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Q00005 (2ABB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. 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 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 names
Name:PPP2R2B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

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.

Subcellular location

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.

Tissue specificity

Brain.

Domain

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.

Involvement in disease

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).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Sequence similarities

Belongs to the phosphatase 2A regulatory subunit B family.

Contains 7 WD repeats.

Sequence caution

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.

Binary interactions

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q00005-1)

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.
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.
Isoform 2 (identifier: Q00005-2)

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).
Isoform 3 (identifier: Q00005-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MEEDIDTRKINNSFLRDHSYA → MIPGIGTLTQDTLWCFSQVKGTIEIGT
Isoform 4 (identifier: Q00005-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVLQPSERHYRDWNHRRLGPWCSPTGSPAPLSCETGCGEGSWILVCRLLVPTQVSLLSM
Isoform 5 (identifier: Q00005-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLLSLPALHLQTSEHHPFFQLPHRRLGPWCSPTGSPAPLSCETGCGEGSWILVCRLLVPTQVSLLSM
Isoform 6 (identifier: Q00005-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MEEDIDTRKINNSFLRDHSYATE → MNYPDENTYGNK
Isoform 7 (identifier: Q00005-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHQPPPASCS...VPTQVSLLSM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
PRO_0000071421

Regions

Repeat22 – 6140WD 1
Repeat87 – 12842WD 2
Repeat171 – 20939WD 3
Repeat220 – 26041WD 4
Repeat279 – 31739WD 5
Repeat334 – 37542WD 6
Repeat410 – 44233WD 7

Amino acid modifications

Modified residue2751Phosphoserine By similarity
Modified residue2951Phosphotyrosine By similarity
Modified residue2981Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 2323MEEDI…SYATE → MNYPDENTYGNK in isoform 6.
VSP_044923
Alternative sequence1 – 2121MEEDI…DHSYA → MKCFSRYLPYIFRPPNTILS SSCH in isoform 2.
VSP_037976
Alternative sequence1 – 2121MEEDI…DHSYA → MIPGIGTLTQDTLWCFSQVK GTIEIGT in isoform 3.
VSP_037977
Alternative sequence11M → MVLQPSERHYRDWNHRRLGP WCSPTGSPAPLSCETGCGEG SWILVCRLLVPTQVSLLSM in isoform 4.
VSP_037978
Alternative sequence11M → MLLSLPALHLQTSEHHPFFQ LPHRRLGPWCSPTGSPAPLS CETGCGEGSWILVCRLLVPT QVSLLSM in isoform 5.
VSP_037979
Alternative sequence11M → MHQPPPASCSSSSSSSSSSC ECARVGVRVSALAPAAAPCP APRQLPYPRLPEPPSRGTST LIPARLGPWCSPTGSPAPLS CETGCGEGSWILVCRLLVPT QVSLLSM in isoform 7.
VSP_045748
Natural variant361G → V.
Corresponds to variant rs11547494 [ dbSNP | Ensembl ].
VAR_051738

Experimental info

Sequence conflict221T → A in BAH11838. Ref.2
Sequence conflict621H → N in BI669304. Ref.5
Sequence conflict1091S → F in BAH12040. Ref.2
Sequence conflict1631T → S in BI490027. Ref.6
Sequence conflict1641P → S in BAF82406. Ref.2
Sequence conflict2921S → R in BAH12040. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Bbeta) (Bbeta1) [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: C383C834B2852B8F

FASTA44351,710
        10         20         30         40         50         60 
MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI FQREQESKNQ 

        70         80         90        100        110        120 
VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV 

       130        140        150        160        170        180 
SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS 

       190        200        210        220        230        240 
VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY 

       250        260        270        280        290        300 
SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD 

       310        320        330        340        350        360 
YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN 

       370        380        390        400        410        420 
FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW 

       430        440 
HPSENIIAVA ATNNLYIFQD KVN 

« Hide

Isoform 2 (Bbeta2) [UniParc].

Checksum: D5BDD8D10F79CF0B
Show »

FASTA44652,017
Isoform 3 [UniParc].

Checksum: 6773D04E733403B1
Show »

FASTA44952,066
Isoform 4 [UniParc].

Checksum: 3FE3DD278143364A
Show »

FASTA50158,171
Isoform 5 [UniParc].

Checksum: D47AFC5DD1629FDB
Show »

FASTA50958,897
Isoform 6 [UniParc].

