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P46013 (KI67_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Antigen KI-67
Gene names
Name:MKI67
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3256 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thought to be required for maintaining cell proliferation.

Subunit structure

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. Ref.4 Ref.5 Ref.13 Ref.19

Subcellular location

Nucleus. Nucleusnucleolus. Chromosome. 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. Ref.20

Developmental stage

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.

Sequence similarities

Contains 1 FHA domain.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA metabolic process

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Traceable author statement PubMed 17577209. Source: UniProtKB

cellular response to heat

Inferred from electronic annotation. Source: Ensembl

hyaluronan metabolic process

Inferred from electronic annotation. Source: Ensembl

meiotic nuclear division

Inferred from electronic annotation. Source: Ensembl

organ regeneration

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchromosome, centromeric region

Inferred from electronic annotation. Source: Ensembl

condensed chromosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from direct assay PubMed 17577209. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction PubMed 17577209. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P46013-1)

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 Short (identifier: P46013-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 32563256Antigen KI-67
PRO_0000084301

Regions

Domain27 – 7650FHA
Repeat1000 – 11121131
Repeat1122 – 12341132
Repeat1244 – 13561133
Repeat1366 – 14771124
Repeat1487 – 15981125
Repeat1608 – 17201136
Repeat1730 – 18421137
Repeat1851 – 19641148
Repeat1974 – 20861139
Repeat2096 – 220410910
Repeat2214 – 232611311
Repeat2335 – 244711312
Repeat2457 – 256911313
Repeat2579 – 268911114
Repeat2699 – 280811015
Repeat2818 – 292811116
Nucleotide binding3034 – 30418ATP Potential
Region1000 – 2928192916 X 122 AA approximate repeats

Amino acid modifications

Modified residue1251Phosphoserine Ref.11
Modified residue2641Phosphoserine Ref.11
Modified residue3081Phosphoserine Ref.10 Ref.11 Ref.17 Ref.18
Modified residue3281Phosphothreonine Ref.7 Ref.11
Modified residue3471Phosphothreonine Ref.11
Modified residue3521Phosphoserine Ref.18
Modified residue3571Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11 Ref.17 Ref.18
Modified residue4011Phosphothreonine Ref.11
Modified residue5791Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11 Ref.14 Ref.17
Modified residue5841Phosphoserine Ref.7 Ref.9 Ref.11 Ref.17
Modified residue6481Phosphoserine Ref.10 Ref.11 Ref.15 Ref.17
Modified residue7611Phosphothreonine Ref.11
Modified residue8591Phosphoserine Ref.11
Modified residue10171Phosphothreonine Ref.11
Modified residue10711Phosphoserine Ref.11
Modified residue10911Phosphothreonine Ref.11 Ref.17
Modified residue10981Phosphoserine Ref.11 Ref.17 Ref.18
Modified residue11111Phosphothreonine Ref.11
Modified residue11311Phosphoserine Ref.7 Ref.11 Ref.15 Ref.17 Ref.18
Modified residue11391Phosphothreonine Ref.11
Modified residue11421Phosphoserine Ref.11
Modified residue11671Phosphothreonine Ref.17
Modified residue11931Phosphothreonine Ref.17
Modified residue12071Phosphoserine Ref.11 Ref.17
Modified residue12331Phosphothreonine Ref.8 Ref.17
Modified residue12531Phosphoserine Ref.11
Modified residue12561Phosphoserine Ref.11
Modified residue12611Phosphothreonine Ref.11
Modified residue12981Phosphothreonine Ref.11
Modified residue13151Phosphothreonine Ref.11 Ref.17
Modified residue13271Phosphothreonine Ref.7 Ref.11 Ref.17
Modified residue13291Phosphoserine Ref.11 Ref.17
Modified residue13351Phosphothreonine Ref.11 Ref.15 Ref.17
Modified residue13551Phosphothreonine Ref.8 Ref.11 Ref.17
Modified residue13761Phosphoserine Ref.11
Modified residue13831Phosphothreonine Ref.11
Modified residue14961Phosphoserine Ref.18
Modified residue15031Phosphothreonine Ref.11
Modified residue15061Phosphoserine Ref.11
Modified residue15401Phosphothreonine Ref.11
Modified residue15521Phosphotyrosine Ref.11
Modified residue15571Phosphothreonine Ref.11 Ref.15 Ref.17
Modified residue15691Phosphothreonine Ref.7 Ref.11 Ref.17
Modified residue15711Phosphoserine Ref.11 Ref.17
Modified residue16391N6-acetyllysine Ref.16
Modified residue16791Phosphoserine Ref.8 Ref.10 Ref.11 Ref.17
Modified residue16891Phosphoserine Ref.11
Modified residue17191Phosphothreonine Ref.11
Modified residue17211Phosphoserine Ref.11
Modified residue17401Phosphoserine Ref.11
Modified residue17471Phosphothreonine Ref.11 Ref.17
Modified residue17641Phosphothreonine Ref.8 Ref.15
Modified residue17841Phosphothreonine Ref.11
Modified residue18011Phosphothreonine Ref.7 Ref.11 Ref.17
Modified residue18151Phosphoserine Ref.17
Modified residue18411Phosphothreonine Ref.11
Modified residue18611Phosphoserine Ref.9 Ref.11 Ref.17 Ref.18
Modified residue18641Phosphoserine Ref.11
Modified residue18691Phosphothreonine Ref.11
Modified residue18971Phosphothreonine Ref.17
Modified residue19231Phosphothreonine Ref.7 Ref.11 Ref.17
Modified residue19371Phosphoserine Ref.15 Ref.17
Modified residue19631Phosphothreonine Ref.17
Modified residue19831Phosphoserine Ref.17 Ref.18
Modified residue20051N6-acetyllysine Ref.16
Modified residue20651Phosphothreonine Ref.11 Ref.17
Modified residue20721Phosphoserine Ref.11 Ref.17 Ref.18
Modified residue20851Phosphothreonine Ref.11 Ref.17
Modified residue21051Phosphoserine Ref.11 Ref.17 Ref.18
Modified residue21131Phosphothreonine Ref.11
Modified residue21351Phosphoserine Ref.17
Modified residue22031Phosphothreonine Ref.11
Modified residue22231Phosphoserine Ref.11 Ref.17
Modified residue22311Phosphothreonine Ref.11 Ref.17
Modified residue22331Phosphothreonine Ref.17
Modified residue22391Phosphoserine Ref.11 Ref.17
Modified residue22681Phosphothreonine Ref.17
Modified residue22851Phosphothreonine Ref.11 Ref.17
Modified residue23251Phosphothreonine Ref.11 Ref.17
Modified residue23281Phosphothreonine Ref.11
Modified residue23331Phosphothreonine Ref.11
Modified residue23441Phosphoserine Ref.11 Ref.17 Ref.18
Modified residue23521Phosphothreonine Ref.11
Modified residue23891Phosphothreonine Ref.11 Ref.17
Modified residue23951Phosphoserine Ref.11 Ref.17
Modified residue24061Phosphothreonine Ref.6 Ref.7 Ref.11 Ref.15 Ref.17
Modified residue24201Phosphoserine Ref.15 Ref.17
Modified residue24461Phosphothreonine Ref.17
Modified residue25281Phosphoserine Ref.11 Ref.17 Ref.18
Modified residue25881Phosphoserine Ref.11 Ref.17 Ref.18
Modified residue27081Phosphoserine Ref.6 Ref.11 Ref.17 Ref.18
Modified residue28271Phosphoserine Ref.11
Modified residue28281Phosphoserine Ref.11
Modified residue30411Phosphoserine Ref.11
Modified residue31281Phosphoserine Ref.17

