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Q6ZVD8 (PHLP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PH domain leucine-rich repeat-containing protein phosphatase 2

EC=3.1.3.16
Alternative name(s):
PH domain leucine-rich repeat-containing protein phosphatase-like
Short name=PHLPP-like
Gene names
Name:PHLPP2
Synonyms:KIAA0931, PHLPPL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1323 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein phosphatase that mediates dephosphorylation of 'Ser-473' of AKT1, 'Ser-660' of PRKCB isoform beta-IIand 'Ser-657' of PRKCA. AKT1 regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of AKT1 triggers apoptosis and decreases cell proliferation. Also controls the phosphorylation of AKT3. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Inhibits cancer cell proliferation and may act as a tumor suppressor. Ref.7 Ref.8 Ref.9

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 manganese ions per subunit By similarity.

Subunit structure

Interacts with AKT1, AKT3 and PRKCB isoform beta-II Ref.7 Ref.8

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein. Nucleus. Note: In colorectal cancer tissue, expression is concentrated in the cytoplasm and nucleus. Ref.7 Ref.9

Tissue specificity

In colorectal cancer tissue, expression is highest in the surface epithelium of normal colonic mucosa adjacent to the cancer tissue but is largely excluded from the crypt bases. Expression is lost or significantly decreased in 80% of tested tumors (at protein level). Ref.9

Sequence similarities

Contains 22 LRR (leucine-rich) repeats.

Contains 1 PH domain.

Contains 1 PP2C-like domain.

Biophysicochemical properties

Kinetic parameters:

KM=4.13 mM for p-nitrophenyl phosphate

Sequence caution

The sequence BAA76775.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAA91943.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   DomainLeucine-rich repeat
Repeat
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

protein dephosphorylation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay. Source: LIFEdb

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

photoreceptor inner segment

Inferred from electronic annotation. Source: Ensembl

photoreceptor outer segment membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine phosphatase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6ZVD8-1)

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: Q6ZVD8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     940-956: DNKVNGVTCCTRMLGCT → NWVLNQKHLQDFPGEDK
     957-1323: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q6ZVD8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     596-662: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13231323PH domain leucine-rich repeat-containing protein phosphatase 2
PRO_0000057784

Regions

Domain150 – 24899PH
Repeat250 – 27122LRR 1
Repeat273 – 29624LRR 2
Repeat300 – 32122LRR 3
Repeat323 – 34422LRR 4
Repeat346 – 36823LRR 5
Repeat369 – 39022LRR 6
Repeat392 – 41221LRR 7
Repeat416 – 43924LRR 8
Repeat440 – 46021LRR 9
Repeat461 – 48020LRR 10
Repeat481 – 50222LRR 11
Repeat503 – 52422LRR 12
Repeat526 – 54722LRR 13
Repeat549 – 57022LRR 14
Repeat571 – 59222LRR 15
Repeat595 – 61622LRR 16
Repeat621 – 64424LRR 17
Repeat645 – 66622LRR 18
Repeat669 – 69022LRR 19
Repeat692 – 71322LRR 20
Repeat714 – 73522LRR 21
Repeat737 – 75822LRR 22
Domain775 – 1031257PP2C-like
Compositional bias40 – 4910Poly-Thr
Compositional bias50 – 6011Poly-Ser
Compositional bias1071 – 10744Poly-Ser

Sites

Metal binding8201Manganese 1 By similarity
Metal binding8201Manganese 2 By similarity
Metal binding8211Manganese 1; via carbonyl oxygen By similarity
Metal binding9851Manganese 2 By similarity
Metal binding10241Manganese 2 By similarity

Natural variations

Alternative sequence596 – 66267Missing in isoform 3.
VSP_017265
Alternative sequence940 – 95617DNKVN…MLGCT → NWVLNQKHLQDFPGEDK in isoform 2.
VSP_014056
Alternative sequence957 – 1323367Missing in isoform 2.
VSP_014057

Experimental info

Sequence conflict1471R → C in BX647823. Ref.3
Sequence conflict5421V → L Ref.4
Sequence conflict7661K → E in BX647823. Ref.3
Sequence conflict8961A → G in BAA91943. Ref.6
Sequence conflict9781E → G in BX647823. Ref.3
Sequence conflict10161L → S in BX647823. Ref.3
Sequence conflict13121R → Q in AAI29928. Ref.5

Sequences

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

Last modified October 17, 2006. Version 3.
Checksum: 04FC8550C2E22A6D

FASTA1,323146,751
        10         20         30         40         50         60 
MKRNGSRNCL NRRSRFGSRE RDWLREDVKR GCVYLYGADT TTATTTTTTS SSSSSSSSSS 

        70         80         90        100        110        120 
DLHLVLCTVE TPASEICAGE GRESLYLQLH GDLVRRLEPT ERPLQIVYDY LSRLGFDDPV 

       130        140        150        160        170        180 
RIQEEATNPD LGCMIRFYGE KPCHMDRLDR ILLSGIYNVR KGKTQLHKWA ERLVVLCGTC 

       190        200        210        220        230        240 
LIVSSVKDCQ TGKMHILPLV GGKIEEVKRR QYSLAFSSAG AQAQTYHVSF ETLAEYQRWQ 

       250        260        270        280        290        300 
RQASKVVSQR ISTVDLSCYS LEEVPEHLFY SQDITYLNLR HNFMQLERPG GLDTLYKFSQ 

       310        320        330        340        350        360 
LKGLNLSHNK LGLFPILLCE ISTLTELNLS CNGFHDLPSQ IGNLLNLQTL CLDGNFLTTL 

       370        380        390        400        410        420 
PEELGNLQQL SSLGISFNNF SQIPEVYEKL TMLDRVVMAG NCLEVLNLGV LNRMNHIKHV 

       430        440        450        460        470        480 
DLRMNHLKTM VIENLEGNKH ITHVDLRDNR LTDLDLSSLC SLEQLHCGRN QLRELTLSGF 

       490        500        510        520        530        540 
SLRTLYASSN RLTAVNVYPV PSLLTFLDLS RNLLECVPDW ACEAKKIEVL DVSYNLLTEV 

       550        560        570        580        590        600 
PVRILSSLSL RKLMLGHNHV QNLPTLVEHI PLEVLDLQHN ALTRLPDTLF SKALNLRYLN 

       610        620        630        640        650        660 
ASANSLESLP SACTGEESLS MLQLLYLTNN LLTDQCIPVL VGHLHLRILH LANNQLQTFP 

       670        680        690        700        710        720 
ASKLNKLEQL EELNLSGNKL KTIPTTIANC KRLHTLVAHS NNISIFPEIL QLPQIQFVDL 

       730        740        750        760        770        780 
SCNDLTEILI PEALPATLQD LDLTGNTNLV LEHKTLDIFS HITTLKIDQK PLPTTDSTVT 

       790        800        810        820        830        840 
STFWSHGLAE MAGQRNKLCV SALAMDSFAE GVGAVYGMFD GDRNEELPRL LQCTMADVLL 

       850        860        870        880        890        900 
EEVQQSTNDT VFMANTFLVS HRKLGMAGQK LGSSALLCYI RPDTADPASS FSLTVANVGT 

       910        920        930        940        950        960 
CQAVLCRGGK PVPLSKVFSL EQDPEEAQRV KDQKAIITED NKVNGVTCCT RMLGCTYLYP 

       970        980        990       1000       1010       1020 
WILPKPHISS TPLTIQDELL ILGNKALWEH LSYTEAVNAV RHVQDPLAAA KKLCTLAQSY 

      1030       1040       1050       1060       1070       1080 
GCQDNVGAMV VYLNIGEEGC TCEMNGLTLP GPVGFASTTT IKDAPKPATP SSSSGIASEF 

      1090       1100       1110       1120       1130       1140 
SSEMSTSEVS SEVGSTASDE HNAGGLDTAL LPRPERRCSL HPTPTSGLFQ RQPSSATFSS 

      1150       1160       1170       1180       1190       1200 
NQSDNGLDSD DDQPVEGVIT NGSKVEVEVD IHCCRGRDLE NSPPLIESSP TLCSEEHARG 

      1210       1220       1230       1240       1250       1260 
SCFGIRRQNS VNSGMLLPMS KDRMELQKSP STSCLYGKKL SNGSIVPLED SLNLIEVATE 

      1270       1280       1290       1300       1310       1320 
VPKRKTGYFA APTQMEPEDQ FVVPHDLEEE VKEQMKQHQD SRLEPEPHEE DRTEPPEEFD 


TAL 

« Hide

Isoform 2 [UniParc].

