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Q00005

- 2ABB_HUMAN

UniProt

Q00005 - 2ABB_HUMAN

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Protein

Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform

Gene

PPP2R2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. Within the PP2A holoenzyme complex, isoform 2 is required to promote proapoptotic activity (By similarity). Isoform 2 regulates neuronal survival through the mitochondrial fission and fusion balance (By similarity).By similarity

GO - Molecular functioni

  1. protein phosphatase type 2A regulator activity Source: ProtInc

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. regulation of catalytic activity Source: GOC
  3. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

SignaLinkiQ00005.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
Alternative name(s):
PP2A subunit B isoform B55-beta
PP2A subunit B isoform PR55-beta
PP2A subunit B isoform R2-beta
PP2A subunit B isoform beta
Gene namesi
Name:PPP2R2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:9305. PPP2R2B.

Subcellular locationi

Isoform 1 : Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Membrane By similarity
Isoform 2 : Cytoplasm By similarity. Mitochondrion By similarity. Mitochondrion outer membrane By similarity
Note: Under basal conditions, localizes to both cytosolic and mitochondrial compartments. Relocalizes from the cytosolic to the mitochondrial compartment during apoptosis. Its targeting to the outer mitochondrial membrane (OMM) involves an association with import receptors of the TOM complex and is required to promote proapoptotic activity (By similarity).By similarity

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB-KW
  2. mitochondrial outer membrane Source: UniProtKB
  3. mitochondrion Source: UniProtKB
  4. protein phosphatase type 2A complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia 12 (SCA12) [MIM:604326]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA12 is an autosomal dominant cerebellar ataxia (ADCA).1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

MIMi604326. phenotype.
Orphaneti98762. Spinocerebellar ataxia type 12.
PharmGKBiPA33669.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoformPRO_0000071421Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei275 – 2751PhosphoserineBy similarity
Modified residuei295 – 2951PhosphotyrosineBy similarity
Modified residuei298 – 2981PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ00005.
PRIDEiQ00005.

PTM databases

PhosphoSiteiQ00005.

Expressioni

Tissue specificityi

Brain.

Gene expression databases

BgeeiQ00005.
CleanExiHS_PPP2R2B.
ExpressionAtlasiQ00005. baseline and differential.
GenevestigatoriQ00005.

Organism-specific databases

HPAiHPA038118.

Interactioni

Subunit structurei

PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules.

Binary interactionsi

WithEntry#Exp.IntActNotes
PDPK1O155308EBI-1052159,EBI-717097
PPP2R1AP301535EBI-1052159,EBI-302388
RPS6KB1P234432EBI-1052159,EBI-1775921

Protein-protein interaction databases

BioGridi111513. 45 interactions.
IntActiQ00005. 167 interactions.
MINTiMINT-6631022.
STRINGi9606.ENSP00000336591.

Structurei

3D structure databases

ProteinModelPortaliQ00005.
SMRiQ00005. Positions 23-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati22 – 6140WD 1Add
BLAST
Repeati87 – 12842WD 2Add
BLAST
Repeati171 – 20939WD 3Add
BLAST
Repeati220 – 26041WD 4Add
BLAST
Repeati279 – 31739WD 5Add
BLAST
Repeati334 – 37542WD 6Add
BLAST
Repeati410 – 44233WD 7Add
BLAST

Domaini

The N-terminal 26 residues of isoform 2 constitute a cryptic mitochondrial matrix import signal with critical basic and hydrophobic residues, that is necessary and sufficient for targeting the PP2A holoenzyme to the outer mitochondrial membrane (OMM) and does not affect holoenzyme formation or catalytic activity.By similarity
The last WD repeat of isoform 2 constitutes a mitochondrial stop-transfer domain that confers resistance to the unfolding step process required for import and therefore prevents PPP2R2B matrix translocation and signal sequence cleavage.By similarity

Sequence similaritiesi

Contains 7 WD repeats.Curated

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG5170.
GeneTreeiENSGT00390000006311.
HOVERGENiHBG000012.
InParanoidiQ00005.
KOiK04354.
OMAiRLRDPSM.
OrthoDBiEOG7Q5HCZ.
PhylomeDBiQ00005.
TreeFamiTF105553.

Family and domain databases

Gene3Di2.130.10.10. 3 hits.
InterProiIPR000009. PP2A_PR55.
IPR018067. PP2A_PR55_CS.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR11871. PTHR11871. 1 hit.
PIRSFiPIRSF037309. PP2A_PR55. 1 hit.
PRINTSiPR00600. PP2APR55.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 3 hits.
PROSITEiPS01024. PR55_1. 1 hit.
PS01025. PR55_2. 1 hit.
PS00678. WD_REPEATS_1. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q00005-1) [UniParc]FASTAAdd to Basket

Also known as: Bbeta, Bbeta1

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
MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI
60 70 80 90 100
FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ
110 120 130 140 150
QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV
160 170 180 190 200
PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN
210 220 230 240 250
FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC
260 270 280 290 300
DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD
310 320 330 340 350
YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD
360 370 380 390 400
SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR
410 420 430 440
KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN

Note: Conserved additional ATG codons are found 5' of the putative initiator codon in transcripts supporting isoform 1. They may initiate the translation of upstream short open reading frames altering the expression of that isoform as described in PubMed:1849734.

Length:443
Mass (Da):51,710
Last modified:April 1, 1993 - v1
Checksum:iC383C834B2852B8F
GO
Isoform 2 (identifier: Q00005-2) [UniParc]FASTAAdd to Basket

Also known as: Bbeta2

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MEEDIDTRKINNSFLRDHSYA → MKCFSRYLPYIFRPPNTILSSSCH

Note: Contains a cryptic mitochondrial transit peptide at positions 1-26.By similarity

Show »
Length:446
Mass (Da):52,017
Checksum:iD5BDD8D10F79CF0B
GO
Isoform 3 (identifier: Q00005-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MEEDIDTRKINNSFLRDHSYA → MIPGIGTLTQDTLWCFSQVKGTIEIGT

Show »
Length:449
Mass (Da):52,066
Checksum:i6773D04E733403B1
GO
Isoform 4 (identifier: Q00005-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVLQPSERHYRDWNHRRLGPWCSPTGSPAPLSCETGCGEGSWILVCRLLVPTQVSLLSM

Show »
Length:501
Mass (Da):58,171
Checksum:i3FE3DD278143364A
GO
Isoform 5 (identifier: Q00005-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLLSLPALHLQTSEHHPFFQLPHRRLGPWCSPTGSPAPLSCETGCGEGSWILVCRLLVPTQVSLLSM

Show »
Length:509
Mass (Da):58,897
Checksum:iD47AFC5DD1629FDB
GO
Isoform 6 (identifier: Q00005-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MEEDIDTRKINNSFLRDHSYATE → MNYPDENTYGNK

Show »
Length:432
Mass (Da):50,371
Checksum:iB63F511DEF9670CA
GO
Isoform 7 (identifier: Q00005-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHQPPPASCS...VPTQVSLLSM

Note: No experimental confirmation available.

Show »
Length:549
Mass (Da):62,505
Checksum:iDFACDC3C235450D7
GO

Sequence cautioni

The sequence AAH31790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAG51642.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAG51642.1 differs from that shown. Reason: Erroneous termination at position 116. Translated as Lys.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221T → A in BAH11838. (PubMed:14702039)Curated
Sequence conflicti62 – 621H → N in BI669304. (PubMed:15489334)Curated
Sequence conflicti109 – 1091S → F in BAH12040. (PubMed:14702039)Curated
Sequence conflicti163 – 1631T → S in BI490027. 1 PublicationCurated
Sequence conflicti164 – 1641P → S in BAF82406. (PubMed:14702039)Curated
Sequence conflicti292 – 2921S → R in BAH12040. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361G → V.
Corresponds to variant rs11547494 [ dbSNP | Ensembl ].
VAR_051738

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2323MEEDI…SYATE → MNYPDENTYGNK in isoform 6. 1 PublicationVSP_044923Add
BLAST
Alternative sequencei1 – 2121MEEDI…DHSYA → MKCFSRYLPYIFRPPNTILS SSCH in isoform 2. 1 PublicationVSP_037976Add
BLAST
Alternative sequencei1 – 2121MEEDI…DHSYA → MIPGIGTLTQDTLWCFSQVK GTIEIGT in isoform 3. 1 PublicationVSP_037977Add
BLAST
Alternative sequencei1 – 11M → MVLQPSERHYRDWNHRRLGP WCSPTGSPAPLSCETGCGEG SWILVCRLLVPTQVSLLSM in isoform 4. 1 PublicationVSP_037978
Alternative sequencei1 – 11M → MLLSLPALHLQTSEHHPFFQ LPHRRLGPWCSPTGSPAPLS CETGCGEGSWILVCRLLVPT QVSLLSM in isoform 5. 1 PublicationVSP_037979
Alternative sequencei1 – 11M → MHQPPPASCSSSSSSSSSSC ECARVGVRVSALAPAAAPCP APRQLPYPRLPEPPSRGTST LIPARLGPWCSPTGSPAPLS CETGCGEGSWILVCRLLVPT QVSLLSM in isoform 7. 1 PublicationVSP_045748

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64930 mRNA. Translation: AAA36493.1.
AK056192 mRNA. Translation: BAG51642.1. Sequence problems.
AK289717 mRNA. Translation: BAF82406.1.
AK294659 mRNA. Translation: BAH11838.1.
AK295347 mRNA. Translation: BAH12040.1.
AC008728 Genomic DNA. No translation available.
AC009186 Genomic DNA. No translation available.
AC010251 Genomic DNA. No translation available.
AC011386 Genomic DNA. No translation available.
AC011357 Genomic DNA. No translation available.
AC091919 Genomic DNA. No translation available.
AC091924 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61829.1.
CH471062 Genomic DNA. Translation: EAW61831.1.
CH471062 Genomic DNA. Translation: EAW61832.1.
CH471062 Genomic DNA. Translation: EAW61833.1.
CH471062 Genomic DNA. Translation: EAW61834.1.
CH471062 Genomic DNA. Translation: EAW61835.1.
BC031790 mRNA. Translation: AAH31790.1. Different initiation.
BI490027 mRNA. No translation available.
BI669304 mRNA. No translation available.
CCDSiCCDS4283.1. [Q00005-2]
CCDS4284.2. [Q00005-5]
CCDS43380.1. [Q00005-6]
CCDS64282.1. [Q00005-3]
PIRiB38351.
RefSeqiNP_001258828.1. NM_001271899.1. [Q00005-3]
NP_001258829.1. NM_001271900.1. [Q00005-4]
NP_001258877.1. NM_001271948.1. [Q00005-6]
NP_858060.2. NM_181674.2. [Q00005-5]
NP_858061.2. NM_181675.3. [Q00005-7]
NP_858062.1. NM_181676.2. [Q00005-2]
NP_858063.1. NM_181677.2.
NP_858064.1. NM_181678.2. [Q00005-6]
UniGeneiHs.627618.
Hs.655213.

Genome annotation databases

EnsembliENST00000336640; ENSP00000336591; ENSG00000156475. [Q00005-2]
ENST00000394409; ENSP00000377931; ENSG00000156475. [Q00005-1]
ENST00000394411; ENSP00000377933; ENSG00000156475. [Q00005-1]
ENST00000394413; ENSP00000377935; ENSG00000156475. [Q00005-6]
ENST00000394414; ENSP00000377936; ENSG00000156475. [Q00005-5]
ENST00000453001; ENSP00000398779; ENSG00000156475. [Q00005-6]
ENST00000504198; ENSP00000421396; ENSG00000156475. [Q00005-3]
ENST00000508545; ENSP00000431320; ENSG00000156475. [Q00005-6]
GeneIDi5521.
KEGGihsa:5521.
UCSCiuc003loe.4. human. [Q00005-1]
uc003log.5. human. [Q00005-4]
uc003loh.5. human. [Q00005-5]
uc003loi.5. human. [Q00005-2]
uc003lok.5. human.
uc011dbu.3. human. [Q00005-3]

Polymorphism databases

DMDMi231446.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64930 mRNA. Translation: AAA36493.1 .
AK056192 mRNA. Translation: BAG51642.1 . Sequence problems.
AK289717 mRNA. Translation: BAF82406.1 .
AK294659 mRNA. Translation: BAH11838.1 .
AK295347 mRNA. Translation: BAH12040.1 .
AC008728 Genomic DNA. No translation available.
AC009186 Genomic DNA. No translation available.
AC010251 Genomic DNA. No translation available.
AC011386 Genomic DNA. No translation available.
AC011357 Genomic DNA. No translation available.
AC091919 Genomic DNA. No translation available.
AC091924 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61829.1 .
CH471062 Genomic DNA. Translation: EAW61831.1 .
CH471062 Genomic DNA. Translation: EAW61832.1 .
CH471062 Genomic DNA. Translation: EAW61833.1 .
CH471062 Genomic DNA. Translation: EAW61834.1 .
CH471062 Genomic DNA. Translation: EAW61835.1 .
BC031790 mRNA. Translation: AAH31790.1 . Different initiation.
BI490027 mRNA. No translation available.
BI669304 mRNA. No translation available.
CCDSi CCDS4283.1. [Q00005-2 ]
CCDS4284.2. [Q00005-5 ]
CCDS43380.1. [Q00005-6 ]
CCDS64282.1. [Q00005-3 ]
PIRi B38351.
RefSeqi NP_001258828.1. NM_001271899.1. [Q00005-3 ]
NP_001258829.1. NM_001271900.1. [Q00005-4 ]
NP_001258877.1. NM_001271948.1. [Q00005-6 ]
NP_858060.2. NM_181674.2. [Q00005-5 ]
NP_858061.2. NM_181675.3. [Q00005-7 ]
NP_858062.1. NM_181676.2. [Q00005-2 ]
NP_858063.1. NM_181677.2.
NP_858064.1. NM_181678.2. [Q00005-6 ]
UniGenei Hs.627618.
Hs.655213.

3D structure databases

ProteinModelPortali Q00005.
SMRi Q00005. Positions 23-442.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111513. 45 interactions.
IntActi Q00005. 167 interactions.
MINTi MINT-6631022.
STRINGi 9606.ENSP00000336591.

PTM databases

PhosphoSitei Q00005.

Polymorphism databases

DMDMi 231446.

Proteomic databases

PaxDbi Q00005.
PRIDEi Q00005.

Protocols and materials databases

DNASUi 5521.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336640 ; ENSP00000336591 ; ENSG00000156475 . [Q00005-2 ]
ENST00000394409 ; ENSP00000377931 ; ENSG00000156475 . [Q00005-1 ]
ENST00000394411 ; ENSP00000377933 ; ENSG00000156475 . [Q00005-1 ]
ENST00000394413 ; ENSP00000377935 ; ENSG00000156475 . [Q00005-6 ]
ENST00000394414 ; ENSP00000377936 ; ENSG00000156475 . [Q00005-5 ]
ENST00000453001 ; ENSP00000398779 ; ENSG00000156475 . [Q00005-6 ]
ENST00000504198 ; ENSP00000421396 ; ENSG00000156475 . [Q00005-3 ]
ENST00000508545 ; ENSP00000431320 ; ENSG00000156475 . [Q00005-6 ]
GeneIDi 5521.
KEGGi hsa:5521.
UCSCi uc003loe.4. human. [Q00005-1 ]
uc003log.5. human. [Q00005-4 ]
uc003loh.5. human. [Q00005-5 ]
uc003loi.5. human. [Q00005-2 ]
uc003lok.5. human.
uc011dbu.3. human. [Q00005-3 ]

Organism-specific databases

CTDi 5521.
GeneCardsi GC05M145969.
GeneReviewsi PPP2R2B.
HGNCi HGNC:9305. PPP2R2B.
HPAi HPA038118.
MIMi 604325. gene.
604326. phenotype.
neXtProti NX_Q00005.
Orphaneti 98762. Spinocerebellar ataxia type 12.
PharmGKBi PA33669.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5170.
GeneTreei ENSGT00390000006311.
HOVERGENi HBG000012.
InParanoidi Q00005.
KOi K04354.
OMAi RLRDPSM.
OrthoDBi EOG7Q5HCZ.
PhylomeDBi Q00005.
TreeFami TF105553.

Enzyme and pathway databases

SignaLinki Q00005.

Miscellaneous databases

ChiTaRSi PPP2R2B. human.
GeneWikii PPP2R2B.
GenomeRNAii 5521.
NextBioi 21356.
PROi Q00005.
SOURCEi Search...

Gene expression databases

Bgeei Q00005.
CleanExi HS_PPP2R2B.
ExpressionAtlasi Q00005. baseline and differential.
Genevestigatori Q00005.

Family and domain databases

Gene3Di 2.130.10.10. 3 hits.
InterProi IPR000009. PP2A_PR55.
IPR018067. PP2A_PR55_CS.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view ]
PANTHERi PTHR11871. PTHR11871. 1 hit.
PIRSFi PIRSF037309. PP2A_PR55. 1 hit.
PRINTSi PR00600. PP2APR55.
SMARTi SM00320. WD40. 6 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 3 hits.
PROSITEi PS01024. PR55_1. 1 hit.
PS01025. PR55_2. 1 hit.
PS00678. WD_REPEATS_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence for a neuronal-specific isoform."
    Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J., Merlevede W., Hofsteenge J., Hemmings B.A.
    Biochemistry 30:3589-3597(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  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.
    , 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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-433 (ISOFORM 7).
    Tissue: Brain and Corpus callosum.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-131 (ISOFORM 6).
    Tissue: Brain and Hypothalamus.
  6. Strausberg R.L.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-197 (ISOFORM 2).
  7. Cited for: INVOLVEMENT IN SCA12.

Entry informationi

Entry namei2ABB_HUMAN
AccessioniPrimary (citable) accession number: Q00005
Secondary accession number(s): A6NEJ2
, A8K102, B3KPD0, B7Z2F2, B7Z304, D3DQF7, D3DQF8, G3V149
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 29, 2014
This is version 152 of the entry and version 1 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 5
    Human chromosome 5: 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