Skip Header

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

UniProtKB - Q08209 (PP2BA_HUMAN)

(max 400 entries)x

Your basket is currently empty. i

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform

Gene

PPP3CA

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

Functioni

Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca2+-mediated signals (PubMed:15671020, PubMed:18838687, PubMed:19154138, PubMed:23468591). Many of the substrates contain a PxIxIT motif and/or a LxVP motif (PubMed:17498738, PubMed:17502104, PubMed:23468591, PubMed:27974827, PubMed:22343722). In response to increased Ca2+ levels, dephosphorylates and activates phosphatase SSH1 which results in cofilin dephosphorylation (PubMed:15671020). In response to increased Ca2+ levels following mitochondrial depolarization, dephosphorylates DNM1L inducing DNM1L translocation to the mitochondrion (PubMed:18838687). Dephosphorylates heat shock protein HSPB1 (By similarity). Dephosphorylates and activates transcription factor NFATC1 (PubMed:19154138). In response to increased Ca2+ levels, regulates NFAT-mediated transcription probably by dephosphorylating NFAT and promoting its nuclear translocation (PubMed:26248042). Dephosphorylates and inactivates transcription factor ELK1 (PubMed:19154138). Dephosphorylates DARPP32 (PubMed:19154138).By similarity9 Publications

Miscellaneous

Although African swine fever virus infects pigs and not humans, human PPP3CA has been used for the crystallization. PPP3CA interacts with African swine fever virus Mal-047/A238L (via PKIIIT and FLCVK motifs); the interaction does not block catalytic activity per se but inhibits PPP3CA function by blocking the access to the two substrate recognition sites.1 Publication

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication4 Publications

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Activated by Ca2+-bound calmodulin following an increase in intracellular Ca2+. At low Ca2+ concentrations, the catalytic subunit (also known as calcineurin A) is inactive and is bound to the regulatory subunit (also known as calcineurin B) in which only two high-affinity binding sites are occupied by Ca2+. In response to elevated calcium levels, the occupancy of the low-affinity sites on calcineurin B by Ca2+ causes a conformational change of the C-terminal regulatory domain of calcineurin A, resulting in the exposure of the calmodulin-binding domain and in the partial activation of calcineurin A. The subsequent binding of Ca2+-bound calmodulin leads to the displacement of the autoinhibitory domain from the active site and possibly of the autoinhibitory segment from the substrate binding site which fully activates calcineurin A. Inhibited by immunosuppressant drug FK506 (tacrolimus) in complex with FKBP12 and also by immunosuppressant drug cyclosporin A (CsA) in complex with PPIA/cyclophilin A; the inhibition is Ca2+-dependent (PubMed:26248042).By similarity1 Publication

Kineticsi

  1. KM=2.04 µM for NFATC11 Publication
  2. KM=2.22 µM for DARPP321 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi90IronCombined sources6 Publications1
    Metal bindingi92Iron; via tele nitrogenCombined sources6 Publications1
    Metal bindingi118IronCombined sources6 Publications1
    Metal bindingi118ZincCombined sources6 Publications1
    Metal bindingi150ZincCombined sources6 Publications1
    Active sitei151Proton donor1 Publication1
    Metal bindingi199Zinc; via tele nitrogenCombined sources6 Publications1
    Metal bindingi281Zinc; via pros nitrogenCombined sources6 Publications1

    GO - Molecular functioni

    • calcium ion binding Source: UniProtKB
    • calmodulin binding Source: UniProtKB
    • calmodulin-dependent protein phosphatase activity Source: UniProtKB
    • cyclosporin A binding Source: UniProtKB
    • drug binding Source: UniProtKB
    • enzyme binding Source: UniProtKB
    • protein dimerization activity Source: UniProtKB
    • protein heterodimerization activity Source: Ensembl
    • protein serine/threonine phosphatase activity Source: UniProtKB
    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