Checksum: D639027D022AFED9
Show »

FASTA956107,079
Isoform 3 [UniParc].

Checksum: DC706C3744570432
Show »

FASTA1,256139,394

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[2]Ohara O., Nagase T., Kikuno R.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Retina.
[4]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
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 1).
[6]"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] OF 1-423 (ISOFORMS 1/2/3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 639-1323 (ISOFORM 2).
Tissue: Amygdala and Placenta.
[7]"PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms."
Brognard J., Sierecki E., Gao T., Newton A.C.
Mol. Cell 25:917-931(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AKT1 AND AKT3.
[8]"The phosphatase PHLPP controls the cellular levels of protein kinase C."
Gao T., Brognard J., Newton A.C.
J. Biol. Chem. 283:6300-6311(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PRKCB.
[9]"Loss of PHLPP expression in colon cancer: role in proliferation and tumorigenesis."
Liu J., Weiss H.L., Rychahou P., Jackson L.N., Evers B.M., Gao T.
Oncogene 28:994-1004(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB023148 mRNA. Translation: BAA76775.2. Different initiation.
BX647823 mRNA. No translation available.
AC009097 Genomic DNA. No translation available.
BC129927 mRNA. Translation: AAI29928.1.
AK001854 mRNA. Translation: BAA91943.1. Different initiation.
AK124678 mRNA. Translation: BAC85924.1.
CCDSCCDS32479.1. [Q6ZVD8-1]
RefSeqNP_001275932.1. NM_001289003.1. [Q6ZVD8-3]
NP_055835.2. NM_015020.3. [Q6ZVD8-1]
UniGeneHs.709458.

3D structure databases

ProteinModelPortalQ6ZVD8.
SMRQ6ZVD8. Positions 251-773, 797-1033.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116674. 13 interactions.
IntActQ6ZVD8. 14 interactions.
MINTMINT-4781843.
STRING9606.ENSP00000348611.

Chemistry

BindingDBQ6ZVD8.
ChEMBLCHEMBL1275209.

PTM databases

PhosphoSiteQ6ZVD8.

Polymorphism databases

DMDM116242711.

Proteomic databases

MaxQBQ6ZVD8.
PaxDbQ6ZVD8.
PRIDEQ6ZVD8.

Protocols and materials databases

DNASU23035.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356272; ENSP00000348611; ENSG00000040199. [Q6ZVD8-1]
ENST00000360429; ENSP00000353610; ENSG00000040199. [Q6ZVD8-2]
ENST00000393524; ENSP00000377159; ENSG00000040199. [Q6ZVD8-3]
ENST00000568954; ENSP00000457991; ENSG00000040199. [Q6ZVD8-1]
GeneID23035.
KEGGhsa:23035.
UCSCuc002fax.3. human. [Q6ZVD8-1]
uc010cgf.3. human. [Q6ZVD8-3]

Organism-specific databases

CTD23035.
GeneCardsGC16M071674.
H-InvDBHIX0013215.
HIX0173315.
HGNCHGNC:29149. PHLPP2.
HPAHPA048598.
MIM611066. gene.
neXtProtNX_Q6ZVD8.
PharmGKBPA165450496.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000115529.
InParanoidQ6ZVD8.
KOK16340.
PhylomeDBQ6ZVD8.
TreeFamTF315993.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ6ZVD8.
BgeeQ6ZVD8.
CleanExHS_PHLPPL.
GenevestigatorQ6ZVD8.

Family and domain databases

Gene3D3.60.40.10. 1 hit.
InterProIPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR001932. PP2C-like_dom.
[Graphical view]
PfamPF00560. LRR_1. 2 hits.
PF13855. LRR_8. 2 hits.
PF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00369. LRR_TYP. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. SSF81606. 1 hit.
PROSITEPS51450. LRR. 18 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPHLPPL.
GenomeRNAi23035.
NextBio44034.
PROQ6ZVD8.
SOURCESearch...

Entry information

Entry namePHLP2_HUMAN
AccessionPrimary (citable) accession number: Q6ZVD8
Secondary accession number(s): A1L374, Q9NV17, Q9Y2E3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 107 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 chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM