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P46013

- KI67_HUMAN

UniProt

P46013 - KI67_HUMAN

Protein

Antigen KI-67

Gene

MKI67

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (28 Nov 2006)
      Previous versions | rss
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    Functioni

    Thought to be required for maintaining cell proliferation.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi3034 – 30418ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein C-terminus binding Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: UniProtKB
    2. cellular response to heat Source: Ensembl
    3. DNA metabolic process Source: Ensembl
    4. hyaluronan metabolic process Source: Ensembl
    5. meiotic nuclear division Source: Ensembl
    6. organ regeneration Source: Ensembl
    7. response to organic cyclic compound Source: Ensembl

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Antigen KI-67
    Gene namesi
    Name:MKI67
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:7107. MKI67.

    Subcellular locationi

    Nucleus 1 Publication. Nucleusnucleolus 1 Publication. Chromosome 1 Publication
    Note: Predominantly localized in the G1 phase in the perinucleolar region, in the later phases it is also detected throughout the nuclear interior, being predominantly localized in the nuclear matrix. In mitosis, it is present on all chromosomes.

    GO - Cellular componenti

    1. chromosome, centromeric region Source: Ensembl
    2. condensed chromosome Source: Ensembl
    3. cytoplasm Source: Ensembl
    4. membrane Source: UniProtKB
    5. nucleolus Source: UniProtKB
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30825.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 32563256Antigen KI-67PRO_0000084301Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei125 – 1251Phosphoserine1 Publication
    Modified residuei264 – 2641Phosphoserine1 Publication
    Modified residuei308 – 3081Phosphoserine4 Publications
    Modified residuei328 – 3281Phosphothreonine2 Publications
    Modified residuei347 – 3471Phosphothreonine1 Publication
    Modified residuei352 – 3521Phosphoserine1 Publication
    Modified residuei357 – 3571Phosphoserine6 Publications
    Modified residuei401 – 4011Phosphothreonine1 Publication
    Modified residuei579 – 5791Phosphoserine6 Publications
    Modified residuei584 – 5841Phosphoserine4 Publications
    Modified residuei648 – 6481Phosphoserine4 Publications
    Modified residuei761 – 7611Phosphothreonine1 Publication
    Modified residuei859 – 8591Phosphoserine1 Publication
    Modified residuei1017 – 10171Phosphothreonine1 Publication
    Modified residuei1071 – 10711Phosphoserine1 Publication
    Modified residuei1091 – 10911Phosphothreonine2 Publications
    Modified residuei1098 – 10981Phosphoserine3 Publications
    Modified residuei1111 – 11111Phosphothreonine1 Publication
    Modified residuei1131 – 11311Phosphoserine5 Publications
    Modified residuei1139 – 11391Phosphothreonine1 Publication
    Modified residuei1142 – 11421Phosphoserine1 Publication
    Modified residuei1167 – 11671Phosphothreonine1 Publication
    Modified residuei1193 – 11931Phosphothreonine1 Publication
    Modified residuei1207 – 12071Phosphoserine2 Publications
    Modified residuei1233 – 12331Phosphothreonine2 Publications
    Modified residuei1253 – 12531Phosphoserine1 Publication
    Modified residuei1256 – 12561Phosphoserine1 Publication
    Modified residuei1261 – 12611Phosphothreonine1 Publication
    Modified residuei1298 – 12981Phosphothreonine1 Publication
    Modified residuei1315 – 13151Phosphothreonine2 Publications
    Modified residuei1327 – 13271Phosphothreonine3 Publications
    Modified residuei1329 – 13291Phosphoserine2 Publications
    Modified residuei1335 – 13351Phosphothreonine3 Publications
    Modified residuei1355 – 13551Phosphothreonine3 Publications
    Modified residuei1376 – 13761Phosphoserine1 Publication
    Modified residuei1383 – 13831Phosphothreonine1 Publication
    Modified residuei1496 – 14961Phosphoserine1 Publication
    Modified residuei1503 – 15031Phosphothreonine1 Publication
    Modified residuei1506 – 15061Phosphoserine1 Publication
    Modified residuei1540 – 15401Phosphothreonine1 Publication
    Modified residuei1552 – 15521Phosphotyrosine1 Publication
    Modified residuei1557 – 15571Phosphothreonine3 Publications
    Modified residuei1569 – 15691Phosphothreonine3 Publications
    Modified residuei1571 – 15711Phosphoserine2 Publications
    Modified residuei1639 – 16391N6-acetyllysine1 Publication
    Modified residuei1679 – 16791Phosphoserine4 Publications
    Modified residuei1689 – 16891Phosphoserine1 Publication
    Modified residuei1719 – 17191Phosphothreonine1 Publication
    Modified residuei1721 – 17211Phosphoserine1 Publication
    Modified residuei1740 – 17401Phosphoserine1 Publication
    Modified residuei1747 – 17471Phosphothreonine2 Publications
    Modified residuei1764 – 17641Phosphothreonine2 Publications
    Modified residuei1784 – 17841Phosphothreonine1 Publication
    Modified residuei1801 – 18011Phosphothreonine3 Publications
    Modified residuei1815 – 18151Phosphoserine1 Publication
    Modified residuei1841 – 18411Phosphothreonine1 Publication
    Modified residuei1861 – 18611Phosphoserine4 Publications
    Modified residuei1864 – 18641Phosphoserine1 Publication
    Modified residuei1869 – 18691Phosphothreonine1 Publication
    Modified residuei1897 – 18971Phosphothreonine1 Publication
    Modified residuei1923 – 19231Phosphothreonine3 Publications
    Modified residuei1937 – 19371Phosphoserine2 Publications
    Modified residuei1963 – 19631Phosphothreonine1 Publication
    Modified residuei1983 – 19831Phosphoserine2 Publications
    Modified residuei2005 – 20051N6-acetyllysine1 Publication
    Modified residuei2065 – 20651Phosphothreonine2 Publications
    Modified residuei2072 – 20721Phosphoserine3 Publications
    Modified residuei2085 – 20851Phosphothreonine2 Publications
    Modified residuei2105 – 21051Phosphoserine3 Publications
    Modified residuei2113 – 21131Phosphothreonine1 Publication
    Modified residuei2135 – 21351Phosphoserine1 Publication
    Modified residuei2203 – 22031Phosphothreonine1 Publication
    Modified residuei2223 – 22231Phosphoserine2 Publications
    Modified residuei2231 – 22311Phosphothreonine2 Publications
    Modified residuei2233 – 22331Phosphothreonine1 Publication
    Modified residuei2239 – 22391Phosphoserine2 Publications
    Modified residuei2268 – 22681Phosphothreonine1 Publication
    Modified residuei2285 – 22851Phosphothreonine2 Publications
    Modified residuei2325 – 23251Phosphothreonine2 Publications
    Modified residuei2328 – 23281Phosphothreonine1 Publication
    Modified residuei2333 – 23331Phosphothreonine1 Publication
    Modified residuei2344 – 23441Phosphoserine3 Publications
    Modified residuei2352 – 23521Phosphothreonine1 Publication
    Modified residuei2389 – 23891Phosphothreonine2 Publications
    Modified residuei2395 – 23951Phosphoserine2 Publications
    Modified residuei2406 – 24061Phosphothreonine5 Publications
    Modified residuei2420 – 24201Phosphoserine2 Publications
    Modified residuei2446 – 24461Phosphothreonine1 Publication
    Modified residuei2528 – 25281Phosphoserine3 Publications
    Modified residuei2588 – 25881Phosphoserine3 Publications
    Modified residuei2708 – 27081Phosphoserine4 Publications
    Modified residuei2827 – 28271Phosphoserine1 Publication
    Modified residuei2828 – 28281Phosphoserine1 Publication
    Modified residuei3041 – 30411Phosphoserine1 Publication
    Modified residuei3128 – 31281Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP46013.
    PaxDbiP46013.
    PRIDEiP46013.

    PTM databases

    PhosphoSiteiP46013.

    Expressioni

    Developmental stagei

    Expression of this antigen occurs preferentially during late G1, S, G2 and M phases of the cell cycle, while in cells in G0 phase the antigen cannot be detected.

    Gene expression databases

    BgeeiP46013.
    CleanExiHS_MKI67.
    GenevestigatoriP46013.

    Organism-specific databases

    HPAiCAB000058.
    HPA000451.
    HPA001164.

    Interactioni

    Subunit structurei

    Interacts with KIF15. Binds through the FHA domain to NIFK. Part of a complex composed at least of ASCL2, C11orf30/EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity.6 Publications

    Protein-protein interaction databases

    BioGridi110434. 23 interactions.
    DIPiDIP-28132N.
    IntActiP46013. 17 interactions.
    MINTiMINT-137995.
    STRINGi9606.ENSP00000357643.

