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Protein

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform

Gene

PPP2R1B

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

Functioni

The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit.

GO - Molecular functioni

GO - Biological processi

  • apoptotic process involved in morphogenesis Source: UniProtKB
  • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: UniProtKB
  • protein complex assembly Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137713-MONOMER.
ReactomeiR-HSA-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-HSA-163685. Integration of energy metabolism.
R-HSA-163767. PP2A-mediated dephosphorylation of key metabolic factors.
R-HSA-180024. DARPP-32 events.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-196299. Beta-catenin phosphorylation cascade.
R-HSA-198753. ERK/MAPK targets.
R-HSA-202670. ERKs are inactivated.
R-HSA-2465910. MASTL Facilitates Mitotic Progression.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-389513. CTLA4 inhibitory signaling.
R-HSA-432142. Platelet sensitization by LDL.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5339716. Misspliced GSK3beta mutants stabilize beta-catenin.
R-HSA-5358747. S33 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358749. S37 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358751. S45 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358752. T41 mutants of beta-catenin aren't phosphorylated.
R-HSA-5467337. APC truncation mutants have impaired AXIN binding.
R-HSA-5467340. AXIN missense mutants destabilize the destruction complex.
R-HSA-5467348. Truncations of AMER1 destabilize the destruction complex.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5673000. RAF activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-6804757. Regulation of TP53 Degradation.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-69231. Cyclin D associated events in G1.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-70171. Glycolysis.
SIGNORiP30154.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
Alternative name(s):
PP2A subunit A isoform PR65-beta
PP2A subunit A isoform R1-beta
Gene namesi
Name:PPP2R1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:9303. PPP2R1B.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • membrane raft Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi5519.
MalaCardsiPPP2R1B.
OpenTargetsiENSG00000137713.
PharmGKBiPA33667.

Polymorphism and mutation databases

BioMutaiPPP2R1B.
DMDMi116241236.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000714032 – 601Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoformAdd BLAST600

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP30154.
MaxQBiP30154.
PaxDbiP30154.
PeptideAtlasiP30154.
PRIDEiP30154.

PTM databases

iPTMnetiP30154.
PhosphoSitePlusiP30154.

Expressioni

Gene expression databases

BgeeiENSG00000137713.
CleanExiHS_PPP2R1B.
ExpressionAtlasiP30154. baseline and differential.
GenevisibleiP30154. HS.

Organism-specific databases

HPAiCAB004034.
HPA018908.

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. Interacts with IPO9. Interacts with SGO1. Interacts with RAF1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ClockO087852EBI-357094,EBI-79859From a different organism.
PPP2CAP677757EBI-357094,EBI-712311
PPP2R1AP301532EBI-357094,EBI-302388
PPP2R2AP631513EBI-357094,EBI-1048931
PPP2R5AQ151722EBI-357094,EBI-641666
PPP2R5CQ133622EBI-357094,EBI-1266156
PPP2R5DQ147383EBI-357094,EBI-396563
PPP2R5EQ165373EBI-357094,EBI-968374
RALAP112336EBI-357094,EBI-1036803
Unc5bO087224EBI-357094,EBI-4404185From a different organism.

Protein-protein interaction databases

BioGridi111511. 109 interactors.
DIPiDIP-36616N.
IntActiP30154. 77 interactors.
MINTiMINT-1150161.
STRINGi9606.ENSP00000311344.

Structurei

3D structure databases

ProteinModelPortaliP30154.
SMRiP30154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati20 – 58HEAT 1Add BLAST39
Repeati59 – 96HEAT 2Add BLAST38
Repeati97 – 135HEAT 3Add BLAST39
Repeati136 – 173HEAT 4Add BLAST38
Repeati174 – 212HEAT 5Add BLAST39
Repeati213 – 251HEAT 6Add BLAST39
Repeati252 – 290HEAT 7Add BLAST39
Repeati291 – 333HEAT 8Add BLAST43
Repeati334 – 372HEAT 9Add BLAST39
Repeati373 – 411HEAT 10Add BLAST39
Repeati412 – 450HEAT 11Add BLAST39
Repeati451 – 489HEAT 12Add BLAST39
Repeati490 – 528HEAT 13Add BLAST39
Repeati529 – 567HEAT 14Add BLAST39
Repeati568 – 601HEAT 15Add BLAST34

Domaini

Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure.

Sequence similaritiesi

Contains 15 HEAT repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0211. Eukaryota.
ENOG410XQVI. LUCA.
GeneTreeiENSGT00730000110944.
HOGENOMiHOG000078539.
HOVERGENiHBG000011.
InParanoidiP30154.
KOiK03456.
OMAiCGREITT.
OrthoDBiEOG091G045V.
PhylomeDBiP30154.
TreeFamiTF105552.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
IPR031090. PP2A_A_meta.
[Graphical view]
PANTHERiPTHR10648:SF9. PTHR10648:SF9. 1 hit.
PfamiPF02985. HEAT. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 12 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P30154-1) [UniParc]FASTAAdd to basket

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
MAGASELGTG PGAAGGDGDD SLYPIAVLID ELRNEDVQLR LNSIKKLSTI
60 70 80 90 100
ALALGVERTR SELLPFLTDT IYDEDEVLLA LAEQLGNFTG LVGGPDFAHC
110 120 130 140 150
LLPPLENLAT VEETVVRDKA VESLRQISQE HTPVALEAYF VPLVKRLASG
160 170 180 190 200
DWFTSRTSAC GLFSVCYPRA SNAVKAEIRQ QFRSLCSDDT PMVRRAAASK
210 220 230 240 250
LGEFAKVLEL DSVKSEIVPL FTSLASDEQD SVRLLAVEAC VSIAQLLSQD
260 270 280 290 300
DLETLVMPTL RQAAEDKSWR VRYMVADRFS ELQKAMGPKI TLNDLIPAFQ
310 320 330 340 350
NLLKDCEAEV RAAAAHKVKE LGENLPIEDR ETIIMNQILP YIKELVSDTN
360 370 380 390 400
QHVKSALASV IMGLSTILGK ENTIEHLLPL FLAQLKDECP DVRLNIISNL
410 420 430 440 450
DCVNEVIGIR QLSQSLLPAI VELAEDAKWR VRLAIIEYMP LLAGQLGVEF
460 470 480 490 500
FDEKLNSLCM AWLVDHVYAI REAATNNLMK LVQKFGTEWA QNTIVPKVLV
510 520 530 540 550
MANDPNYLHR MTTLFCINAL SEACGQEITT KQMLPIVLKM AGDQVANVRF
560 570 580 590 600
NVAKSLQKIG PILDTNALQG EVKPVLQKLG QDEDMDVKYF AQEAISVLAL

A
Length:601
Mass (Da):66,214
Last modified:October 17, 2006 - v3
Checksum:i86AB20D7505210B0
GO
Isoform 2 (identifier: P30154-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     598-601: LALA → VAQRLRKLEFPVKDSGEPSVPRADKNHFPRPTVPGEDMGKGPVYQLRGDTRDTLAQLGIAELVHFSQSTD

Show »
Length:667
Mass (Da):73,585
Checksum:i726EA8A8FB0DEB23
GO
Isoform 3 (identifier: P30154-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     39-102: Missing.
     598-601: LALA → VAQRLRKLEFPVKDSGEPSVPRADKNHFPRPTVPGEDMGKGPVYQLRGDTRDTLAQLGIAELVHFSQSTD

Note: No experimental confirmation available.
Show »
Length:603
Mass (Da):66,617
Checksum:i3FB011FD47C65810
GO
Isoform 4 (identifier: P30154-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     344-388: Missing.

Note: No experimental confirmation available.
Show »
Length:556
Mass (Da):61,314
Checksum:i1FFAFBC9A8C38FA2
GO
Isoform 5 (identifier: P30154-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     103-229: Missing.