    Keywordsi

    Molecular functionCalmodulin-binding, Hydrolase, Protein phosphatase
    LigandIron, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiR-HSA-180024 DARPP-32 events
    R-HSA-2025928 Calcineurin activates NFAT
    R-HSA-2871809 FCERI mediated Ca+2 mobilization
    R-HSA-4086398 Ca2+ pathway
    R-HSA-5607763 CLEC7A (Dectin-1) induces NFAT activation
    SIGNORiQ08209

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC:3.1.3.161 Publication4 Publications)
    Alternative name(s):
    CAM-PRP catalytic subunit
    Calmodulin-dependent calcineurin A subunit alpha isoform
    Gene namesi
    Name:PPP3CAImported
    Synonyms:CALNA, CNA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    Proteomesi
    • UP000005640 Componenti: Chromosome 4

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000138814.16
    HGNCiHGNC:9314 PPP3CA
    MIMi114105 gene
    neXtProtiNX_Q08209

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Epileptic encephalopathy, infantile or early childhood, 1 (IECEE1)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. IECEE1 is an autosomal dominant condition with onset of seizures between the first weeks and first years of life.
    See also OMIM:617711
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_08034892H → R in IECEE1; unknown pathological significance. 1 Publication1
    Natural variantiVAR_080349281H → Q in IECEE1; unknown pathological significance. 1 Publication1
    Natural variantiVAR_080350282E → K in IECEE1; unknown pathological significance. 1 Publication1
    Natural variantiVAR_080351445 – 521Missing in IECEE1; unknown pathological significance. 1 PublicationAdd BLAST77
    Natural variantiVAR_080352447A → T in IECEE1; unknown pathological significance. 1 Publication1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi288Y → F: Partial loss of Ca(2+)-mediated transcription factor NFAT activation; when associated with F-341. 1 Publication1
    Mutagenesisi288Y → N or A: Loss of Ca(2+)-mediated transcription factor NFAT activation; when associated with F-341. 1 Publication1
    Mutagenesisi328 – 332Missing : Loss of Ca(2+)-mediated transcription factor NFAT activation; when associated with F-341. 1 Publication5
    Mutagenesisi341Y → F: Resistant to cyclosporin A-mediated inhibition. Loss of Ca(2+)-mediated transcription factor NFAT activation; when associated with N-288, A-228 or 328-V--R-332 DEL. Partial loss in Ca(2+)-mediated transcription factor NFAT activation; when associated with F-288. 1 Publication1

    Keywords - Diseasei

    Disease mutation, Epilepsy

    Organism-specific databases

    DisGeNETi5530
    MalaCardsiPPP3CA
    MIMi617711 phenotype
    OpenTargetsiENSG00000138814
    PharmGKBiPA33678

    Chemistry databases

    ChEMBLiCHEMBL4445
    DrugBankiDB08231 MYRISTIC ACID

    Polymorphism and mutation databases

    BioMutaiPPP3CA
    DMDMi1352673

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00000588222 – 521Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoformAdd BLAST520

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylserineCombined sources1
    Modified residuei224Nitrated tyrosineBy similarity1
    Modified residuei469PhosphoserineBy similarity1
    Modified residuei492PhosphoserineCombined sources1

    Keywords - PTMi

    Acetylation, Nitration, Phosphoprotein

    Proteomic databases

    EPDiQ08209
    MaxQBiQ08209
    PaxDbiQ08209
    PeptideAtlasiQ08209
    PRIDEiQ08209
    ProteomicsDBi58579
    58580 [Q08209-2]
    58581 [Q08209-3]

    PTM databases

    DEPODiQ08209
    iPTMnetiQ08209
    PhosphoSitePlusiQ08209
    SwissPalmiQ08209

    Miscellaneous databases

    PMAP-CutDBiQ08209

    Expressioni

    Gene expression databases

    BgeeiENSG00000138814
    CleanExiHS_PPP3CA
    ExpressionAtlasiQ08209 baseline and differential
    GenevisibleiQ08209 HS

    Organism-specific databases

    HPAiCAB018581
    HPA012778

    Interactioni

    Subunit structurei

    Forms a complex composed of a calmodulin-dependent catalytic subunit (also known as calcineurin A) and a regulatory Ca2+-binding subunit (also known as calcineurin B) (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591, PubMed:27974827). There are three catalytic subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded by separate genes (PPP3R1 and PPP3R2). In response to an increase in Ca2+ intracellular levels, forms a complex composed of PPP3CA/calcineurin A, calcineurin B and calmodulin (By similarity). Interacts (via calcineurin B binding domain) with regulatory subunit PPP3R1/calcineurin B (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591, PubMed:27974827). Interacts (via calmodulin-binding domain) with CALM1/calmodulin; the interaction depends on calmodulin binding to Ca2+ (PubMed:18384083, Ref. 28, PubMed:19404396, PubMed:25144868). Forms a complex composed of MYOZ2 and ACTN1 (By similarity). Within the complex interacts with MYOZ2 (PubMed:11114196). Interacts with MYOZ1 (PubMed:11114196). Interacts with MYOZ3 (PubMed:11842093). Interacts with CIB1; the interaction increases upon cardiomyocyte hypertrophy (By similarity). Interacts with CHP1 and CHP2 (By similarity). Interacts with CRTC2 (PubMed:15454081). Interacts with DNM1L; the interaction dephosphorylates DNM1L and promotes its translocation to mitochondria (PubMed:18838687). Interacts with CMYA5; this interaction represses calcineurin activity in muscle (By similarity). Interacts (constitutively active form) with SYNPO2 (PubMed:17923693). Interacts with scaffold protein AKAP5 (via IAIIIT motif); the interaction recruits PPP3CA to the plasma membrane following L-type Ca2+-channel activation (PubMed:22343722). Interacts with NFATC2 (PubMed:26248042). Interacts with RCAN3 (PubMed:26248042). Interacts with PPIA (PubMed:12218175, PubMed:12357034). Interacts with RCAN1 (PubMed:12809556).By similarity18 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei352Interaction with PxVP motif in substrate2 Publications1

    Binary interactionsi

    Show more details

    GO - Molecular functioni

    • calmodulin binding Source: UniProtKB
    • enzyme binding Source: UniProtKB
    • protein dimerization activity Source: UniProtKB
    • protein heterodimerization activity Source: Ensembl
    View the complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    BioGridi111522, 69 interactors
    ComplexPortaliCPX-1003 Calcineurin-Calmodulin complex, alpha-R1 variant
    CPX-1048 Calcineurin-Calmodulin complex, alpha-R2 variant
    CPX-1114 Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant
    CPX-674 Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant
    CORUMiQ08209
    DIPiDIP-6095N
    ELMiQ08209
    IntActiQ08209, 30 interactors
    MINTiQ08209
    STRINGi9606.ENSP00000378323

    Chemistry databases

    BindingDBiQ08209

    Structurei

    Secondary structure

    1521
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi13 – 15Combined sources3
    Helixi31 – 34Combined sources4
    Helixi43 – 51Combined sources9
    Helixi58 – 73Combined sources16
    Beta strandi77 – 81Combined sources5
    Beta strandi83 – 88Combined sources6
    Helixi95 – 105Combined sources11
    Turni108 – 110Combined sources3
    Beta strandi113 – 115Combined sources3
    Beta strandi120 – 123Combined sources4
    Helixi126 – 139Combined sources14
    Turni141 – 143Combined sources3
    Beta strandi144 – 146Combined sources3
    Helixi154 – 159Combined sources6
    Helixi162 – 169Combined sources8
    Helixi172 – 183Combined sources12
    Beta strandi188 – 191Combined sources4
    Turni192 – 194Combined sources3
    Beta strandi195 – 200Combined sources6
    Beta strandi206 – 208Combined sources3
    Helixi210 – 213Combined sources4
    Beta strandi218 – 220Combined sources3
    Beta strandi223 – 225Combined sources3
    Helixi226 – 232Combined sources7
    Turni237 – 240Combined sources4
    Beta strandi247 – 250Combined sources4
    Turni252 – 254Combined sources3
    Beta strandi255 – 260Combined sources6
    Helixi262 – 271Combined sources10
    Beta strandi276 – 279Combined sources4
    Beta strandi287 – 290Combined sources4
    Turni295 – 297Combined sources3
    Beta strandi298 – 306Combined sources9
    Helixi311 – 313Combined sources3
    Beta strandi319 – 325Combined sources7
    Beta strandi328 – 334Combined sources7
    Helixi344 – 346Combined sources3
    Helixi349 – 369Combined sources21
    Helixi396 – 409Combined sources14
    Helixi470 – 477Combined sources8
    Helixi478 – 481Combined sources4

    3D structure databases

    DisProtiDP00092
    ProteinModelPortaliQ08209
    SMRiQ08209
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ08209

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni56 – 340CatalyticCuratedAdd BLAST285
    Regioni327 – 336Interaction with PxIxIF motif in substrate5 Publications10
    Regioni341 – 369Calcineurin B binding6 PublicationsAdd BLAST29
    Regioni392 – 406Calmodulin-binding4 PublicationsAdd BLAST15
    Regioni407 – 414Autoinhibitory segmentBy similarity8
    Regioni465 – 487Autoinhibitory domain1 PublicationAdd BLAST23

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi307 – 311SAPNY motif1 Publication5

    Domaini

    The autoinhibitory domain prevents access to the catalytic site.By similarity
    The autoinhibitory segment prevents access to the substrate binding site.By similarity
    Possible isomerization of Pro-309 within the SAPNY motif triggers a conformation switch which affects the organization and thus accessibility of the active site and the substrate binding region (PxIxIF motif). The trans- to cis-transition may favor calcineurin A activation and substrate binding. The reverse cis- to trans-transition may be enhanced by peptidyl-prolyl isomerases such as PPIA.1 Publication

    Sequence similaritiesi

    Belongs to the PPP phosphatase family. PP-2B subfamily.Curated

    Phylogenomic databases

    eggNOGiKOG0375 Eukaryota
    COG0639 LUCA
    GeneTreeiENSGT00530000063087
    HOGENOMiHOG000172699
    HOVERGENiHBG002819
    InParanoidiQ08209
    KOiK04348
    OMAiLWSLKIW
    OrthoDBiEOG091G094R
    PhylomeDBiQ08209
    TreeFamiTF105557

    Family and domain databases

    Gene3Di3.60.21.10, 1 hit
    InterProiView protein in InterPro
    IPR004843 Calcineurin-like_PHP_ApaH
    IPR029052 Metallo-depent_PP-like
    IPR006186 Ser/Thr-sp_prot-phosphatase
    PfamiView protein in Pfam
    PF00149 Metallophos, 1 hit
    PRINTSiPR00114 STPHPHTASE
    SMARTiView protein in SMART
    SM00156 PP2Ac, 1 hit
    PROSITEiView protein in PROSITE
    PS00125 SER_THR_PHOSPHATASE, 1 hit

    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: Q08209-1) [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
    MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL 
            60         70         80         90        100
    MKEGRLEESV ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK 
           110        120        130        140        150
    LFEVGGSPAN TRYLFLGDYV DRGYFSIECV LYLWALKILY PKTLFLLRGN 
           160        170        180        190        200
    HECRHLTEYF TFKQECKIKY SERVYDACMD AFDCLPLAAL MNQQFLCVHG 
           210        220        230        240        250
    GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG NEKTQEHFTH 
           260        270        280        290        300
    NTVRGCSYFY SYPAVCEFLQ HNNLLSILRA HEAQDAGYRM YRKSQTTGFP 
           310        320        330        340        350
    SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF 
           360        370        380        390        400
    TWSLPFVGEK VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI 
           410        420        430        440        450
    RAIGKMARVF SVLREESESV LTLKGLTPTG MLPSGVLSGG KQTLQSATVE 
           460        470        480        490        500
    AIEADEAIKG FSPQHKITSF EEAKGLDRIN ERMPPRRDAM PSDANLNSIN 
           510        520 
    KALTSETNGT DSNGSNSSNI Q
    Length:521
    Mass (Da):58,688
    Last modified:February 1, 1996 - v1
    Checksum:i16480D62DDBF1F40
    GO
    Isoform 2 (identifier: Q08209-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         448-457: Missing.

    Show »
    Length:511
    Mass (Da):57,659
    Checksum:iB1E98CC0D6034CCC
    GO
    Isoform 3 (identifier: Q08209-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         318-359: Missing.
         448-457: Missing.

    Show »
    Length:469
    Mass (Da):52,672
    Checksum:iA3365471746633B7
    GO
    Isoform 4 (identifier: Q08209-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         87-318: Missing.

    Show »
    Length:289
    Mass (Da):31,736
    Checksum:iB3AEE20F6A4F19B7
    GO
    Isoform 5 (identifier: Q08209-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         20-86: Missing.

    Show »
    Length:454
    Mass (Da):51,245
    Checksum:iE28DCB758984D380
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_08034892H → R in IECEE1; unknown pathological significance. 1 Publication1
    Natural variantiVAR_080349281H → Q in IECEE1; unknown pathological significance. 1 Publication1
    Natural variantiVAR_080350282E → K in IECEE1; unknown pathological significance. 1 Publication1
    Natural variantiVAR_080351445 – 521Missing in IECEE1; unknown pathological significance. 1 PublicationAdd BLAST77
    Natural variantiVAR_080352447A → T in IECEE1; unknown pathological significance. 1 Publication1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_05446720 – 86Missing in isoform 5. 1 PublicationAdd BLAST67
    Alternative sequenceiVSP_04775587 – 318Missing in isoform 4. 1 PublicationAdd BLAST232
    Alternative sequenceiVSP_043378318 – 359Missing in isoform 3. 1 PublicationAdd BLAST42
    Alternative sequenceiVSP_018562448 – 457Missing in isoform 2 and isoform 3. 3 Publications10

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		L14778 mRNA Translation: AAA02631.1
    EU192652 mRNA Translation: ABW74484.1
    EU192653 mRNA Translation: ABW74485.1
    AY904364 mRNA Translation: AAY17314.1
    AK290532 mRNA Translation: BAF83221.1
    AL353950 mRNA Translation: CAB89253.1
    AB451338 mRNA Translation: BAG70152.1
    AB451487 mRNA Translation: BAG70301.1
    AC092671 Genomic DNA No translation available.
    AP001816 Genomic DNA No translation available.
    AP001870 Genomic DNA No translation available.
    AP001939 Genomic DNA No translation available.
    CH471057 Genomic DNA Translation: EAX06125.1
    CH471057 Genomic DNA Translation: EAX06124.1
    BC025714 mRNA Translation: AAH25714.1
    CCDSiCCDS34037.1 [Q08209-1]
    CCDS47113.1 [Q08209-3]
    CCDS47114.1 [Q08209-2]
    PIRiS35067
    RefSeqiNP_000935.1, NM_000944.4 [Q08209-1]
    NP_001124163.1, NM_001130691.1 [Q08209-2]
    NP_001124164.1, NM_001130692.1 [Q08209-3]
    UniGeneiHs.435512

    Genome annotation databases

    EnsembliENST00000323055; ENSP00000320580; ENSG00000138814 [Q08209-3]
    ENST00000394853; ENSP00000378322; ENSG00000138814 [Q08209-2]
    ENST00000394854; ENSP00000378323; ENSG00000138814 [Q08209-1]
    ENST00000512215; ENSP00000422781; ENSG00000138814 [Q08209-4]
    GeneIDi5530
    KEGGihsa:5530
    UCSCiuc003hvu.3 human [Q08209-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Similar proteinsi

    Entry informationi

    Entry nameiPP2BA_HUMAN
    AccessioniPrimary (citable) accession number: Q08209
    Secondary accession number(s): A1A441
    , A8K3B7, A8W6Z7, A8W6Z8, B5BUA2, Q8TAW9
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: July 18, 2018
    This is version 196 of the entry and version 1 of the sequence. See 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health