Checksum: B63F511DEF9670CA
Show »

FASTA43250,371
Isoform 7 [UniParc].

Checksum: DFACDC3C235450D7
Show »

FASTA54962,505

References

« Hide 'large scale' references
[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. 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 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. expand/collapse author list , 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]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] [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]"Expansion of a novel CAG trinucleotide repeat in the 5' region of PPP2R2B is associated with SCA12."
Holmes S.E., O'Hearn E.E., McInnis M.G., Gorelick-Feldman D.A., Kleiderlein J.J., Callahan C., Kwak N.G., Ingersoll-Ashworth R.G., Sherr M., Sumner A.J., Sharp A.H., Ananth U., Seltzer W.K., Boss M.A., Vieria-Saecker A.-M., Epplen J.T., Riess O., Ross C.A., Margolis R.L.
Nat. Genet. 23:391-392(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SCA12.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4283.1. [Q00005-2]
CCDS4284.2. [Q00005-5]
CCDS43380.1. [Q00005-6]
CCDS64281.1. [Q00005-4]
CCDS64282.1. [Q00005-3]
PIRB38351.
RefSeqNP_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]
UniGeneHs.627618.
Hs.655213.

3D structure databases

ProteinModelPortalQ00005.
SMRQ00005. Positions 23-442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111513. 45 interactions.
IntActQ00005. 167 interactions.
MINTMINT-6631022.
STRING9606.ENSP00000336591.

PTM databases

PhosphoSiteQ00005.

Polymorphism databases

DMDM231446.

Proteomic databases

PaxDbQ00005.
PRIDEQ00005.

Protocols and materials databases

DNASU5521.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336640; ENSP00000336591; ENSG00000156475. [Q00005-2]
ENST00000356826; ENSP00000349283; ENSG00000156475. [Q00005-1]
ENST00000394409; ENSP00000377931; ENSG00000156475. [Q00005-4]
ENST00000394410; ENSP00000377932; ENSG00000156475. [Q00005-6]
ENST00000394411; ENSP00000377933; ENSG00000156475. [Q00005-1]
ENST00000394413; ENSP00000377935; ENSG00000156475. [Q00005-1]
ENST00000394414; ENSP00000377936; ENSG00000156475. [Q00005-5]
ENST00000453001; ENSP00000398779; ENSG00000156475. [Q00005-1]
ENST00000504198; ENSP00000421396; ENSG00000156475. [Q00005-3]
ENST00000508545; ENSP00000431320; ENSG00000156475. [Q00005-6]
GeneID5521.
KEGGhsa:5521.
UCSCuc003loe.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

CTD5521.
GeneCardsGC05M145969.
GeneReviewsPPP2R2B.
HGNCHGNC:9305. PPP2R2B.
HPAHPA038118.
MIM604325. gene.
604326. phenotype.
neXtProtNX_Q00005.
Orphanet98762. Spinocerebellar ataxia type 12.
PharmGKBPA33669.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5170.
HOVERGENHBG000012.
InParanoidQ00005.
KOK04354.
OMARLRDPSM.
OrthoDBEOG7Q5HCZ.
PhylomeDBQ00005.
TreeFamTF105553.

Enzyme and pathway databases

SignaLinkQ00005.

Gene expression databases

ArrayExpressQ00005.
BgeeQ00005.
CleanExHS_PPP2R2B.
GenevestigatorQ00005.

Family and domain databases

Gene3D2.130.10.10. 3 hits.
InterProIPR000009. 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]
PANTHERPTHR11871. PTHR11871. 1 hit.
PIRSFPIRSF037309. PP2A_PR55. 1 hit.
PRINTSPR00600. PP2APR55.
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 3 hits.
PROSITEPS01024. PR55_1. 1 hit.
PS01025. PR55_2. 1 hit.
PS00678. WD_REPEATS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP2R2B. human.
GeneWikiPPP2R2B.
GenomeRNAi5521.
NextBio21356.
PROQ00005.
SOURCESearch...

Entry information

Entry name2ABB_HUMAN
AccessionPrimary (citable) accession number: Q00005
Secondary accession number(s): A6NEJ2 expand/collapse secondary AC list , A8K102, B3KPD0, B7Z2F2, B7Z304, D3DQF7, D3DQF8, G3V149
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: July 9, 2014
This is version 150 of the entry and version 1 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 5

Human chromosome 5: entries, gene names and cross-references to MIM