Natural variations

Alternative sequence136 – 495360Missing in isoform Short.
VSP_004298
Natural variant1041N → S.
Corresponds to variant rs2071498 [ dbSNP | Ensembl ].
VAR_029055
Natural variant2381W → R.
Corresponds to variant rs7095325 [ dbSNP | Ensembl ].
VAR_029056
Natural variant4971E → D.
Corresponds to variant rs11016076 [ dbSNP | Ensembl ].
VAR_029057
Natural variant5741Q → P.
Corresponds to variant rs4471342 [ dbSNP | Ensembl ].
VAR_029058
Natural variant6311I → L.
Corresponds to variant rs997983 [ dbSNP | Ensembl ].
VAR_024161
Natural variant8321R → W.
Corresponds to variant rs34916904 [ dbSNP | Ensembl ].
VAR_033995
Natural variant8541L → V.
Corresponds to variant rs2240 [ dbSNP | Ensembl ].
VAR_024162
Natural variant8721A → V. Ref.1
Corresponds to variant rs2853344 [ dbSNP | Ensembl ].
VAR_029059
Natural variant10421G → S.
Corresponds to variant rs2152143 [ dbSNP | Ensembl ].
VAR_024163
Natural variant11201T → S.
Corresponds to variant rs11016074 [ dbSNP | Ensembl ].
VAR_029060
Natural variant12471T → I.
Corresponds to variant rs4750685 [ dbSNP | Ensembl ].
VAR_021838
Natural variant14031E → V.
Corresponds to variant rs3740423 [ dbSNP | Ensembl ].
VAR_020047
Natural variant14701L → W. Ref.1
Corresponds to variant rs2853345 [ dbSNP | Ensembl ].
VAR_029061
Natural variant15591V → M.
Corresponds to variant rs7918199 [ dbSNP | Ensembl ].
VAR_029062
Natural variant16221P → L. Ref.1
Corresponds to variant rs2782871 [ dbSNP | Ensembl ].
VAR_029063
Natural variant18491T → A. Ref.1
Corresponds to variant rs2782872 [ dbSNP | Ensembl ].
VAR_029064
Natural variant18761R → Q.
Corresponds to variant rs11591817 [ dbSNP | Ensembl ].
VAR_029065
Natural variant19511L → I.
Corresponds to variant rs34116632 [ dbSNP | Ensembl ].
VAR_033996
Natural variant21011I → T.
Corresponds to variant rs11016073 [ dbSNP | Ensembl ].
VAR_029066
Natural variant23371T → N.
Corresponds to variant rs7083622 [ dbSNP | Ensembl ].
VAR_024164
Natural variant23631N → S.
Corresponds to variant rs7071768 [ dbSNP | Ensembl ].
VAR_029067
Natural variant26071R → H.
Corresponds to variant rs34688192 [ dbSNP | Ensembl ].
VAR_061671
Natural variant26081P → L.
Corresponds to variant rs1063535 [ dbSNP | Ensembl ].
VAR_024165
Natural variant26491R → H.
Corresponds to variant rs12777740 [ dbSNP | Ensembl ].
VAR_029068
Natural variant27201T → P.
Corresponds to variant rs1050767 [ dbSNP | Ensembl ].
VAR_024166
Natural variant27601D → G.
Corresponds to variant rs10082391 [ dbSNP | Ensembl ].
VAR_029069
Natural variant27861R → Q.
Corresponds to variant rs10764749 [ dbSNP | Ensembl ].
VAR_029070
Natural variant27931S → N.
Corresponds to variant rs10082533 [ dbSNP | Ensembl ].
VAR_029071
Natural variant28451R → H.
Corresponds to variant rs11016072 [ dbSNP | Ensembl ].
VAR_029072
Natural variant28681T → S.
Corresponds to variant rs2071496 [ dbSNP | Ensembl ].
VAR_024167
Natural variant29041Q → R.
Corresponds to variant rs11016071 [ dbSNP | Ensembl ].
VAR_029073
Natural variant30971N → D. Ref.1
Corresponds to variant rs2798669 [ dbSNP | Ensembl ].
VAR_029074
Natural variant31021E → G.
Corresponds to variant rs34750407 [ dbSNP | Ensembl ].
VAR_033997
Natural variant31501T → S.
Corresponds to variant rs11106 [ dbSNP | Ensembl ].
VAR_014858
Natural variant32171K → E.
Corresponds to variant rs8473 [ dbSNP | Ensembl ].
VAR_014859

Experimental info

Sequence conflict619 – 6268RKSGNLPS → ERVATCLQ in CAA46519. Ref.1
Sequence conflict619 – 6268RKSGNLPS → ERVATCLQ in CAA46520. Ref.1
Sequence conflict22051I → V in CAA46519. Ref.1
Sequence conflict22051I → V in CAA46520. Ref.1
Sequence conflict2892 – 28932KL → NV in CAA46519. Ref.1
Sequence conflict2892 – 28932KL → NV in CAA46520. Ref.1
Sequence conflict32461R → T in CAA46519. Ref.1
Sequence conflict32461R → T in CAA46520. Ref.1

Secondary structure

..................... 3256
Helix Strand Turn

Details...

Sequences

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

Last modified November 28, 2006. Version 2.
Checksum: 1332BC6C799AD64D

FASTA3,256358,694
        10         20         30         40         50         60 
MWPTRRLVTI KRSGVDGPHF PLSLSTCLFG RGIECDIRIQ LPVVSKQHCK IEIHEQEAIL 

        70         80         90        100        110        120 
HNFSSTNPTQ VNGSVIDEPV RLKHGDVITI IDRSFRYENE SLQNGRKSTE FPRKIREQEP 

       130        140        150        160        170        180 
ARRVSRSSFS SDPDEKAQDS KAYSKITEGK VSGNPQVHIK NVKEDSTADD SKDSVAQGTT 

       190        200        210        220        230        240 
NVHSSEHAGR NGRNAADPIS GDFKEISSVK LVSRYGELKS VPTTQCLDNS KKNESPFWKL 

       250        260        270        280        290        300 
YESVKKELDV KSQKENVLQY CRKSGLQTDY ATEKESADGL QGETQLLVSR KSRPKSGGSG 

       310        320        330        340        350        360 
HAVAEPASPE QELDQNKGKG RDVESVQTPS KAVGASFPLY EPAKMKTPVQ YSQQQNSPQK 

       370        380        390        400        410        420 
HKNKDLYTTG RRESVNLGKS EGFKAGDKTL TPRKLSTRNR TPAKVEDAAD SATKPENLSS 

       430        440        450        460        470        480 
KTRGSIPTDV EVLPTETEIH NEPFLTLWLT QVERKIQKDS LSKPEKLGTT AGQMCSGLPG 

       490        500        510        520        530        540 
LSSVDINNFG DSINESEGIP LKRRRVSFGG HLRPELFDEN LPPNTPLKRG EAPTKRKSLV 

       550        560        570        580        590        600 
MHTPPVLKKI IKEQPQPSGK QESGSEIHVE VKAQSLVISP PAPSPRKTPV ASDQRRRSCK 

       610        620        630        640        650        660 
TAPASSSKSQ TEVPKRGGRK SGNLPSKRVS ISRSQHDILQ MICSKRRSGA SEANLIVAKS 

       670        680        690        700        710        720 
WADVVKLGAK QTQTKVIKHG PQRSMNKRQR RPATPKKPVG EVHSQFSTGH ANSPCTIIIG 

       730        740        750        760        770        780 
KAHTEKVHVP ARPYRVLNNF ISNQKMDFKE DLSGIAEMFK TPVKEQPQLT STCHIAISNS 

       790        800        810        820        830        840 
ENLLGKQFQG TDSGEEPLLP TSESFGGNVF FSAQNAAKQP SDKCSASPPL RRQCIRENGN 

       850        860        870        880        890        900 
VAKTPRNTYK MTSLETKTSD TETEPSKTVS TANRSGRSTE FRNIQKLPVE SKSEETNTEI 

       910        920        930        940        950        960 
VECILKRGQK ATLLQQRREG EMKEIERPFE TYKENIELKE NDEKMKAMKR SRTWGQKCAP 

       970        980        990       1000       1010       1020 
MSDLTDLKSL PDTELMKDTA RGQNLLQTQD HAKAPKSEKG KITKMPCQSL QPEPINTPTH 

      1030       1040       1050       1060       1070       1080 
TKQQLKASLG KVGVKEELLA VGKFTRTSGE TTHTHREPAG DGKSIRTFKE SPKQILDPAA 

      1090       1100       1110       1120       1130       1140 
RVTGMKKWPR TPKEEAQSLE DLAGFKELFQ TPGPSEESMT DEKTTKIACK SPPPESVDTP 

      1150       1160       1170       1180       1190       1200 
TSTKQWPKRS LRKADVEEEF LALRKLTPSA GKAMLTPKPA GGDEKDIKAF MGTPVQKLDL 

      1210       1220       1230       1240       1250       1260 
AGTLPGSKRQ LQTPKEKAQA LEDLAGFKEL FQTPGHTEEL VAAGKTTKIP CDSPQSDPVD 

      1270       1280       1290       1300       1310       1320 
TPTSTKQRPK RSIRKADVEG ELLACRNLMP SAGKAMHTPK PSVGEEKDII IFVGTPVQKL 

      1330       1340       1350       1360       1370       1380 
DLTENLTGSK RRPQTPKEEA QALEDLTGFK ELFQTPGHTE EAVAAGKTTK MPCESSPPES 

      1390       1400       1410       1420       1430       1440 
ADTPTSTRRQ PKTPLEKRDV QKELSALKKL TQTSGETTHT DKVPGGEDKS INAFRETAKQ 

      1450       1460       1470       1480       1490       1500 
KLDPAASVTG SKRHPKTKEK AQPLEDLAGL KELFQTPVCT DKPTTHEKTT KIACRSQPDP 

      1510       1520       1530       1540       1550       1560 
VDTPTSSKPQ SKRSLRKVDV EEEFFALRKR TPSAGKAMHT PKPAVSGEKN IYAFMGTPVQ 

      1570       1580       1590       1600       1610       1620 
KLDLTENLTG SKRRLQTPKE KAQALEDLAG FKELFQTRGH TEESMTNDKT AKVACKSSQP 

      1630       1640       1650       1660       1670       1680 
DPDKNPASSK RRLKTSLGKV GVKEELLAVG KLTQTSGETT HTHTEPTGDG KSMKAFMESP 

      1690       1700       1710       1720       1730       1740 
KQILDSAASL TGSKRQLRTP KGKSEVPEDL AGFIELFQTP SHTKESMTNE KTTKVSYRAS 

      1750       1760       1770       1780       1790       1800 
QPDLVDTPTS SKPQPKRSLR KADTEEEFLA FRKQTPSAGK AMHTPKPAVG EEKDINTFLG 

      1810       1820       1830       1840       1850       1860 
TPVQKLDQPG NLPGSNRRLQ TRKEKAQALE ELTGFRELFQ TPCTDNPTTD EKTTKKILCK 

      1870       1880       1890       1900       1910       1920 
SPQSDPADTP TNTKQRPKRS LKKADVEEEF LAFRKLTPSA GKAMHTPKAA VGEEKDINTF 

      1930       1940       1950       1960       1970       1980 
VGTPVEKLDL LGNLPGSKRR PQTPKEKAKA LEDLAGFKEL FQTPGHTEES MTDDKITEVS 

      1990       2000       2010       2020       2030       2040 
CKSPQPDPVK TPTSSKQRLK ISLGKVGVKE EVLPVGKLTQ TSGKTTQTHR ETAGDGKSIK 

      2050       2060       2070       2080       2090       2100 
AFKESAKQML DPANYGTGME RWPRTPKEEA QSLEDLAGFK ELFQTPDHTE ESTTDDKTTK 

      2110       2120       2130       2140       2150       2160 
IACKSPPPES MDTPTSTRRR PKTPLGKRDI VEELSALKQL TQTTHTDKVP GDEDKGINVF 

      2170       2180       2190       2200       2210       2220 
RETAKQKLDP AASVTGSKRQ PRTPKGKAQP LEDLAGLKEL FQTPICTDKP TTHEKTTKIA 

      2230       2240       2250       2260       2270       2280 
CRSPQPDPVG TPTIFKPQSK RSLRKADVEE ESLALRKRTP SVGKAMDTPK PAGGDEKDMK 

      2290       2300       2310       2320       2330       2340 
AFMGTPVQKL DLPGNLPGSK RWPQTPKEKA QALEDLAGFK ELFQTPGTDK PTTDEKTTKI 

      2350       2360       2370       2380       2390       2400 
ACKSPQPDPV DTPASTKQRP KRNLRKADVE EEFLALRKRT PSAGKAMDTP KPAVSDEKNI 

      2410       2420       2430       2440       2450       2460 
NTFVETPVQK LDLLGNLPGS KRQPQTPKEK AEALEDLVGF KELFQTPGHT EESMTDDKIT 

      2470       2480       2490       2500       2510       2520 
EVSCKSPQPE SFKTSRSSKQ RLKIPLVKVD MKEEPLAVSK LTRTSGETTQ THTEPTGDSK 

      2530       2540       2550       2560       2570       2580 
SIKAFKESPK QILDPAASVT GSRRQLRTRK EKARALEDLV DFKELFSAPG HTEESMTIDK 

      2590       2600       2610       2620       2630       2640 
NTKIPCKSPP PELTDTATST KRCPKTRPRK EVKEELSAVE RLTQTSGQST HTHKEPASGD 

      2650       2660       2670       2680       2690       2700 
EGIKVLKQRA KKKPNPVEEE PSRRRPRAPK EKAQPLEDLA GFTELSETSG HTQESLTAGK 

      2710       2720       2730       2740       2750       2760 
ATKIPCESPP LEVVDTTAST KRHLRTRVQK VQVKEEPSAV KFTQTSGETT DADKEPAGED 

      2770       2780       2790       2800       2810       2820 
KGIKALKESA KQTPAPAASV TGSRRRPRAP RESAQAIEDL AGFKDPAAGH TEESMTDDKT 

      2830       2840       2850       2860       2870       2880 
TKIPCKSSPE LEDTATSSKR RPRTRAQKVE VKEELLAVGK LTQTSGETTH TDKEPVGEGK 

      2890       2900       2910       2920       2930       2940 
GTKAFKQPAK RKLDAEDVIG SRRQPRAPKE KAQPLEDLAS FQELSQTPGH TEELANGAAD 

      2950       2960       2970       2980       2990       3000 
SFTSAPKQTP DSGKPLKISR RVLRAPKVEP VGDVVSTRDP VKSQSKSNTS LPPLPFKRGG 

      3010       3020       3030       3040       3050       3060 
GKDGSVTGTK RLRCMPAPEE IVEELPASKK QRVAPRARGK SSEPVVIMKR SLRTSAKRIE 

      3070       3080       3090       3100       3110       3120 
PAEELNSNDM KTNKEEHKLQ DSVPENKGIS LRSRRQNKTE AEQQITEVFV LAERIEINRN 

      3130       3140       3150       3160       3170       3180 
EKKPMKTSPE MDIQNPDDGA RKPIPRDKVT ENKRCLRSAR QNESSQPKVA EESGGQKSAK 

      3190       3200       3210       3220       3230       3240 
VLMQNQKGKG EAGNSDSMCL RSRKTKSQPA ASTLESKSVQ RVTRSVKRCA ENPKKAEDNV 

      3250 
CVKKIRTRSH RDSEDI 

« Hide

Isoform Short [UniParc].

Checksum: 4FACAA90AC686C72
Show »

FASTA2,896319,444

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Microcephaly gene links trithorax and REST/NRSF to control neural stem cell proliferation and differentiation."
Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D., Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J., Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A., Mahajnah M., Shenhav R., Walsh C.A.
Cell 151:1097-1112(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Wikipedia

Ki-67 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65550 mRNA. Translation: CAA46519.1.
X65551 mRNA. Translation: CAA46520.1.
AL390236, AL355529 Genomic DNA. Translation: CAH73169.1.
X94762 Genomic DNA. Translation: CAA64388.1.
CCDSCCDS53588.1. [P46013-2]
CCDS7659.1. [P46013-1]
PIRA48666.
RefSeqNP_001139438.1. NM_001145966.1. [P46013-2]
NP_002408.3. NM_002417.4. [P46013-1]
UniGeneHs.689823.
Hs.80976.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R21NMR-A1-120[»]
2AFFNMR-A1-120[»]
ProteinModelPortalP46013.
SMRP46013. Positions 1-100.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110434. 22 interactions.
DIPDIP-28132N.
IntActP46013. 17 interactions.
MINTMINT-137995.
STRING9606.ENSP00000357643.

PTM databases

PhosphoSiteP46013.

Polymorphism databases

DMDM118572663.

Proteomic databases

MaxQBP46013.
PaxDbP46013.
PRIDEP46013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368653; ENSP00000357642; ENSG00000148773. [P46013-2]
ENST00000368654; ENSP00000357643; ENSG00000148773. [P46013-1]
GeneID4288.
KEGGhsa:4288.
UCSCuc001lke.3. human. [P46013-1]
uc001lkf.3. human. [P46013-2]

Organism-specific databases

CTD4288.
GeneCardsGC10M129894.
HGNCHGNC:7107. MKI67.
HPACAB000058.
HPA000451.
HPA001164.
MIM176741. gene.
neXtProtNX_P46013.
PharmGKBPA30825.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000113223.
HOVERGENHBG006213.
InParanoidP46013.
KOK17582.
OMAQTPKEKA.
OrthoDBEOG76QFGJ.
PhylomeDBP46013.
TreeFamTF336000.

Gene expression databases

BgeeP46013.
CleanExHS_MKI67.
GenevestigatorP46013.

Family and domain databases

Gene3D2.60.200.20. 1 hit.
InterProIPR000253. FHA_dom.
IPR012568. K167R.
IPR029334. PP1-bd.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamPF00498. FHA. 1 hit.
PF08065. K167R. 16 hits.
PF15276. PP1_bind. 1 hit.
[Graphical view]
SMARTSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
PROSITEPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMKI67. human.
EvolutionaryTraceP46013.
GeneWikiKi-67_(protein).
GenomeRNAi4288.
NextBio16881.
PROP46013.
SOURCESearch...

Entry information

Entry nameKI67_HUMAN
AccessionPrimary (citable) accession number: P46013
Secondary accession number(s): Q5VWH2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 28, 2006
Last modified: July 9, 2014
This is version 148 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM