Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein phosphatase 1F

Gene

PPM1F

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

Functioni

Dephosphorylates and concomitantly deactivates CaM-kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis.

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi198 – 1981Manganese 1By similarity
Metal bindingi198 – 1981Manganese 2By similarity
Metal bindingi199 – 1991Manganese 1; via carbonyl oxygenBy similarity
Metal bindingi360 – 3601Manganese 2By similarity
Metal bindingi404 – 4041Manganese 2By similarity

GO - Molecular functioni

  1. calmodulin-dependent protein phosphatase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. phosphatase activity Source: UniProtKB
  4. protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. cellular response to drug Source: UniProtKB
  2. histone dephosphorylation Source: Ensembl
  3. intrinsic apoptotic signaling pathway Source: UniProtKB
  4. negative regulation of peptidyl-serine phosphorylation Source: UniProtKB
  5. negative regulation of protein kinase activity Source: UniProtKB
  6. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
  7. negative regulation of transcription, DNA-templated Source: UniProtKB
  8. peptidyl-threonine dephosphorylation Source: UniProtKB
  9. positive regulation of cell-substrate adhesion Source: UniProtKB
  10. positive regulation of chemotaxis Source: UniProtKB
  11. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  12. positive regulation of epithelial cell migration Source: UniProtKB
  13. positive regulation of focal adhesion assembly Source: UniProtKB
  14. positive regulation of gene expression Source: UniProtKB
  15. positive regulation of growth Source: UniProtKB
  16. positive regulation of stress fiber assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 1F (EC:3.1.3.16)
Alternative name(s):
Ca(2+)/calmodulin-dependent protein kinase phosphatase
Short name:
CaM-kinase phosphatase
Short name:
CaMKPase
Partner of PIX 2
Protein fem-2 homolog
Short name:
hFem-2
Gene namesi
Name:PPM1F
Synonyms:KIAA0015, POPX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:19388. PPM1F.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. perinuclear region of cytoplasm Source: Ensembl
  3. protein complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134935566.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Protein phosphatase 1FPRO_0000057758Add
BLAST

Proteomic databases

MaxQBiP49593.
PaxDbiP49593.
PeptideAtlasiP49593.
PRIDEiP49593.

2D gel databases

OGPiP49593.

PTM databases

DEPODiP49593.
PhosphoSiteiP49593.

Expressioni

Gene expression databases

BgeeiP49593.
CleanExiHS_PPM1F.
ExpressionAtlasiP49593. baseline and differential.
GenevestigatoriP49593.

Organism-specific databases

HPAiHPA030989.
HPA030990.

Interactioni

Subunit structurei

Associates with FEM1B.

Binary interactionsi

WithEntry#Exp.IntActNotes
Camkk2Q8C0783EBI-719945,EBI-937199From a different organism.
DIAPH1O606103EBI-719945,EBI-3959709
FEM1BQ9UK732EBI-719945,EBI-310482

Protein-protein interaction databases

BioGridi115005. 10 interactions.
IntActiP49593. 10 interactions.
MINTiMINT-1397077.
STRINGi9606.ENSP00000263212.

Structurei

3D structure databases

ProteinModelPortaliP49593.
SMRiP49593. Positions 84-445.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini156 – 413258PPM-type phosphatasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi101 – 1077Poly-Glu

Sequence similaritiesi

Belongs to the PP2C family.Curated
Contains 1 PPM-type phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0631.
GeneTreeiENSGT00740000114971.
HOGENOMiHOG000232094.
HOVERGENiHBG053656.
InParanoidiP49593.
KOiK17502.
OMAiGDVFQKP.
OrthoDBiEOG7D2FDH.
PhylomeDBiP49593.
TreeFamiTF317617.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P49593-1) [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
MSSGAPQKSS PMASGAEETP GFLDTLLQDF PALLNPEDPL PWKAPGTVLS
60 70 80 90 100
QEEVEGELAE LAMGFLGSRK APPPLAAALA HEAVSQLLQT DLSEFRKLPR
110 120 130 140 150
EEEEEEEDDD EEEKAPVTLL DAQSLAQSFF NRLWEVAGQW QKQVPLAARA
160 170 180 190 200
SQRQWLVSIH AIRNTRRKME DRHVSLPSFN QLFGLSDPVN RAYFAVFDGH
210 220 230 240 250
GGVDAARYAA VHVHTNAARQ PELPTDPEGA LREAFRRTDQ MFLRKAKRER
260 270 280 290 300
LQSGTTGVCA LIAGATLHVA WLGDSQVILV QQGQVVKLME PHRPERQDEK
310 320 330 340 350
ARIEALGGFV SHMDCWRVNG TLAVSRAIGD VFQKPYVSGE ADAASRALTG
360 370 380 390 400
SEDYLLLACD GFFDVVPHQE VVGLVQSHLT RQQGSGLRVA EELVAAARER
410 420 430 440 450
GSHDNITVMV VFLRDPQELL EGGNQGEGDP QAEGRRQDLP SSLPEPETQA

PPRS
Length:454
Mass (Da):49,831
Last modified:November 1, 2002 - v3
Checksum:i2B49262333D4C9CF
GO
Isoform 2 (identifier: P49593-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MSSGAPQKSSPMASG → MGLCPSTRETAPPAV
     16-119: Missing.

Note: No experimental confirmation available.

Show »
Length:350
Mass (Da):38,518
Checksum:i3762283304FF2BA8
GO

Sequence cautioni

The sequence BAA02803.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021G → D in AAL15579 (PubMed:11559703).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321R → C.
Corresponds to variant rs9610645 [ dbSNP | Ensembl ].
VAR_050620
Natural varianti296 – 2961R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036520
Natural varianti417 – 4171Q → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_036521
Natural varianti420 – 4201L → R.1 Publication
Corresponds to variant rs2070507 [ dbSNP | Ensembl ].
VAR_024580

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515MSSGA…PMASG → MGLCPSTRETAPPAV in isoform 2. 1 PublicationVSP_056483Add
BLAST
Alternative sequencei16 – 119104Missing in isoform 2. 1 PublicationVSP_056484Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305840 mRNA. Translation: AAL15579.1.
AF520615 mRNA. Translation: AAM76059.1.
D13640 mRNA. Translation: BAA02803.2. Different initiation.
AK291628 mRNA. Translation: BAF84317.1.
AK294557 mRNA. Translation: BAH11809.1.
AP000555 Genomic DNA. No translation available.
D86995 Genomic DNA. No translation available.
D87012 Genomic DNA. No translation available.
D87019 Genomic DNA. No translation available.
CCDSiCCDS13796.1. [P49593-1]
RefSeqiNP_055449.1. NM_014634.3. [P49593-1]
UniGeneiHs.112728.

Genome annotation databases

EnsembliENST00000263212; ENSP00000263212; ENSG00000100034. [P49593-1]
GeneIDi9647.
KEGGihsa:9647.
UCSCiuc002zvp.2. human. [P49593-1]

Polymorphism databases

DMDMi24638458.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305840 mRNA. Translation: AAL15579.1.
AF520615 mRNA. Translation: AAM76059.1.
D13640 mRNA. Translation: BAA02803.2. Different initiation.
AK291628 mRNA. Translation: BAF84317.1.
AK294557 mRNA. Translation: BAH11809.1.
AP000555 Genomic DNA. No translation available.
D86995 Genomic DNA. No translation available.
D87012 Genomic DNA. No translation available.
D87019 Genomic DNA. No translation available.
CCDSiCCDS13796.1. [P49593-1]
RefSeqiNP_055449.1. NM_014634.3. [P49593-1]
UniGeneiHs.112728.

3D structure databases

ProteinModelPortaliP49593.
SMRiP49593. Positions 84-445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115005. 10 interactions.
IntActiP49593. 10 interactions.
MINTiMINT-1397077.
STRINGi9606.ENSP00000263212.

PTM databases

DEPODiP49593.
PhosphoSiteiP49593.

Polymorphism databases

DMDMi24638458.

2D gel databases

OGPiP49593.

Proteomic databases

MaxQBiP49593.
PaxDbiP49593.
PeptideAtlasiP49593.
PRIDEiP49593.

Protocols and materials databases

DNASUi9647.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263212; ENSP00000263212; ENSG00000100034. [P49593-1]
GeneIDi9647.
KEGGihsa:9647.
UCSCiuc002zvp.2. human. [P49593-1]

Organism-specific databases

CTDi9647.
GeneCardsiGC22M022273.
H-InvDBHIX0027933.
HGNCiHGNC:19388. PPM1F.
HPAiHPA030989.
HPA030990.
neXtProtiNX_P49593.
PharmGKBiPA134935566.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0631.
GeneTreeiENSGT00740000114971.
HOGENOMiHOG000232094.
HOVERGENiHBG053656.
InParanoidiP49593.
KOiK17502.
OMAiGDVFQKP.
OrthoDBiEOG7D2FDH.
PhylomeDBiP49593.
TreeFamiTF317617.

Miscellaneous databases

ChiTaRSiPPM1F. human.
GeneWikiiPPM1F.
GenomeRNAii9647.
NextBioi35478962.
PROiP49593.

Gene expression databases

BgeeiP49593.
CleanExiHS_PPM1F.
ExpressionAtlasiP49593. baseline and differential.
GenevestigatoriP49593.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Caenorhabditis elegans sex-determining protein fem-2 and its human homologue, hFEM-2, are Ca2+/calmodulin-dependent protein kinase phosphatases that promote apoptosis."
    Tan K.M.L., Chan S.-L., Tan K.O., Yu V.C.
    J. Biol. Chem. 276:44193-44202(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH FEM1B.
  2. "The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family."
    Koh C.-G., Tan E.-J., Manser E., Lim L.
    Curr. Biol. 12:317-321(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
    Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
    DNA Res. 1:27-35(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ARG-420.
    Tissue: Amygdala and Placenta.
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-296 AND LYS-417.

Entry informationi

Entry nameiPPM1F_HUMAN
AccessioniPrimary (citable) accession number: P49593
Secondary accession number(s): A8K6G3, B7Z2C3, Q96PM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 1, 2002
Last modified: April 1, 2015
This is version 142 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 22
    Human chromosome 22: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.