Show »
Length:474
Mass (Da):52,214
Checksum:i6F8EEB7D9779BFB1
GO

Sequence cautioni

The sequence AAA59983 differs from that shown. Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence BAG59103 differs from that shown. Reason: Frameshift at position 540.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti74E → V in AAA59983 (PubMed:2159327).Curated1
Sequence conflicti178I → T in AAC63525 (PubMed:9795170).Curated1
Sequence conflicti178I → T in AAG39644 (PubMed:11313745).Curated1
Sequence conflicti178I → T in AAA59983 (PubMed:2159327).Curated1
Sequence conflicti211D → G in BAG57867 (PubMed:14702039).Curated1
Sequence conflicti411Q → R in AAA59983 (PubMed:2159327).Curated1
Sequence conflicti503N → S in BAG57867 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0228958G → R in a lung cancer patient. 1 PublicationCorresponds to variant rs142771326dbSNPEnsembl.1
Natural variantiVAR_02289615G → A in a colorectal cancer patient. 1 Publication1
Natural variantiVAR_02289765P → S in a lung cancer patient. 1 Publication1
Natural variantiVAR_00638490G → D in a lung cancer patient. 3 PublicationsCorresponds to variant rs1805076dbSNPEnsembl.1
Natural variantiVAR_022898101L → P in a colon adenocarcinoma. 1 Publication1
Natural variantiVAR_022899343K → E in a lung cancer patient. 1 Publication1
Natural variantiVAR_022900365S → P in a colorectal cancer patient. 1 Publication1
Natural variantiVAR_022901448V → A in a colon adenocarcinoma. 1 Publication1
Natural variantiVAR_022902498V → E in a colorectal cancer patient. 1 Publication1
Natural variantiVAR_022903499L → I in a colorectal cancer patient. 1 Publication1
Natural variantiVAR_022904500V → G in a colorectal cancer patient. 1 Publication1
Natural variantiVAR_022905504D → G in a lung cancer patient. 1 Publication1
Natural variantiVAR_022906545V → A in a colon adenocarcinoma. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04337939 – 102Missing in isoform 3. 1 PublicationAdd BLAST64
Alternative sequenceiVSP_046684103 – 229Missing in isoform 5. 1 PublicationAdd BLAST127
Alternative sequenceiVSP_045275344 – 388Missing in isoform 4. 1 PublicationAdd BLAST45
Alternative sequenceiVSP_036460598 – 601LALA → VAQRLRKLEFPVKDSGEPSV PRADKNHFPRPTVPGEDMGK GPVYQLRGDTRDTLAQLGIA ELVHFSQSTD in isoform 2 and isoform 3. 2 Publications4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF083439
, AF083425, AF083426, AF083427, AF083428, AF083429, AF083430, AF083431, AF083432, AF083433, AF083434, AF083435, AF083436, AF083437, AF083438 Genomic DNA. Translation: AAC63525.1.
AF087438 mRNA. Translation: AAC69624.1.
AF163473 mRNA. Translation: AAG39644.1.
AK294716 mRNA. Translation: BAG57867.1.
AK296455 mRNA. Translation: BAG59103.1. Frameshift.
AK301705 mRNA. Translation: BAG63177.1.
EF445011 Genomic DNA. Translation: ACA06046.1.
EF445011 Genomic DNA. Translation: ACA06047.1.
AP000925 Genomic DNA. No translation available.
AP001781 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67150.1.
CH471065 Genomic DNA. Translation: EAW67151.1.
BC027596 mRNA. Translation: AAH27596.1.
M65254 mRNA. Translation: AAA59983.1. Sequence problems.
CCDSiCCDS53706.1. [P30154-3]
CCDS53707.1. [P30154-5]
CCDS53708.1. [P30154-4]
CCDS8348.1. [P30154-2]
CCDS8349.1. [P30154-1]
PIRiB34541.
RefSeqiNP_001171033.1. NM_001177562.1. [P30154-4]
NP_001171034.1. NM_001177563.1. [P30154-5]
NP_002707.3. NM_002716.4. [P30154-1]
NP_859050.1. NM_181699.2. [P30154-2]
NP_859051.1. NM_181700.1. [P30154-3]
UniGeneiHs.269128.
Hs.584790.

Genome annotation databases

EnsembliENST00000311129; ENSP00000311344; ENSG00000137713. [P30154-2]
ENST00000341980; ENSP00000343317; ENSG00000137713. [P30154-4]
ENST00000393055; ENSP00000376775; ENSG00000137713. [P30154-5]
ENST00000426998; ENSP00000410671; ENSG00000137713. [P30154-3]
ENST00000527614; ENSP00000437193; ENSG00000137713. [P30154-1]
GeneIDi5519.
KEGGihsa:5519.
UCSCiuc001plw.2. human. [P30154-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF083439
, AF083425, AF083426, AF083427, AF083428, AF083429, AF083430, AF083431, AF083432, AF083433, AF083434, AF083435, AF083436, AF083437, AF083438 Genomic DNA. Translation: AAC63525.1.
AF087438 mRNA. Translation: AAC69624.1.
AF163473 mRNA. Translation: AAG39644.1.
AK294716 mRNA. Translation: BAG57867.1.
AK296455 mRNA. Translation: BAG59103.1. Frameshift.
AK301705 mRNA. Translation: BAG63177.1.
EF445011 Genomic DNA. Translation: ACA06046.1.
EF445011 Genomic DNA. Translation: ACA06047.1.
AP000925 Genomic DNA. No translation available.
AP001781 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67150.1.
CH471065 Genomic DNA. Translation: EAW67151.1.
BC027596 mRNA. Translation: AAH27596.1.
M65254 mRNA. Translation: AAA59983.1. Sequence problems.
CCDSiCCDS53706.1. [P30154-3]
CCDS53707.1. [P30154-5]
CCDS53708.1. [P30154-4]
CCDS8348.1. [P30154-2]
CCDS8349.1. [P30154-1]
PIRiB34541.
RefSeqiNP_001171033.1. NM_001177562.1. [P30154-4]
NP_001171034.1. NM_001177563.1. [P30154-5]
NP_002707.3. NM_002716.4. [P30154-1]
NP_859050.1. NM_181699.2. [P30154-2]
NP_859051.1. NM_181700.1. [P30154-3]
UniGeneiHs.269128.
Hs.584790.

3D structure databases

ProteinModelPortaliP30154.
SMRiP30154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111511. 109 interactors.
DIPiDIP-36616N.
IntActiP30154. 77 interactors.
MINTiMINT-1150161.
STRINGi9606.ENSP00000311344.

PTM databases

iPTMnetiP30154.
PhosphoSitePlusiP30154.

Polymorphism and mutation databases

BioMutaiPPP2R1B.
DMDMi116241236.

Proteomic databases

EPDiP30154.
MaxQBiP30154.
PaxDbiP30154.
PeptideAtlasiP30154.
PRIDEiP30154.

Protocols and materials databases

DNASUi5519.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311129; ENSP00000311344; ENSG00000137713. [P30154-2]
ENST00000341980; ENSP00000343317; ENSG00000137713. [P30154-4]
ENST00000393055; ENSP00000376775; ENSG00000137713. [P30154-5]
ENST00000426998; ENSP00000410671; ENSG00000137713. [P30154-3]
ENST00000527614; ENSP00000437193; ENSG00000137713. [P30154-1]
GeneIDi5519.
KEGGihsa:5519.
UCSCiuc001plw.2. human. [P30154-1]

Organism-specific databases

CTDi5519.
DisGeNETi5519.
GeneCardsiPPP2R1B.
HGNCiHGNC:9303. PPP2R1B.
HPAiCAB004034.
HPA018908.
MalaCardsiPPP2R1B.
MIMi603113. gene.
neXtProtiNX_P30154.
OpenTargetsiENSG00000137713.
PharmGKBiPA33667.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0211. Eukaryota.
ENOG410XQVI. LUCA.
GeneTreeiENSGT00730000110944.
HOGENOMiHOG000078539.
HOVERGENiHBG000011.
InParanoidiP30154.
KOiK03456.
OMAiCGREITT.
OrthoDBiEOG091G045V.
PhylomeDBiP30154.
TreeFamiTF105552.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137713-MONOMER.
ReactomeiR-HSA-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-HSA-163685. Integration of energy metabolism.
R-HSA-163767. PP2A-mediated dephosphorylation of key metabolic factors.
R-HSA-180024. DARPP-32 events.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-196299. Beta-catenin phosphorylation cascade.
R-HSA-198753. ERK/MAPK targets.
R-HSA-202670. ERKs are inactivated.
R-HSA-2465910. MASTL Facilitates Mitotic Progression.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-389513. CTLA4 inhibitory signaling.
R-HSA-432142. Platelet sensitization by LDL.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5339716. Misspliced GSK3beta mutants stabilize beta-catenin.
R-HSA-5358747. S33 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358749. S37 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358751. S45 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358752. T41 mutants of beta-catenin aren't phosphorylated.
R-HSA-5467337. APC truncation mutants have impaired AXIN binding.
R-HSA-5467340. AXIN missense mutants destabilize the destruction complex.
R-HSA-5467348. Truncations of AMER1 destabilize the destruction complex.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5673000. RAF activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-6804757. Regulation of TP53 Degradation.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-69231. Cyclin D associated events in G1.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-70171. Glycolysis.
SIGNORiP30154.

Miscellaneous databases

ChiTaRSiPPP2R1B. human.
GeneWikiiPPP2R1B.
GenomeRNAii5519.
PROiP30154.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137713.
CleanExiHS_PPP2R1B.
ExpressionAtlasiP30154. baseline and differential.
GenevisibleiP30154. HS.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
IPR031090. PP2A_A_meta.
[Graphical view]
PANTHERiPTHR10648:SF9. PTHR10648:SF9. 1 hit.
PfamiPF02985. HEAT. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 12 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei2AAB_HUMAN
AccessioniPrimary (citable) accession number: P30154
Secondary accession number(s): A8MY67
, B0YJ69, B4DGQ6, B4DK91, B4DWW5, F8W8G1, O75620, Q8NHV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 17, 2006
Last modified: November 2, 2016
This is version 164 of the entry and version 3 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 11
    Human chromosome 11: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.