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P30154 (2AAB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PPP2R1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length601 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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 SGOL1. Interacts with RAF1. Ref.10 Ref.11 Ref.12

Domain

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 similarities

Belongs to the phosphatase 2A regulatory subunit A family.

Contains 15 HEAT repeats.

Sequence caution

The sequence AAA59983.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

The sequence BAG59103.1 differs from that shown. Reason: Frameshift at position 540.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P30154-1)

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.
Isoform 2 (identifier: P30154-2)

The sequence of this isoform differs from the canonical sequence as follows:
     598-601: LALA → VAQRLRKLEFPVKDSGEPSVPRADKNHFPRPTVPGEDMGKGPVYQLRGDTRDTLAQLGIAELVHFSQSTD
Isoform 3 (identifier: P30154-3)

The sequence of this isoform differs from the canonical sequence as follows:
     39-102: Missing.
     598-601: LALA → VAQRLRKLEFPVKDSGEPSVPRADKNHFPRPTVPGEDMGKGPVYQLRGDTRDTLAQLGIAELVHFSQSTD
Note: No experimental confirmation available.
Isoform 4 (identifier: P30154-4)

The sequence of this isoform differs from the canonical sequence as follows:
     344-388: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: P30154-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 601600Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
PRO_0000071403

Regions

Repeat20 – 5839HEAT 1
Repeat59 – 9638HEAT 2
Repeat97 – 13539HEAT 3
Repeat136 – 17338HEAT 4
Repeat174 – 21239HEAT 5
Repeat213 – 25139HEAT 6
Repeat252 – 29039HEAT 7
Repeat291 – 33343HEAT 8
Repeat334 – 37239HEAT 9
Repeat373 – 41139HEAT 10
Repeat412 – 45039HEAT 11
Repeat451 – 48939HEAT 12
Repeat490 – 52839HEAT 13
Repeat529 – 56739HEAT 14
Repeat568 – 60134HEAT 15

Amino acid modifications

Modified residue21N-acetylalanine Ref.14

Natural variations

Alternative sequence39 – 10264Missing in isoform 3.
VSP_043379
Alternative sequence103 – 229127Missing in isoform 5.
VSP_046684
Alternative sequence344 – 38845Missing in isoform 4.
VSP_045275
Alternative sequence598 – 6014LALA → VAQRLRKLEFPVKDSGEPSV PRADKNHFPRPTVPGEDMGK GPVYQLRGDTRDTLAQLGIA ELVHFSQSTD in isoform 2 and isoform 3.
VSP_036460
Natural variant81G → R in a lung cancer patient. Ref.2
Corresponds to variant rs142771326 [ dbSNP | Ensembl ].
VAR_022895
Natural variant151G → A in a colorectal cancer patient. Ref.16
VAR_022896
Natural variant651P → S in a lung cancer patient. Ref.2
VAR_022897
Natural variant901G → D in a lung cancer patient. Ref.2 Ref.15 Ref.17
Corresponds to variant rs1805076 [ dbSNP | Ensembl ].
VAR_006384
Natural variant1011L → P in a colon adenocarcinoma. Ref.2
VAR_022898
Natural variant3431K → E in a lung cancer patient. Ref.2
VAR_022899
Natural variant3651S → P in a colorectal cancer patient. Ref.16
VAR_022900
Natural variant4481V → A in a colon adenocarcinoma. Ref.2
VAR_022901
Natural variant4981V → E in a colorectal cancer patient. Ref.16
VAR_022902
Natural variant4991L → I in a colorectal cancer patient. Ref.16
VAR_022903
Natural variant5001V → G in a colorectal cancer patient. Ref.16
VAR_022904
Natural variant5041D → G in a lung cancer patient. Ref.2
VAR_022905
Natural variant5451V → A in a colon adenocarcinoma. Ref.2
VAR_022906

Experimental info

Sequence conflict741E → V in AAA59983. Ref.9
Sequence conflict1781I → T in AAC63525. Ref.1
Sequence conflict1781I → T in AAG39644. Ref.3
Sequence conflict1781I → T in AAA59983. Ref.9
Sequence conflict2111D → G in BAG57867. Ref.4
Sequence conflict4111Q → R in AAA59983. Ref.9
Sequence conflict5031N → S in BAG57867. Ref.4

Sequences

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

Last modified October 17, 2006. Version 3.
Checksum: 86AB20D7505210B0

FASTA60166,214
        10         20         30         40         50         60 
MAGASELGTG PGAAGGDGDD SLYPIAVLID ELRNEDVQLR LNSIKKLSTI ALALGVERTR 

        70         80         90        100        110        120 
SELLPFLTDT IYDEDEVLLA LAEQLGNFTG LVGGPDFAHC LLPPLENLAT VEETVVRDKA 

       130        140        150        160        170        180 
VESLRQISQE HTPVALEAYF VPLVKRLASG DWFTSRTSAC GLFSVCYPRA SNAVKAEIRQ 

       190        200        210        220        230        240 
QFRSLCSDDT PMVRRAAASK LGEFAKVLEL DSVKSEIVPL FTSLASDEQD SVRLLAVEAC 

       250        260        270        280        290        300 
VSIAQLLSQD DLETLVMPTL RQAAEDKSWR VRYMVADRFS ELQKAMGPKI TLNDLIPAFQ 

       310        320        330        340        350        360 
NLLKDCEAEV RAAAAHKVKE LGENLPIEDR ETIIMNQILP YIKELVSDTN QHVKSALASV 

       370        380        390        400        410        420 
IMGLSTILGK ENTIEHLLPL FLAQLKDECP DVRLNIISNL DCVNEVIGIR QLSQSLLPAI 

       430        440        450        460        470        480 
VELAEDAKWR VRLAIIEYMP LLAGQLGVEF FDEKLNSLCM AWLVDHVYAI REAATNNLMK 

       490        500        510        520        530        540 
LVQKFGTEWA QNTIVPKVLV MANDPNYLHR MTTLFCINAL SEACGQEITT KQMLPIVLKM 

       550        560        570        580        590        600 
AGDQVANVRF NVAKSLQKIG PILDTNALQG EVKPVLQKLG QDEDMDVKYF AQEAISVLAL 


A 

« Hide

Isoform 2 [UniParc].

Checksum: 726EA8A8FB0DEB23
Show »

FASTA66773,585
Isoform 3 [UniParc].

Checksum: 3FB011FD47C65810
Show »

FASTA60366,617
Isoform 4 [UniParc].

Checksum: 1FFAFBC9A8C38FA2
Show »

FASTA55661,314
Isoform 5 [UniParc].

Checksum: 6F8EEB7D9779BFB1
Show »

FASTA47452,214

References

« Hide 'large scale' references
[1]"Genomic organization and precise physical location of protein phosphatase 2A regulatory subunit A beta isoform gene on chromosome band 11q23."
Baysal B.E., Farr J.E., Goss J.R., Devlin B., Richard C.W. III
Gene 217:107-116(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Alterations of the PPP2R1B gene in human lung and colon cancer."
Wang S.S., Esplin E.D., Li J.L., Huang L., Gazdar A., Minna J., Evans G.A.
Science 282:284-287(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-8; SER-65; ASP-90; PRO-101; GLU-343; ALA-448; GLY-504 AND ALA-545.
[3]"A high-resolution integrated map spanning the SDHD gene at 11q23: a 1.1-Mb BAC contig, a partial transcript map and 15 new repeat polymorphisms in a tumour-suppressor region."
Baysal B.E., Willett-Brozick J.E., Taschner P.E.M., Dauwerse J.G., Devilee P., Devlin B.
Eur. J. Hum. Genet. 9:121-129(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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. 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 3; 4 AND 5).
Tissue: Brain, Testis and Thalamus.
[5]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 2).
Tissue: Testis.
[9]"Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure."
Hemmings B.A., Adams-Pearson C., Maurer F., Mueller P., Goris J., Merlevede W., Hofsteenge J., Stone S.R.
Biochemistry 29:3166-3173(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-601 (ISOFORM 1).
[10]"Raf-1-associated protein phosphatase 2A as a positive regulator of kinase activation."
Abraham D., Podar K., Pacher M., Kubicek M., Welzel N., Hemmings B.A., Dilworth S.M., Mischak H., Kolch W., Baccarini M.
J. Biol. Chem. 275:22300-22304(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAF1.
[11]"Interaction between protein phosphatase 2A and members of the importin beta superfamily."
Lubert E.J., Sarge K.D.
Biochem. Biophys. Res. Commun. 303:908-913(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IPO9.
[12]"Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SGOL1.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"Absence of PPP2R1B gene alterations in primary ovarian cancers."
Campbell I.G., Manolitsas T.
Oncogene 18:6367-6369(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASP-90.
[16]"Alterations of the PPP2R1B gene located at 11q23 in human colorectal cancers."
Takagi Y., Futamura M., Yamaguchi K., Aoki S., Takahashi T., Saji S.
Gut 47:268-271(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALA-15; PRO-365; GLU-498; ILE-499 AND GLY-500.
[17]"Alterations in the suppressor gene PPP2R1B in parathyroid hyperplasias and adenomas."
Hemmer S., Wasenius V.M., Haglund C., Zhu Y., Knuutila S., Franssila K., Joensuu H.
Cancer Genet. Cytogenet. 134:13-17(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASP-90.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF083439 expand/collapse EMBL AC list , 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.
PIRB34541.
RefSeqNP_001171033.1. NM_001177562.1.
NP_001171034.1. NM_001177563.1.
NP_002707.3. NM_002716.4.
NP_859050.1. NM_181699.2.
NP_859051.1. NM_181700.1.
UniGeneHs.584790.

3D structure databases

ProteinModelPortalP30154.
SMRP30154. Positions 19-601.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111511. 56 interactions.
IntActP30154. 64 interactions.
MINTMINT-1150161.
STRING9606.ENSP00000311344.

PTM databases

PhosphoSiteP30154.

Polymorphism databases

DMDM116241236.

Proteomic databases

PaxDbP30154.
PRIDEP30154.

Protocols and materials databases

DNASU5519.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311129; ENSP00000311344; ENSG00000137713. [P30154-2]
ENST00000341980; ENSP00000343317; ENSG00000137713. [P30154-4]
ENST00000393055; ENSP00000376775; ENSG00000137713. [P30154-5]
ENST00000426998; ENSP00000410671; ENSG00000137713. [P30154-3]
ENST00000527614; ENSP00000437193; ENSG00000137713. [P30154-1]
ENST00000571902; ENSP00000459644; ENSG00000262764. [P30154-3]
ENST00000571959; ENSP00000459838; ENSG00000262764. [P30154-2]
ENST00000573946; ENSP00000459456; ENSG00000262764. [P30154-5]
ENST00000575443; ENSP00000459827; ENSG00000262764. [P30154-4]
ENST00000576276; ENSP00000461254; ENSG00000262764. [P30154-1]
GeneID5519.
KEGGhsa:5519.
UCSCuc001plw.1. human. [P30154-2]
uc001plx.1. human. [P30154-1]
uc010rwi.1. human. [P30154-3]

Organism-specific databases

CTD5519.
GeneCardsGC11M111642.
HGNCHGNC:9303. PPP2R1B.
HPACAB004034.
HPA018908.
MIM603113. gene.
neXtProtNX_P30154.
PharmGKBPA33667.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG247268.
HOGENOMHOG000078539.
HOVERGENHBG000011.
KOK03456.
OMAPQEDLET.
OrthoDBEOG764722.
PhylomeDBP30154.
TreeFamTF105552.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP30154.
BgeeP30154.
CleanExHS_PPP2R1B.
GenevestigatorP30154.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
[Graphical view]
PfamPF02985. HEAT. 2 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50077. HEAT_REPEAT. 12 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP2R1B. human.
GeneWikiPPP2R1B.
GenomeRNAi5519.
NextBio21346.
PROP30154.
SOURCESearch...

Entry information

Entry name2AAB_HUMAN
AccessionPrimary (citable) accession number: P30154
Secondary accession number(s): A8MY67 expand/collapse secondary AC list , B0YJ69, B4DGQ6, B4DK91, B4DWW5, F8W8G1, O75620, Q8NHV8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 137 of the entry and version 3 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

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 11

Human chromosome 11: entries, gene names and cross-references to MIM