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Reviewed, UniProtKB/Swiss-Prot P46013 (KI67_HUMAN)

Last modified July 13, 2010. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents
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Names and originHide

Protein namesRecommended name:
Antigen KI-67
Gene names
Name:MKI67
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
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Protein attributesHide

Sequence length3256 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.
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General annotation (Comments)Hide

Function

Thought to be required for maintaining cell proliferation.

Subunit structure

Interacts with KIF15. Binds through the FHA domain to MKI67IP. Ref.4 Ref.5

Subcellular location

Nucleus. 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.

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.

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OntologiesHide

Keywords
   Biological processCell cycle
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processcell proliferation

Traceable author statement. Source: UniProtKB

   Cellular componentnucleolus

Inferred from direct assay. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein C-terminus binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...
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Alternative productsHide

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.
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Sequence annotation (Features)Hide

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 residue1081Phosphoserine Ref.9 Ref.12
Modified residue1091Phosphothreonine Ref.12
Modified residue1251Phosphoserine Ref.11 Ref.16
Modified residue1281Phosphoserine Ref.12 Ref.11 Ref.16
Modified residue1311Phosphoserine Ref.16
Modified residue2641Phosphoserine Ref.12 Ref.16
Modified residue3081Phosphoserine Ref.9 Ref.12 Ref.16 Ref.7 Ref.15 Ref.19
Modified residue3281Phosphothreonine Ref.12 Ref.16 Ref.8
Modified residue3471Phosphothreonine Ref.16 Ref.19
Modified residue3521Phosphoserine Ref.13
Modified residue3571Phosphoserine Ref.12 Ref.11 Ref.16 Ref.15 Ref.19 Ref.8 Ref.13 Ref.6 Ref.14
Modified residue3741Phosphoserine Ref.9 Ref.12 Ref.11 Ref.16
Modified residue4011Phosphothreonine Ref.16
Modified residue4111Phosphoserine Ref.16
Modified residue5381Phosphoserine Ref.16
Modified residue5431Phosphothreonine Ref.9 Ref.16
Modified residue5791Phosphoserine Ref.9 Ref.12 Ref.16 Ref.15 Ref.6 Ref.14 Ref.18
Modified residue5841Phosphoserine Ref.12 Ref.16 Ref.15 Ref.19 Ref.14 Ref.18
Modified residue6301Phosphoserine Ref.12
Modified residue6481Phosphoserine Ref.9 Ref.12 Ref.11 Ref.16 Ref.15 Ref.19
Modified residue7131Phosphoserine Ref.12
Modified residue7611Phosphothreonine Ref.16
Modified residue8271Phosphoserine Ref.12
Modified residue8591Phosphoserine Ref.12 Ref.16
Modified residue10171Phosphothreonine Ref.16
Modified residue10981Phosphoserine Ref.9
Modified residue11111Phosphothreonine Ref.16 Ref.19
Modified residue11311Phosphoserine Ref.9 Ref.12 Ref.11 Ref.16 Ref.19
Modified residue11391Phosphothreonine Ref.11 Ref.16
Modified residue11761Phosphothreonine Ref.16
Modified residue11931Phosphothreonine Ref.9 Ref.19
Modified residue12071Phosphoserine Ref.16 Ref.10
Modified residue12331Phosphothreonine Ref.16 Ref.10
Modified residue12371Phosphothreonine Ref.16
Modified residue12531Phosphoserine Ref.9 Ref.16 Ref.17
Modified residue12561Phosphoserine Ref.16
Modified residue12611Phosphothreonine Ref.16 Ref.17
Modified residue12981Phosphothreonine Ref.11 Ref.16
Modified residue13021Phosphoserine Ref.11 Ref.16
Modified residue13151Phosphothreonine Ref.16
Modified residue13271Phosphothreonine Ref.9 Ref.19
Modified residue13291Phosphoserine Ref.19
Modified residue13351Phosphothreonine Ref.9 Ref.16 Ref.19 Ref.10
Modified residue13551Phosphothreonine Ref.16 Ref.10
Modified residue13751Phosphoserine Ref.9 Ref.16
Modified residue13761Phosphoserine Ref.16 Ref.6
Modified residue13831Phosphothreonine Ref.16
Modified residue15031Phosphothreonine Ref.12 Ref.16
Modified residue15061Phosphoserine Ref.16
Modified residue15401Phosphothreonine Ref.16
Modified residue15461Phosphoserine Ref.16
Modified residue15521Phosphotyrosine Ref.16
Modified residue15571Phosphothreonine Ref.9 Ref.12 Ref.16 Ref.19 Ref.10
Modified residue15651Phosphothreonine Ref.16
Modified residue15691Phosphothreonine Ref.12 Ref.16
Modified residue15711Phosphoserine Ref.12 Ref.16
Modified residue16181Phosphoserine Ref.11
Modified residue16281Phosphoserine Ref.12
Modified residue16291Phosphoserine Ref.12 Ref.11
Modified residue16361Phosphoserine Ref.10
Modified residue16391N6-acetyllysine Ref.20
Modified residue16791Phosphoserine Ref.12 Ref.16 Ref.15 Ref.10
Modified residue16891Phosphoserine Ref.16
Modified residue17191Phosphothreonine Ref.16
Modified residue17211Phosphoserine Ref.16
Modified residue17261Phosphoserine Ref.16
Modified residue17401Phosphoserine Ref.9 Ref.16
Modified residue17471Phosphothreonine Ref.16
Modified residue17641Phosphothreonine Ref.16 Ref.19 Ref.10
Modified residue17841Phosphothreonine Ref.16
Modified residue18011Phosphothreonine Ref.9 Ref.12 Ref.16 Ref.17
Modified residue18151Phosphoserine Ref.9 Ref.12 Ref.16
Modified residue18411Phosphothreonine Ref.16
Modified residue18611Phosphoserine Ref.9 Ref.12 Ref.16 Ref.14 Ref.17
Modified residue18641Phosphoserine Ref.16
Modified residue18691Phosphothreonine Ref.12 Ref.16 Ref.17
Modified residue18971Phosphothreonine Ref.12 Ref.10
Modified residue19231Phosphothreonine Ref.9 Ref.12 Ref.16 Ref.7 Ref.15 Ref.19
Modified residue19371Phosphoserine Ref.19 Ref.10
Modified residue19831Phosphoserine Ref.12
Modified residue20021Phosphoserine Ref.9
Modified residue20051N6-acetyllysine Ref.20
Modified residue20651Phosphothreonine Ref.16
Modified residue20721Phosphoserine Ref.16 Ref.19
Modified residue20851Phosphothreonine Ref.9 Ref.16
Modified residue21051Phosphoserine Ref.9 Ref.12 Ref.16
Modified residue21131Phosphothreonine Ref.12 Ref.16
Modified residue21351Phosphoserine Ref.16
Modified residue22031Phosphothreonine Ref.16
Modified residue22111Phosphothreonine Ref.16
Modified residue22231Phosphoserine Ref.9 Ref.12 Ref.11 Ref.16 Ref.7
Modified residue22311Phosphothreonine Ref.12 Ref.11 Ref.16
Modified residue22391Phosphoserine Ref.16
Modified residue22641N6-acetyllysine Ref.20
Modified residue22851Phosphothreonine Ref.16 Ref.10 Ref.17
Modified residue22991Phosphoserine Ref.16
Modified residue23051Phosphothreonine Ref.16 Ref.10
Modified residue23251Phosphothreonine Ref.16
Modified residue23281Phosphothreonine Ref.16
Modified residue23321Phosphothreonine Ref.16
Modified residue23441Phosphoserine Ref.12 Ref.16
Modified residue23521Phosphothreonine Ref.16
Modified residue23551Phosphoserine Ref.16
Modified residue23891Phosphothreonine Ref.12 Ref.16
Modified residue23951Phosphoserine Ref.16
Modified residue24061Phosphothreonine Ref.12 Ref.16 Ref.7 Ref.19 Ref.8
Modified residue24201Phosphoserine Ref.16
Modified residue24261Phosphothreonine Ref.16
Modified residue24461Phosphothreonine Ref.16
Modified residue24661Phosphoserine Ref.12 Ref.16
Modified residue24711Phosphoserine Ref.12
Modified residue25051Phosphoserine Ref.10
Modified residue25081Phosphothreonine Ref.10
Modified residue25091Phosphothreonine Ref.12
Modified residue25281Phosphoserine Ref.12 Ref.16 Ref.7
Modified residue25881Phosphoserine Ref.12 Ref.16
Modified residue26381Phosphoserine Ref.12
Modified residue27081Phosphoserine Ref.9 Ref.12 Ref.16 Ref.7 Ref.6
Modified residue28271Phosphoserine Ref.9 Ref.12 Ref.16
Modified residue28281Phosphoserine Ref.9 Ref.16
Modified residue30411Phosphoserine Ref.12 Ref.16
Modified residue30421Phosphoserine Ref.12
Modified residue30821Phosphoserine Ref.12
Modified residue32071Phosphoserine Ref.12
Modified residue32131Phosphothreonine Ref.15
Modified residue32161Phosphoserine Ref.15
Modified residue32231Phosphothreonine Ref.15

