186792.1. NM_001199863.1. [Q13303-4 ]
NP_003627.1. NM_003636.3. [Q13303-1 ]
NP_742128.1. NM_172130.2. [Q13303-2 ]
XP_005263571.1. XM_005263514.1. [Q13303-2 ]
UniGenei Hs.440497.
Hs.735032.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZSX X-ray 1.90 A 39-360 [» ]
ProteinModelPortali Q13303.
SMRi Q13303. Positions 37-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114086. 10 interactions.
IntActi Q13303. 1 interaction.
MINTi MINT-2865320.
STRINGi 9606.ENSP00000164247.

PTM databases

PhosphoSitei Q13303.

Polymorphism databases

DMDMi 18202496.

Proteomic databases

MaxQBi Q13303.
PaxDbi Q13303.
PRIDEi Q13303.

Protocols and materials databases

DNASUi 8514.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000164247 ; ENSP00000164247 ; ENSG00000069424 . [Q13303-1 ]
ENST00000341524 ; ENSP00000340824 ; ENSG00000069424 . [Q13303-1 ]
ENST00000352527 ; ENSP00000318772 ; ENSG00000069424 . [Q13303-2 ]
ENST00000378083 ; ENSP00000367323 ; ENSG00000069424 . [Q13303-3 ]
ENST00000378092 ; ENSP00000367332 ; ENSG00000069424 . [Q13303-2 ]
ENST00000378097 ; ENSP00000367337 ; ENSG00000069424 . [Q13303-1 ]
ENST00000458166 ; ENSP00000396167 ; ENSG00000069424 . [Q13303-4 ]
GeneIDi 8514.
KEGGi hsa:8514.
UCSCi uc001alv.2. human. [Q13303-1 ]
uc001alw.2. human. [Q13303-2 ]
uc001aly.2. human. [Q13303-3 ]

Organism-specific databases

CTDi 8514.
GeneCardsi GC01P006020.
HGNCi HGNC:6229. KCNAB2.
HPAi CAB001975.
HPA030185.
MIMi 601142. gene.
neXtProti NX_Q13303.
Orphaneti 1606. 1p36 deletion syndrome.
PharmGKBi PA373.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0667.
HOVERGENi HBG052216.
KOi K04883.
OMAi AIGFIEV.
PhylomeDBi Q13303.
TreeFami TF324563.

Enzyme and pathway databases

BioCyci RETL1328306-WGS:GSTH-2009-MONOMER.
Reactomei REACT_75770. Voltage gated Potassium channels.

Miscellaneous databases

ChiTaRSi KCNAB2. human.
EvolutionaryTracei Q13303.
GeneWikii KCNAB2.
GenomeRNAii 8514.
NextBioi 31868.
PROi Q13303.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13303.
Bgeei Q13303.
CleanExi HS_KCNAB2.
HS_KCNK2.
Genevestigatori Q13303.

Family and domain databases

Gene3Di 3.20.20.100. 1 hit.
InterProi IPR001395. Aldo/ket_red.
IPR005983. K_chnl_volt-dep_bsu_KCNAB.
IPR005399. K_chnl_volt-dep_bsu_KCNAB-rel.
IPR005401. K_chnl_volt-dep_bsu_KCNAB2.
IPR023210. NADP_OxRdtase_dom.
[Graphical view ]
PANTHERi PTHR11732. PTHR11732. 1 hit.
Pfami PF00248. Aldo_ket_red. 1 hit.
[Graphical view ]
PRINTSi PR01579. KCNAB2CHANEL.
PR01577. KCNABCHANNEL.
SUPFAMi SSF51430. SSF51430. 1 hit.
TIGRFAMsi TIGR01293. Kv_beta. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Alternative splicing of the human Shaker K+ channel beta 1 gene and functional expression of the beta 2 gene product."
    Mccormack K., McCormack T., Tanouye M.A., Rudy B., Stuehmer W.
    FEBS Lett. 370:32-36(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Tissue: Hippocampus.
  2. McCormack K.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Rae J.L., Shepard A.R.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Lens epithelium.
  4. "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.
    , 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; 3 AND 4).
    Tissue: Amygdala, Brain and Hippocampus.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Brain.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Crystal structure of human potassium channel Kv beta-subunit (KCNAB2)."
    Structural genomics consortium (SGC)
    Submitted (JUN-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 36-360 IN COMPLEX WITH NADP.

Entry informationi

Entry nameiKCAB2_HUMAN
AccessioniPrimary (citable) accession number: Q13303
Secondary accession number(s): A0AVM9
, A8K1A4, B0AZR7, O43659, Q5TG82, Q5TG83, Q6ZNE4, Q99411
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 141 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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