    Structurei

    Secondary structure

    1
    3256
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 128
    Beta strandi15 – 217
    Beta strandi24 – 329
    Beta strandi35 – 384
    Beta strandi49 – 535
    Beta strandi58 – 603
    Beta strandi65 – 673
    Beta strandi80 – 823
    Beta strandi86 – 894
    Beta strandi94 – 996

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1R21NMR-A1-120[»]
    2AFFNMR-A1-120[»]
    ProteinModelPortaliP46013.
    SMRiP46013. Positions 1-100.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46013.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 7650FHAPROSITE-ProRule annotationAdd
    BLAST
    Repeati1000 – 11121131Add
    BLAST
    Repeati1122 – 12341132Add
    BLAST
    Repeati1244 – 13561133Add
    BLAST
    Repeati1366 – 14771124Add
    BLAST
    Repeati1487 – 15981125Add
    BLAST
    Repeati1608 – 17201136Add
    BLAST
    Repeati1730 – 18421137Add
    BLAST
    Repeati1851 – 19641148Add
    BLAST
    Repeati1974 – 20861139Add
    BLAST
    Repeati2096 – 220410910Add
    BLAST
    Repeati2214 – 232611311Add
    BLAST
    Repeati2335 – 244711312Add
    BLAST
    Repeati2457 – 256911313Add
    BLAST
    Repeati2579 – 268911114Add
    BLAST
    Repeati2699 – 280811015Add
    BLAST
    Repeati2818 – 292811116Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1000 – 2928192916 X 122 AA approximate repeatsAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FHA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000113223.
    HOVERGENiHBG006213.
    InParanoidiP46013.
    KOiK17582.
    OMAiQTPKEKA.
    OrthoDBiEOG76QFGJ.
    PhylomeDBiP46013.
    TreeFamiTF336000.

    Family and domain databases

    Gene3Di2.60.200.20. 1 hit.
    InterProiIPR000253. FHA_dom.
    IPR012568. K167R.
    IPR029334. PP1-bd.
    IPR008984. SMAD_FHA_domain.
    [Graphical view]
    PfamiPF00498. FHA. 1 hit.
    PF08065. K167R. 16 hits.
    PF15276. PP1_bind. 1 hit.
    [Graphical view]
    SMARTiSM00240. FHA. 1 hit.
    [Graphical view]
    SUPFAMiSSF49879. SSF49879. 1 hit.
    PROSITEiPS50006. FHA_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P46013-1) [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

    MWPTRRLVTI KRSGVDGPHF PLSLSTCLFG RGIECDIRIQ LPVVSKQHCK     50
    IEIHEQEAIL HNFSSTNPTQ VNGSVIDEPV RLKHGDVITI IDRSFRYENE 100
    SLQNGRKSTE FPRKIREQEP ARRVSRSSFS SDPDEKAQDS KAYSKITEGK 150
    VSGNPQVHIK NVKEDSTADD SKDSVAQGTT NVHSSEHAGR NGRNAADPIS 200
    GDFKEISSVK LVSRYGELKS VPTTQCLDNS KKNESPFWKL YESVKKELDV 250
    KSQKENVLQY CRKSGLQTDY ATEKESADGL QGETQLLVSR KSRPKSGGSG 300
    HAVAEPASPE QELDQNKGKG RDVESVQTPS KAVGASFPLY EPAKMKTPVQ 350
    YSQQQNSPQK HKNKDLYTTG RRESVNLGKS EGFKAGDKTL TPRKLSTRNR 400
    TPAKVEDAAD SATKPENLSS KTRGSIPTDV EVLPTETEIH NEPFLTLWLT 450
    QVERKIQKDS LSKPEKLGTT AGQMCSGLPG LSSVDINNFG DSINESEGIP 500
    LKRRRVSFGG HLRPELFDEN LPPNTPLKRG EAPTKRKSLV MHTPPVLKKI 550
    IKEQPQPSGK QESGSEIHVE VKAQSLVISP PAPSPRKTPV ASDQRRRSCK 600
    TAPASSSKSQ TEVPKRGGRK SGNLPSKRVS ISRSQHDILQ MICSKRRSGA 650
    SEANLIVAKS WADVVKLGAK QTQTKVIKHG PQRSMNKRQR RPATPKKPVG 700
    EVHSQFSTGH ANSPCTIIIG KAHTEKVHVP ARPYRVLNNF ISNQKMDFKE 750
    DLSGIAEMFK TPVKEQPQLT STCHIAISNS ENLLGKQFQG TDSGEEPLLP 800
    TSESFGGNVF FSAQNAAKQP SDKCSASPPL RRQCIRENGN VAKTPRNTYK 850
    MTSLETKTSD TETEPSKTVS TANRSGRSTE FRNIQKLPVE SKSEETNTEI 900
    VECILKRGQK ATLLQQRREG EMKEIERPFE TYKENIELKE NDEKMKAMKR 950
    SRTWGQKCAP MSDLTDLKSL PDTELMKDTA RGQNLLQTQD HAKAPKSEKG 1000
    KITKMPCQSL QPEPINTPTH TKQQLKASLG KVGVKEELLA VGKFTRTSGE 1050
    TTHTHREPAG DGKSIRTFKE SPKQILDPAA RVTGMKKWPR TPKEEAQSLE 1100
    DLAGFKELFQ TPGPSEESMT DEKTTKIACK SPPPESVDTP TSTKQWPKRS 1150
    LRKADVEEEF LALRKLTPSA GKAMLTPKPA GGDEKDIKAF MGTPVQKLDL 1200
    AGTLPGSKRQ LQTPKEKAQA LEDLAGFKEL FQTPGHTEEL VAAGKTTKIP 1250
    CDSPQSDPVD TPTSTKQRPK RSIRKADVEG ELLACRNLMP SAGKAMHTPK 1300
    PSVGEEKDII IFVGTPVQKL DLTENLTGSK RRPQTPKEEA QALEDLTGFK 1350
    ELFQTPGHTE EAVAAGKTTK MPCESSPPES ADTPTSTRRQ PKTPLEKRDV 1400
    QKELSALKKL TQTSGETTHT DKVPGGEDKS INAFRETAKQ KLDPAASVTG 1450
    SKRHPKTKEK AQPLEDLAGL KELFQTPVCT DKPTTHEKTT KIACRSQPDP 1500
    VDTPTSSKPQ SKRSLRKVDV EEEFFALRKR TPSAGKAMHT PKPAVSGEKN 1550
    IYAFMGTPVQ KLDLTENLTG SKRRLQTPKE KAQALEDLAG FKELFQTRGH 1600
    TEESMTNDKT AKVACKSSQP DPDKNPASSK RRLKTSLGKV GVKEELLAVG 1650
    KLTQTSGETT HTHTEPTGDG KSMKAFMESP KQILDSAASL TGSKRQLRTP 1700
    KGKSEVPEDL AGFIELFQTP SHTKESMTNE KTTKVSYRAS QPDLVDTPTS 1750
    SKPQPKRSLR KADTEEEFLA FRKQTPSAGK AMHTPKPAVG EEKDINTFLG 1800
    TPVQKLDQPG NLPGSNRRLQ TRKEKAQALE ELTGFRELFQ TPCTDNPTTD 1850
    EKTTKKILCK SPQSDPADTP TNTKQRPKRS LKKADVEEEF LAFRKLTPSA 1900
    GKAMHTPKAA VGEEKDINTF VGTPVEKLDL LGNLPGSKRR PQTPKEKAKA 1950
    LEDLAGFKEL FQTPGHTEES MTDDKITEVS CKSPQPDPVK TPTSSKQRLK 2000
    ISLGKVGVKE EVLPVGKLTQ TSGKTTQTHR ETAGDGKSIK AFKESAKQML 2050
    DPANYGTGME RWPRTPKEEA QSLEDLAGFK ELFQTPDHTE ESTTDDKTTK 2100
    IACKSPPPES MDTPTSTRRR PKTPLGKRDI VEELSALKQL TQTTHTDKVP 2150
    GDEDKGINVF RETAKQKLDP AASVTGSKRQ PRTPKGKAQP LEDLAGLKEL 2200
    FQTPICTDKP TTHEKTTKIA CRSPQPDPVG TPTIFKPQSK RSLRKADVEE 2250
    ESLALRKRTP SVGKAMDTPK PAGGDEKDMK AFMGTPVQKL DLPGNLPGSK 2300
    RWPQTPKEKA QALEDLAGFK ELFQTPGTDK PTTDEKTTKI ACKSPQPDPV 2350
    DTPASTKQRP KRNLRKADVE EEFLALRKRT PSAGKAMDTP KPAVSDEKNI 2400
    NTFVETPVQK LDLLGNLPGS KRQPQTPKEK AEALEDLVGF KELFQTPGHT 2450
    EESMTDDKIT EVSCKSPQPE SFKTSRSSKQ RLKIPLVKVD MKEEPLAVSK 2500
    LTRTSGETTQ THTEPTGDSK SIKAFKESPK QILDPAASVT GSRRQLRTRK 2550
    EKARALEDLV DFKELFSAPG HTEESMTIDK NTKIPCKSPP PELTDTATST 2600
    KRCPKTRPRK EVKEELSAVE RLTQTSGQST HTHKEPASGD EGIKVLKQRA 2650
    KKKPNPVEEE PSRRRPRAPK EKAQPLEDLA GFTELSETSG HTQESLTAGK 2700
    ATKIPCESPP LEVVDTTAST KRHLRTRVQK VQVKEEPSAV KFTQTSGETT 2750
    DADKEPAGED KGIKALKESA KQTPAPAASV TGSRRRPRAP RESAQAIEDL 2800
    AGFKDPAAGH TEESMTDDKT TKIPCKSSPE LEDTATSSKR RPRTRAQKVE 2850
    VKEELLAVGK LTQTSGETTH TDKEPVGEGK GTKAFKQPAK RKLDAEDVIG 2900
    SRRQPRAPKE KAQPLEDLAS FQELSQTPGH TEELANGAAD SFTSAPKQTP 2950
    DSGKPLKISR RVLRAPKVEP VGDVVSTRDP VKSQSKSNTS LPPLPFKRGG 3000
    GKDGSVTGTK RLRCMPAPEE IVEELPASKK QRVAPRARGK SSEPVVIMKR 3050
    SLRTSAKRIE PAEELNSNDM KTNKEEHKLQ DSVPENKGIS LRSRRQNKTE 3100
    AEQQITEVFV LAERIEINRN EKKPMKTSPE MDIQNPDDGA RKPIPRDKVT 3150
    ENKRCLRSAR QNESSQPKVA EESGGQKSAK VLMQNQKGKG EAGNSDSMCL 3200
    RSRKTKSQPA ASTLESKSVQ RVTRSVKRCA ENPKKAEDNV CVKKIRTRSH 3250
    RDSEDI 3256
    Length:3,256
    Mass (Da):358,694
    Last modified:November 28, 2006 - v2
    Checksum:i1332BC6C799AD64D
    GO
    Isoform Short (identifier: P46013-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         136-495: Missing.

    Show »
    Length:2,896
    Mass (Da):319,444
    Checksum:i4FACAA90AC686C72
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti619 – 6268RKSGNLPS → ERVATCLQ in CAA46519. (PubMed:8227122)Curated
    Sequence conflicti619 – 6268RKSGNLPS → ERVATCLQ in CAA46520. (PubMed:8227122)Curated
    Sequence conflicti2205 – 22051I → V in CAA46519. (PubMed:8227122)Curated
    Sequence conflicti2205 – 22051I → V in CAA46520. (PubMed:8227122)Curated
    Sequence conflicti2892 – 28932KL → NV in CAA46519. (PubMed:8227122)Curated
    Sequence conflicti2892 – 28932KL → NV in CAA46520. (PubMed:8227122)Curated
    Sequence conflicti3246 – 32461R → T in CAA46519. (PubMed:8227122)Curated
    Sequence conflicti3246 – 32461R → T in CAA46520. (PubMed:8227122)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti104 – 1041N → S.
    Corresponds to variant rs2071498 [ dbSNP | Ensembl ].
    VAR_029055
    Natural varianti238 – 2381W → R.
    Corresponds to variant rs7095325 [ dbSNP | Ensembl ].
    VAR_029056
    Natural varianti497 – 4971E → D.
    Corresponds to variant rs11016076 [ dbSNP | Ensembl ].
    VAR_029057
    Natural varianti574 – 5741Q → P.
    Corresponds to variant rs4471342 [ dbSNP | Ensembl ].
    VAR_029058
    Natural varianti631 – 6311I → L.
    Corresponds to variant rs997983 [ dbSNP | Ensembl ].
    VAR_024161
    Natural varianti832 – 8321R → W.
    Corresponds to variant rs34916904 [ dbSNP | Ensembl ].
    VAR_033995
    Natural varianti854 – 8541L → V.
    Corresponds to variant rs2240 [ dbSNP | Ensembl ].
    VAR_024162
    Natural varianti872 – 8721A → V.1 Publication
    Corresponds to variant rs2853344 [ dbSNP | Ensembl ].
    VAR_029059
    Natural varianti1042 – 10421G → S.
    Corresponds to variant rs2152143 [ dbSNP | Ensembl ].
    VAR_024163
    Natural varianti1120 – 11201T → S.
    Corresponds to variant rs11016074 [ dbSNP | Ensembl ].
    VAR_029060
    Natural varianti1247 – 12471T → I.
    Corresponds to variant rs4750685 [ dbSNP | Ensembl ].
    VAR_021838
    Natural varianti1403 – 14031E → V.
    Corresponds to variant rs3740423 [ dbSNP | Ensembl ].
    VAR_020047
    Natural varianti1470 – 14701L → W.1 Publication
    Corresponds to variant rs2853345 [ dbSNP | Ensembl ].
    VAR_029061
    Natural varianti1559 – 15591V → M.
    Corresponds to variant rs7918199 [ dbSNP | Ensembl ].
    VAR_029062
    Natural varianti1622 – 16221P → L.1 Publication
    Corresponds to variant rs2782871 [ dbSNP | Ensembl ].
    VAR_029063
    Natural varianti1849 – 18491T → A.1 Publication
    Corresponds to variant rs2782872 [ dbSNP | Ensembl ].
    VAR_029064
    Natural varianti1876 – 18761R → Q.
    Corresponds to variant rs11591817 [ dbSNP | Ensembl ].
    VAR_029065
    Natural varianti1951 – 19511L → I.
    Corresponds to variant rs34116632 [ dbSNP | Ensembl ].
    VAR_033996
    Natural varianti2101 – 21011I → T.
    Corresponds to variant rs11016073 [ dbSNP | Ensembl ].
    VAR_029066
    Natural varianti2337 – 23371T → N.
    Corresponds to variant rs7083622 [ dbSNP | Ensembl ].
    VAR_024164
    Natural varianti2363 – 23631N → S.
    Corresponds to variant rs7071768 [ dbSNP | Ensembl ].
    VAR_029067
    Natural varianti2607 – 26071R → H.
    Corresponds to variant rs34688192 [ dbSNP | Ensembl ].
    VAR_061671
    Natural varianti2608 – 26081P → L.
    Corresponds to variant rs1063535 [ dbSNP | Ensembl ].
    VAR_024165
    Natural varianti2649 – 26491R → H.
    Corresponds to variant rs12777740 [ dbSNP | Ensembl ].
    VAR_029068
    Natural varianti2720 – 27201T → P.
    Corresponds to variant rs1050767 [ dbSNP | Ensembl ].
    VAR_024166
    Natural varianti2760 – 27601D → G.
    Corresponds to variant rs10082391 [ dbSNP | Ensembl ].
    VAR_029069
    Natural varianti2786 – 27861R → Q.
    Corresponds to variant rs10764749 [ dbSNP | Ensembl ].
    VAR_029070
    Natural varianti2793 – 27931S → N.
    Corresponds to variant rs10082533 [ dbSNP | Ensembl ].
    VAR_029071
    Natural varianti2845 – 28451R → H.
    Corresponds to variant rs11016072 [ dbSNP | Ensembl ].
    VAR_029072
    Natural varianti2868 – 28681T → S.
    Corresponds to variant rs2071496 [ dbSNP | Ensembl ].
    VAR_024167
    Natural varianti2904 – 29041Q → R.
    Corresponds to variant rs11016071 [ dbSNP | Ensembl ].
    VAR_029073
    Natural varianti3097 – 30971N → D.1 Publication
    Corresponds to variant rs2798669 [ dbSNP | Ensembl ].
    VAR_029074
    Natural varianti3102 – 31021E → G.
    Corresponds to variant rs34750407 [ dbSNP | Ensembl ].
    VAR_033997
    Natural varianti3150 – 31501T → S.
    Corresponds to variant rs11106 [ dbSNP | Ensembl ].
    VAR_014858
    Natural varianti3217 – 32171K → E.
    Corresponds to variant rs8473 [ dbSNP | Ensembl ].
    VAR_014859

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei136 – 495360Missing in isoform Short. 1 PublicationVSP_004298Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65550 mRNA. Translation: CAA46519.1.
    X65551 mRNA. Translation: CAA46520.1.
    AL390236, AL355529 Genomic DNA. Translation: CAH73169.1.
    X94762 Genomic DNA. Translation: CAA64388.1.
    CCDSiCCDS53588.1. [P46013-2]
    CCDS7659.1. [P46013-1]
    PIRiA48666.
    RefSeqiNP_001139438.1. NM_001145966.1. [P46013-2]
    NP_002408.3. NM_002417.4. [P46013-1]
    UniGeneiHs.689823.
    Hs.80976.

    Genome annotation databases

    EnsembliENST00000368653; ENSP00000357642; ENSG00000148773. [P46013-2]
    ENST00000368654; ENSP00000357643; ENSG00000148773. [P46013-1]
    GeneIDi4288.
    KEGGihsa:4288.
    UCSCiuc001lke.3. human. [P46013-1]
    uc001lkf.3. human. [P46013-2]

    Polymorphism databases

    DMDMi118572663.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Ki-67 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65550 mRNA. Translation: CAA46519.1 .
    X65551 mRNA. Translation: CAA46520.1 .
    AL390236 , AL355529 Genomic DNA. Translation: CAH73169.1 .
    X94762 Genomic DNA. Translation: CAA64388.1 .
    CCDSi CCDS53588.1. [P46013-2 ]
    CCDS7659.1. [P46013-1 ]
    PIRi A48666.
    RefSeqi NP_001139438.1. NM_001145966.1. [P46013-2 ]
    NP_002408.3. NM_002417.4. [P46013-1 ]
    UniGenei Hs.689823.
    Hs.80976.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1R21 NMR - A 1-120 [» ]
    2AFF NMR - A 1-120 [» ]
    ProteinModelPortali P46013.
    SMRi P46013. Positions 1-100.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110434. 23 interactions.
    DIPi DIP-28132N.
    IntActi P46013. 17 interactions.
    MINTi MINT-137995.
    STRINGi 9606.ENSP00000357643.

    PTM databases

    PhosphoSitei P46013.

    Polymorphism databases

    DMDMi 118572663.

    Proteomic databases

    MaxQBi P46013.
    PaxDbi P46013.
    PRIDEi P46013.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368653 ; ENSP00000357642 ; ENSG00000148773 . [P46013-2 ]
    ENST00000368654 ; ENSP00000357643 ; ENSG00000148773 . [P46013-1 ]
    GeneIDi 4288.
    KEGGi hsa:4288.
    UCSCi uc001lke.3. human. [P46013-1 ]
    uc001lkf.3. human. [P46013-2 ]

    Organism-specific databases

    CTDi 4288.
    GeneCardsi GC10M129894.
    HGNCi HGNC:7107. MKI67.
    HPAi CAB000058.
    HPA000451.
    HPA001164.
    MIMi 176741. gene.
    neXtProti NX_P46013.
    PharmGKBi PA30825.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000113223.
    HOVERGENi HBG006213.
    InParanoidi P46013.
    KOi K17582.
    OMAi QTPKEKA.
    OrthoDBi EOG76QFGJ.
    PhylomeDBi P46013.
    TreeFami TF336000.

    Miscellaneous databases

    ChiTaRSi MKI67. human.
    EvolutionaryTracei P46013.
    GeneWikii Ki-67_(protein).
    GenomeRNAii 4288.
    NextBioi 16881.
    PROi P46013.
    SOURCEi Search...

    Gene expression databases

    Bgeei P46013.
    CleanExi HS_MKI67.
    Genevestigatori P46013.

    Family and domain databases

    Gene3Di 2.60.200.20. 1 hit.
    InterProi IPR000253. FHA_dom.
    IPR012568. K167R.
    IPR029334. PP1-bd.
    IPR008984. SMAD_FHA_domain.
    [Graphical view ]
    Pfami PF00498. FHA. 1 hit.
    PF08065. K167R. 16 hits.
    PF15276. PP1_bind. 1 hit.
    [Graphical view ]
    SMARTi SM00240. FHA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    PROSITEi PS50006. FHA_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The cell proliferation-associated antigen of antibody Ki-67: a very large, ubiquitous nuclear protein with numerous repeated elements, representing a new kind of cell cycle-maintaining proteins."
      Schlueter C., Duchrow M., Wohlenberg C., Becker M.H.G., Key G., Flad H.-D., Gerdes J.
      J. Cell Biol. 123:513-522(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SHORT AND LONG), VARIANTS VAL-872; TRP-1470; LEU-1622; ALA-1849 AND ASP-3097.
    2. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Sequence of the human Ki-67 protein gene 5' and promoter region."
      Gerdes J.
      Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
    4. "The forkhead-associated domain of Ki-67 antigen interacts with the novel kinesin-like protein Hklp2."
      Sueishi M., Takagi M., Yoneda Y.
      J. Biol. Chem. 275:28888-28892(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIF15.
    5. "A novel nucleolar protein, NIFK, interacts with the forkhead associated domain of Ki-67 antigen in mitosis."
      Takagi M., Sueishi M., Saiwaki T., Kametaka A., Yoneda Y.
      J. Biol. Chem. 276:25386-25391(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NIFK.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2406 AND SER-2708, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328; SER-357; SER-579; SER-584; SER-1131; THR-1327; THR-1569; THR-1801; THR-1923 AND THR-2406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1233; THR-1355; SER-1679 AND THR-1764, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357; SER-579; SER-584 AND SER-1861, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-357; SER-579; SER-648 AND SER-1679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-264; SER-308; THR-328; THR-347; SER-357; THR-401; SER-579; SER-584; SER-648; THR-761; SER-859; THR-1017; SER-1071; THR-1091; SER-1098; THR-1111; SER-1131; THR-1139; SER-1142; SER-1207; SER-1253; SER-1256; THR-1261; THR-1298; THR-1315; THR-1327; SER-1329; THR-1335; THR-1355; SER-1376; THR-1383; THR-1503; SER-1506; THR-1540; TYR-1552; THR-1557; THR-1569; SER-1571; SER-1679; SER-1689; THR-1719; SER-1721; SER-1740; THR-1747; THR-1784; THR-1801; THR-1841; SER-1861; SER-1864; THR-1869; THR-1923; THR-2065; SER-2072; THR-2085; SER-2105; THR-2113; THR-2203; SER-2223; THR-2231; SER-2239; THR-2285; THR-2325; THR-2328; THR-2333; SER-2344; THR-2352; THR-2389; SER-2395; THR-2406; SER-2528; SER-2588; SER-2708; SER-2827; SER-2828 AND SER-3041, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation."
      Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.
      J. Biol. Chem. 284:7542-7552(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH ASCL2; C11ORF30; HCFC1; HSPA8; CCAR2; MATR3; RBBP5; TUBB2A; WDR5 AND ZNF335.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648; SER-1131; THR-1335; THR-1557; THR-1764; SER-1937; THR-2406 AND SER-2420, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1639 AND LYS-2005, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-357; SER-579; SER-584; SER-648; THR-1091; SER-1098; SER-1131; THR-1167; THR-1193; SER-1207; THR-1233; THR-1315; THR-1327; SER-1329; THR-1335; THR-1355; THR-1557; THR-1569; SER-1571; SER-1679; THR-1747; THR-1801; SER-1815; SER-1861; THR-1897; THR-1923; SER-1937; THR-1963; SER-1983; THR-2065; SER-2072; THR-2085; SER-2105; SER-2135; SER-2223; THR-2231; THR-2233; SER-2239; THR-2268; THR-2285; THR-2325; SER-2344; THR-2389; SER-2395; THR-2406; SER-2420; THR-2446; SER-2528; SER-2588; SER-2708 AND SER-3128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-352; SER-357; SER-1098; SER-1131; SER-1496; SER-1861; SER-1983; SER-2072; SER-2105; SER-2344; SER-2528; SER-2588 AND SER-2708, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: INTERACTION WITH ZNF335.
    20. "Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
      Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
      Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    21. "Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions."
      Li H., Byeon I.-J., Ju Y., Tsai M.-D.
      J. Mol. Biol. 335:371-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-120 IN COMPLEX WITH NIFK.
    22. "Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67."
      Byeon I.-J., Li H., Song H., Gronenborn A.M., Tsai M.-D.
      Nat. Struct. Mol. Biol. 12:987-993(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-120 IN COMPLEX WITH NIFK.

    Entry informationi

    Entry nameiKI67_HUMAN
    AccessioniPrimary (citable) accession number: P46013
    Secondary accession number(s): Q5VWH2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 150 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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

    External Data

    Dasty 3