Natural variations

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

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SequencesHide

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 

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Isoform Short.

Checksum: 4FACAA90AC686C72
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FASTA2,896319,444
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ReferencesHide

« 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: 8227122] [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: 15164054] [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: 10878014] [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: 11342549] [Abstract]
Cited for: INTERACTION WITH MKI67IP.
[6]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357; SER-579; SER-1376 AND SER-2708, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; THR-1923; SER-2223; THR-2406; SER-2528 AND SER-2708, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328; SER-357 AND THR-2406, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-308; SER-374; THR-543; SER-579; SER-648; SER-1098; SER-1131; THR-1193; SER-1253; THR-1327; THR-1335; SER-1375; THR-1557; SER-1740; THR-1801; SER-1815; SER-1861; THR-1923; SER-2002; THR-2085; SER-2105; SER-2223; SER-2708; SER-2827 AND SER-2828, MASS SPECTROMETRY.
Tissue: Cervix adenocarcinoma.
[10]"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: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1207; THR-1233; THR-1335; THR-1355; THR-1557; SER-1636; SER-1679; THR-1764; THR-1897; SER-1937; THR-2285; THR-2305; SER-2505 AND THR-2508, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-128; SER-357; SER-374; SER-648; SER-1131; THR-1139; THR-1298; SER-1302; SER-1618; SER-1629; SER-2223 AND THR-2231, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[12]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; THR-109; SER-128; SER-264; SER-308; THR-328; SER-357; SER-374; SER-579; SER-584; SER-630; SER-648; SER-713; SER-827; SER-859; SER-1131; THR-1503; THR-1557; THR-1569; SER-1571; SER-1628; SER-1629; SER-1679; THR-1801; SER-1815; SER-1861; THR-1869; THR-1897; THR-1923; SER-1983; SER-2105; THR-2113; SER-2223; THR-2231; SER-2344; THR-2389; THR-2406; SER-2466; SER-2471; THR-2509; SER-2528; SER-2588; SER-2638; SER-2708; SER-2827; SER-3041; SER-3042; SER-3082 AND SER-3207, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352 AND SER-357, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[14]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357; SER-579; SER-584 AND SER-1861, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[15]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-357; SER-579; SER-584; SER-648; SER-1679; THR-1923; THR-3213; SER-3216 AND THR-3223, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[16]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-128; SER-131; SER-264; SER-308; THR-328; THR-347; SER-357; SER-374; THR-401; SER-411; SER-538; THR-543; SER-579; SER-584; SER-648; THR-761; SER-859; THR-1017; THR-1111; SER-1131; THR-1139; THR-1176; SER-1207; THR-1233; THR-1237; SER-1253; SER-1256; THR-1261; THR-1298; SER-1302; THR-1315; THR-1335; THR-1355; SER-1375; SER-1376; THR-1383; THR-1503; SER-1506; THR-1540; SER-1546; TYR-1552; THR-1557; THR-1565; THR-1569; SER-1571; SER-1679; SER-1689; THR-1719; SER-1721; SER-1726; SER-1740; THR-1747; THR-1764; THR-1784; THR-1801; SER-1815; THR-1841; SER-1861; SER-1864; THR-1869; THR-1923; THR-2065; SER-2072; THR-2085; SER-2105; THR-2113; SER-2135; THR-2203; THR-2211; SER-2223; THR-2231; SER-2239; THR-2285; SER-2299; THR-2305; THR-2325; THR-2328; THR-2332; SER-2344; THR-2352; SER-2355; THR-2389; SER-2395; THR-2406; SER-2420; THR-2426; THR-2446; SER-2466; SER-2528; SER-2588; SER-2708; SER-2827; SER-2828 AND SER-3041, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[17]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1253; THR-1261; THR-1801; SER-1861; THR-1869 AND THR-2285, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[18]"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: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579 AND SER-584, MASS SPECTROMETRY.
[19]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; THR-347; SER-357; SER-584; SER-648; THR-1111; SER-1131; THR-1193; THR-1327; SER-1329; THR-1335; THR-1557; THR-1764; THR-1923; SER-1937; SER-2072 AND THR-2406, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[20]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1639; LYS-2005 AND LYS-2264, MASS SPECTROMETRY.
[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: 14659764] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-120 IN COMPLEX WITH MKI67IP.
[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: 16244663] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-120 IN COMPLEX WITH MKI67IP.
+Additional computationally mapped references.
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Web resourcesHide

Wikipedia

Ki-67 entry

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Cross-referencesHide

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.
IPIIPI00004233.
IPI00413173.
PIRA48666.
RefSeqNP_001139438.1.
NP_002408.3.
UniGeneHs.689823
Hs.80976

3D structure databases

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

Protein-protein interaction databases

DIPDIP-28132N.
IntActP46013. 7 interactions.
MINTMINT-137995.
STRINGP46013.

PTM databases

PhosphoSiteP46013.

Proteomic databases

PRIDEP46013.

Genome annotation databases

EnsemblENST00000368654; ENSP00000357643; ENSG00000148773; Homo sapiens. [Genome view]
GeneID4288.
KEGGhsa:4288.
UCSCuc001lke.1. human.
uc001lkf.1. human.

Organism-specific databases

CTD4288.
GeneCardsGC10M129784.
HGNCHGNC:7107. MKI67.
HPACAB000058.
HPA000451.
HPA001164.
MIM176741. gene.
PharmGKBPA30825.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG04868.
HOGENOMHBG283314.
HOVERGENHBG006213.
InParanoidP46013.
OMAQTPKEKA.
OrthoDBEOG9H1DFV.
PhylomeDBP46013.

Gene expression databases

ArrayExpressP46013.
BgeeP46013.
CleanExHS_MKI67.
GenevestigatorP46013.
GermOnlineENSG00000148773. Homo sapiens.

Family and domain databases

InterProIPR000253. FHA_dom.
IPR012568. K167R.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamPF00498. FHA. 1 hit.
PF08065. K167R. 16 hits.
[Graphical view]
SMARTSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMSSF49879. SMAD_FHA. 1 hit.
PROSITEPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio16881.
SOURCESearch...
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Entry informationHide

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 13, 2010
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.
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Relevant documentsHide

Human chromosome 10

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents