Reviewed, UniProtKB/Swiss-Prot P46013 (KI67_HUMAN)

Names and originHide

Protein names

Recommended name:
Antigen KI-67

Gene names

Name:

MKI67

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributesHide

Sequence length	3256 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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.

OntologiesHide

Keywords
Biological process	Cell cycle
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell proliferation Traceable author statement. Source: UniProtKB
Cellular component	nucleolus Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein C-terminus binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactionsHide

With	Entry	#Exp.	IntAct	Notes
ABL1	P00519	1	EBI-876367,EBI-375543
FYN	P06241	1	EBI-876367,EBI-515315
SRC	P12931	1	EBI-876367,EBI-621482

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.

Sequence annotation (Features)Hide

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 3256

3256

Antigen KI-67

PRO_0000084301

Regions

Domain

27 – 76

50

FHA

Repeat

1000 – 1112

113

1

Repeat

1122 – 1234

113

2

Repeat

1244 – 1356

113

3

Repeat

1366 – 1477

112

4

Repeat

1487 – 1598

112

5

Repeat

1608 – 1720

113

6

Repeat

1730 – 1842

113

7

Repeat

1851 – 1964

114

8

Repeat

1974 – 2086

113

9

Repeat

2096 – 2204

109

10

Repeat

2214 – 2326

113

11

Repeat

2335 – 2447

113

12

Repeat

2457 – 2569

113

13

Repeat

2579 – 2689

111

14

Repeat

2699 – 2808

110

15

Repeat

2818 – 2928

111

16

Nucleotide binding

3034 – 3041

8

ATP Potential

Region

1000 – 2928

1929

16 X 122 AA approximate repeats

Amino acid modifications

Modified residue

108

1

Phosphoserine Ref.9 Ref.12

Modified residue

109

1

Phosphothreonine Ref.12

Modified residue

125

1

Phosphoserine Ref.11 Ref.16

Modified residue

128

1

Phosphoserine Ref.12 Ref.11 Ref.16

Modified residue

131

1

Phosphoserine Ref.16

Modified residue

264

1

Phosphoserine Ref.12 Ref.16

Modified residue

308

1

Phosphoserine Ref.9 Ref.12 Ref.16 Ref.7 Ref.15 Ref.19

Modified residue

328

1

Phosphothreonine Ref.12 Ref.16 Ref.8

Modified residue

347

1

Phosphothreonine Ref.16 Ref.19

Modified residue

352

1

Phosphoserine Ref.13

Modified residue

357

1

Phosphoserine Ref.12 Ref.11 Ref.16 Ref.15 Ref.19 Ref.8 Ref.13 Ref.6 Ref.14

Modified residue

374

1

Phosphoserine Ref.9 Ref.12 Ref.11 Ref.16

Modified residue

401

1

Phosphothreonine Ref.16

Modified residue

411

1

Phosphoserine Ref.16

Modified residue

538

1

Phosphoserine Ref.16

Modified residue

543

1

Phosphothreonine Ref.9 Ref.16

Modified residue

579

1

Phosphoserine Ref.9 Ref.12 Ref.16 Ref.15 Ref.6 Ref.14 Ref.18

Modified residue

584

1

Phosphoserine Ref.12 Ref.16 Ref.15 Ref.19 Ref.14 Ref.18

Modified residue

630

1

Phosphoserine Ref.12

Modified residue

648

1

Phosphoserine Ref.9 Ref.12 Ref.11 Ref.16 Ref.15 Ref.19

Modified residue

713

1

Phosphoserine Ref.12

Modified residue

761

1

Phosphothreonine Ref.16

Modified residue

827

1

Phosphoserine Ref.12

Modified residue

859

1

Phosphoserine Ref.12 Ref.16

Modified residue

1017

1

Phosphothreonine Ref.16

Modified residue

1098

1

Phosphoserine Ref.9

Modified residue

1111

1

Phosphothreonine Ref.16 Ref.19

Modified residue

1131

1

Phosphoserine Ref.9 Ref.12 Ref.11 Ref.16 Ref.19

Modified residue

1139

1

Phosphothreonine Ref.11 Ref.16

Modified residue

1176

1

Phosphothreonine Ref.16

Modified residue

1193

1

Phosphothreonine Ref.9 Ref.19

Modified residue

1207

1

Phosphoserine Ref.16 Ref.10

Modified residue

1233

1

Phosphothreonine Ref.16 Ref.10

Modified residue

1237

1

Phosphothreonine Ref.16

Modified residue

1253

1

Phosphoserine Ref.9 Ref.16 Ref.17

Modified residue

1256

1

Phosphoserine Ref.16

Modified residue

1261

1

Phosphothreonine Ref.16 Ref.17

Modified residue

1298

1

Phosphothreonine Ref.11 Ref.16

Modified residue

1302

1

Phosphoserine Ref.11 Ref.16

Modified residue

1315

1

Phosphothreonine Ref.16

Modified residue

1327

1

Phosphothreonine Ref.9 Ref.19

Modified residue

1329

1

Phosphoserine Ref.19

Modified residue

1335

1

Phosphothreonine Ref.9 Ref.16 Ref.19 Ref.10

Modified residue

1355

1

Phosphothreonine Ref.16 Ref.10

Modified residue

1375

1

Phosphoserine Ref.9 Ref.16

Modified residue

1376

1

Phosphoserine Ref.16 Ref.6

Modified residue

1383

1

Phosphothreonine Ref.16

Modified residue

1503

1

Phosphothreonine Ref.12 Ref.16

Modified residue

1506

1

Phosphoserine Ref.16

Modified residue

1540

1

Phosphothreonine Ref.16

Modified residue

1546

1

Phosphoserine Ref.16

Modified residue

1552

1

Phosphotyrosine Ref.16

Modified residue

1557

1

Phosphothreonine Ref.9 Ref.12 Ref.16 Ref.19 Ref.10

Modified residue

1565

1

Phosphothreonine Ref.16

Modified residue

1569

1

Phosphothreonine Ref.12 Ref.16

Modified residue

1571

1

Phosphoserine Ref.12 Ref.16

Modified residue

1618

1

Phosphoserine Ref.11

Modified residue

1628

1

Phosphoserine Ref.12

Modified residue

1629

1

Phosphoserine Ref.12 Ref.11

Modified residue

1636

1

Phosphoserine Ref.10

Modified residue

1639

1

N6-acetyllysine Ref.20

Modified residue

1679

1

Phosphoserine Ref.12 Ref.16 Ref.15 Ref.10

Modified residue

1689

1

Phosphoserine Ref.16

Modified residue

1719

1

Phosphothreonine Ref.16

Modified residue

1721

1

Phosphoserine Ref.16

Modified residue

1726

1

Phosphoserine Ref.16

Modified residue

1740

1

Phosphoserine Ref.9 Ref.16

Modified residue

1747

1

Phosphothreonine Ref.16

Modified residue

1764

1

Phosphothreonine Ref.16 Ref.19 Ref.10

Modified residue

1784

1

Phosphothreonine Ref.16

Modified residue

1801

1

Phosphothreonine Ref.9 Ref.12 Ref.16 Ref.17

Modified residue

1815

1

Phosphoserine Ref.9 Ref.12 Ref.16

Modified residue

1841

1

Phosphothreonine Ref.16

Modified residue

1861

1

Phosphoserine Ref.9 Ref.12 Ref.16 Ref.14 Ref.17

Modified residue

1864

1

Phosphoserine Ref.16

Modified residue

1869

1

Phosphothreonine Ref.12 Ref.16 Ref.17

Modified residue

1897

1

Phosphothreonine Ref.12 Ref.10

Modified residue

1923

1

Phosphothreonine Ref.9 Ref.12 Ref.16 Ref.7 Ref.15 Ref.19

Modified residue

1937

1

Phosphoserine Ref.19 Ref.10

Modified residue

1983

1

Phosphoserine Ref.12

Modified residue

2002

1

Phosphoserine Ref.9

Modified residue

2005

1

N6-acetyllysine Ref.20

Modified residue

2065

1

Phosphothreonine Ref.16

Modified residue

2072

1

Phosphoserine Ref.16 Ref.19

Modified residue

2085

1

Phosphothreonine Ref.9 Ref.16

Modified residue

2105

1

Phosphoserine Ref.9 Ref.12 Ref.16

Modified residue

2113

1

Phosphothreonine Ref.12 Ref.16

Modified residue

2135

1

Phosphoserine Ref.16

Modified residue

2203

1

Phosphothreonine Ref.16

Modified residue

2211

1

Phosphothreonine Ref.16

Modified residue

2223

1

Phosphoserine Ref.9 Ref.12 Ref.11 Ref.16 Ref.7

Modified residue

2231

1

Phosphothreonine Ref.12 Ref.11 Ref.16

Modified residue

2239

1

Phosphoserine Ref.16

Modified residue

2264

1

N6-acetyllysine Ref.20

Modified residue

2285

1

Phosphothreonine Ref.16 Ref.10 Ref.17

Modified residue

2299

1

Phosphoserine Ref.16

Modified residue

2305

1

Phosphothreonine Ref.16 Ref.10

Modified residue

2325

1

Phosphothreonine Ref.16

Modified residue

2328

1

Phosphothreonine Ref.16

Modified residue

2332

1

Phosphothreonine Ref.16

Modified residue

2344

1

Phosphoserine Ref.12 Ref.16

Modified residue

2352

1

Phosphothreonine Ref.16

Modified residue

2355

1

Phosphoserine Ref.16

Modified residue

2389

1

Phosphothreonine Ref.12 Ref.16

Modified residue

2395

1

Phosphoserine Ref.16

Modified residue

2406

1

Phosphothreonine Ref.12 Ref.16 Ref.7 Ref.19 Ref.8

Modified residue

2420

1

Phosphoserine Ref.16

Modified residue

2426

1

Phosphothreonine Ref.16

Modified residue

2446

1

Phosphothreonine Ref.16

Modified residue

2466

1

Phosphoserine Ref.12 Ref.16

Modified residue

2471

1

Phosphoserine Ref.12

Modified residue

2505

1

Phosphoserine Ref.10

Modified residue

2508

1

Phosphothreonine Ref.10

Modified residue

2509

1

Phosphothreonine Ref.12

Modified residue

2528

1

Phosphoserine Ref.12 Ref.16 Ref.7

Modified residue

2588

1

Phosphoserine Ref.12 Ref.16

Modified residue

2638

1

Phosphoserine Ref.12

Modified residue

2708

1

Phosphoserine Ref.9 Ref.12 Ref.16 Ref.7 Ref.6

Modified residue

2827

1

Phosphoserine Ref.9 Ref.12 Ref.16

Modified residue

2828

1

Phosphoserine Ref.9 Ref.16

Modified residue

3041

1

Phosphoserine Ref.12 Ref.16

Modified residue

3042

1

Phosphoserine Ref.12

Modified residue

3082

1

Phosphoserine Ref.12

Modified residue

3207

1

Phosphoserine Ref.12

Modified residue

3213

1

Phosphothreonine Ref.15

Modified residue

3216

1

Phosphoserine Ref.15

Modified residue

3223

1

Phosphothreonine Ref.15

Natural variations

Alternative sequence

136 – 495

360

Missing in isoform Short.

VSP_004298

Natural variant

104

1

N → S. [dbSNP:rs2071498]

VAR_029055

Natural variant

238

1

W → R. [dbSNP:rs7095325]

VAR_029056

Natural variant

497

1

E → D. [dbSNP:rs11016076]

VAR_029057

Natural variant

574

1

Q → P. [dbSNP:rs4471342]

VAR_029058

Natural variant

631

1

I → L. [dbSNP:rs997983]

VAR_024161

Natural variant

832

1

R → W. [dbSNP:rs34916904]

VAR_033995

Natural variant

854

1

L → V. [dbSNP:rs2240]

VAR_024162

Natural variant

872

1

A → V. [dbSNP:rs2853344] Ref.1

VAR_029059

Natural variant

1042

1

G → S. [dbSNP:rs2152143]

VAR_024163

Natural variant

1120

1

T → S. [dbSNP:rs11016074]

VAR_029060

Natural variant

1247

1

T → I. [dbSNP:rs4750685]

VAR_021838

Natural variant

1403

1

E → V. [dbSNP:rs3740423]

VAR_020047

Natural variant

1470

1

L → W. [dbSNP:rs2853345] Ref.1

VAR_029061

Natural variant

1559

1

V → M. [dbSNP:rs7918199]

VAR_029062

Natural variant

1622

1

P → L. [dbSNP:rs2782871] Ref.1

VAR_029063

Natural variant

1849

1

T → A. [dbSNP:rs2782872] Ref.1

VAR_029064

Natural variant

1876

1

R → Q. [dbSNP:rs11591817]

VAR_029065

Natural variant

1951

1

L → I. [dbSNP:rs34116632]

VAR_033996

Natural variant

2101

1

I → T. [dbSNP:rs11016073]

VAR_029066

Natural variant

2337

1

T → N. [dbSNP:rs7083622]

VAR_024164

Natural variant

2363

1

N → S. [dbSNP:rs7071768]

VAR_029067

Natural variant

2607

1

R → H. [dbSNP:rs34688192]

VAR_061671

Natural variant

2608

1

P → L. [dbSNP:rs1063535]

VAR_024165

Natural variant

2649

1

R → H. [dbSNP:rs12777740]

VAR_029068

Natural variant

2720

1

T → P. [dbSNP:rs1050767]

VAR_024166

Natural variant

2760

1

D → G. [dbSNP:rs10082391]

VAR_029069

Natural variant

2786

1

R → Q. [dbSNP:rs10764749]

VAR_029070

Natural variant

2793

1

S → N. [dbSNP:rs10082533]

VAR_029071

Natural variant

2845

1

R → H. [dbSNP:rs11016072]

VAR_029072

Natural variant

2868

1

T → S. [dbSNP:rs2071496]

VAR_024167

Natural variant

2904

1

Q → R. [dbSNP:rs11016071]

VAR_029073

Natural variant

3097

1

N → D. [dbSNP:rs2798669] Ref.1

VAR_029074

Natural variant

3102

1

E → G. [dbSNP:rs34750407]

VAR_033997

Natural variant

3150

1

T → S. [dbSNP:rs11106]

VAR_014858

Natural variant

3217

1

K → E. [dbSNP:rs8473]

VAR_014859

Experimental info

Sequence conflict

619 – 626

8

RKSGNLPS → ERVATCLQ in CAA46519. Ref.1

Sequence conflict

619 – 626

8

RKSGNLPS → ERVATCLQ in CAA46520. Ref.1

Sequence conflict

2205

1

I → V in CAA46519. Ref.1

Sequence conflict

2205

1

I → V in CAA46520. Ref.1

Sequence conflict

2892 – 2893

2

KL → NV in CAA46519. Ref.1

Sequence conflict

2892 – 2893

2

KL → NV in CAA46520. Ref.1

Sequence conflict

3246

1

R → T in CAA46519. Ref.1

Sequence conflict

3246

1

R → T in CAA46520. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

3256

Helix Strand Turn

Details...

Beta strand

5 – 12

8

Beta strand

15 – 21

7

Beta strand

24 – 32

9

Beta strand

35 – 38

4

Beta strand

49 – 53

5

Beta strand

58 – 60

3

Beta strand

65 – 67

3

Beta strand

86 – 89

4

Beta strand

94 – 99

6

SequencesHide

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified November 28, 2006. Version 2. Checksum: 1332BC6C799AD64D	FASTA	3,256	358,694
	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
	Isoform Short. Checksum: 4FACAA90AC686C72	FASTA	2,896	319,444
	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 SDPDESEGIP LKRRRVSFGG HLRPELFDEN LPPNTPLKRG EAPTKRKSLV 190 200 210 220 230 240 MHTPPVLKKI IKEQPQPSGK QESGSEIHVE VKAQSLVISP PAPSPRKTPV ASDQRRRSCK 250 260 270 280 290 300 TAPASSSKSQ TEVPKRGGRK SGNLPSKRVS ISRSQHDILQ MICSKRRSGA SEANLIVAKS 310 320 330 340 350 360 WADVVKLGAK QTQTKVIKHG PQRSMNKRQR RPATPKKPVG EVHSQFSTGH ANSPCTIIIG 370 380 390 400 410 420 KAHTEKVHVP ARPYRVLNNF ISNQKMDFKE DLSGIAEMFK TPVKEQPQLT STCHIAISNS 430 440 450 460 470 480 ENLLGKQFQG TDSGEEPLLP TSESFGGNVF FSAQNAAKQP SDKCSASPPL RRQCIRENGN 490 500 510 520 530 540 VAKTPRNTYK MTSLETKTSD TETEPSKTVS TANRSGRSTE FRNIQKLPVE SKSEETNTEI 550 560 570 580 590 600 VECILKRGQK ATLLQQRREG EMKEIERPFE TYKENIELKE NDEKMKAMKR SRTWGQKCAP 610 620 630 640 650 660 MSDLTDLKSL PDTELMKDTA RGQNLLQTQD HAKAPKSEKG KITKMPCQSL QPEPINTPTH 670 680 690 700 710 720 TKQQLKASLG KVGVKEELLA VGKFTRTSGE TTHTHREPAG DGKSIRTFKE SPKQILDPAA 730 740 750 760 770 780 RVTGMKKWPR TPKEEAQSLE DLAGFKELFQ TPGPSEESMT DEKTTKIACK SPPPESVDTP 790 800 810 820 830 840 TSTKQWPKRS LRKADVEEEF LALRKLTPSA GKAMLTPKPA GGDEKDIKAF MGTPVQKLDL 850 860 870 880 890 900 AGTLPGSKRQ LQTPKEKAQA LEDLAGFKEL FQTPGHTEEL VAAGKTTKIP CDSPQSDPVD 910 920 930 940 950 960 TPTSTKQRPK RSIRKADVEG ELLACRNLMP SAGKAMHTPK PSVGEEKDII IFVGTPVQKL 970 980 990 1000 1010 1020 DLTENLTGSK RRPQTPKEEA QALEDLTGFK ELFQTPGHTE EAVAAGKTTK MPCESSPPES 1030 1040 1050 1060 1070 1080 ADTPTSTRRQ PKTPLEKRDV QKELSALKKL TQTSGETTHT DKVPGGEDKS INAFRETAKQ 1090 1100 1110 1120 1130 1140 KLDPAASVTG SKRHPKTKEK AQPLEDLAGL KELFQTPVCT DKPTTHEKTT KIACRSQPDP 1150 1160 1170 1180 1190 1200 VDTPTSSKPQ SKRSLRKVDV EEEFFALRKR TPSAGKAMHT PKPAVSGEKN IYAFMGTPVQ 1210 1220 1230 1240 1250 1260 KLDLTENLTG SKRRLQTPKE KAQALEDLAG FKELFQTRGH TEESMTNDKT AKVACKSSQP 1270 1280 1290 1300 1310 1320 DPDKNPASSK RRLKTSLGKV GVKEELLAVG KLTQTSGETT HTHTEPTGDG KSMKAFMESP 1330 1340 1350 1360 1370 1380 KQILDSAASL TGSKRQLRTP KGKSEVPEDL AGFIELFQTP SHTKESMTNE KTTKVSYRAS 1390 1400 1410 1420 1430 1440 QPDLVDTPTS SKPQPKRSLR KADTEEEFLA FRKQTPSAGK AMHTPKPAVG EEKDINTFLG 1450 1460 1470 1480 1490 1500 TPVQKLDQPG NLPGSNRRLQ TRKEKAQALE ELTGFRELFQ TPCTDNPTTD EKTTKKILCK 1510 1520 1530 1540 1550 1560 SPQSDPADTP TNTKQRPKRS LKKADVEEEF LAFRKLTPSA GKAMHTPKAA VGEEKDINTF 1570 1580 1590 1600 1610 1620 VGTPVEKLDL LGNLPGSKRR PQTPKEKAKA LEDLAGFKEL FQTPGHTEES MTDDKITEVS 1630 1640 1650 1660 1670 1680 CKSPQPDPVK TPTSSKQRLK ISLGKVGVKE EVLPVGKLTQ TSGKTTQTHR ETAGDGKSIK 1690 1700 1710 1720 1730 1740 AFKESAKQML DPANYGTGME RWPRTPKEEA QSLEDLAGFK ELFQTPDHTE ESTTDDKTTK 1750 1760 1770 1780 1790 1800 IACKSPPPES MDTPTSTRRR PKTPLGKRDI VEELSALKQL TQTTHTDKVP GDEDKGINVF 1810 1820 1830 1840 1850 1860 RETAKQKLDP AASVTGSKRQ PRTPKGKAQP LEDLAGLKEL FQTPICTDKP TTHEKTTKIA 1870 1880 1890 1900 1910 1920 CRSPQPDPVG TPTIFKPQSK RSLRKADVEE ESLALRKRTP SVGKAMDTPK PAGGDEKDMK 1930 1940 1950 1960 1970 1980 AFMGTPVQKL DLPGNLPGSK RWPQTPKEKA QALEDLAGFK ELFQTPGTDK PTTDEKTTKI 1990 2000 2010 2020 2030 2040 ACKSPQPDPV DTPASTKQRP KRNLRKADVE EEFLALRKRT PSAGKAMDTP KPAVSDEKNI 2050 2060 2070 2080 2090 2100 NTFVETPVQK LDLLGNLPGS KRQPQTPKEK AEALEDLVGF KELFQTPGHT EESMTDDKIT 2110 2120 2130 2140 2150 2160 EVSCKSPQPE SFKTSRSSKQ RLKIPLVKVD MKEEPLAVSK LTRTSGETTQ THTEPTGDSK 2170 2180 2190 2200 2210 2220 SIKAFKESPK QILDPAASVT GSRRQLRTRK EKARALEDLV DFKELFSAPG HTEESMTIDK 2230 2240 2250 2260 2270 2280 NTKIPCKSPP PELTDTATST KRCPKTRPRK EVKEELSAVE RLTQTSGQST HTHKEPASGD 2290 2300 2310 2320 2330 2340 EGIKVLKQRA KKKPNPVEEE PSRRRPRAPK EKAQPLEDLA GFTELSETSG HTQESLTAGK 2350 2360 2370 2380 2390 2400 ATKIPCESPP LEVVDTTAST KRHLRTRVQK VQVKEEPSAV KFTQTSGETT DADKEPAGED 2410 2420 2430 2440 2450 2460 KGIKALKESA KQTPAPAASV TGSRRRPRAP RESAQAIEDL AGFKDPAAGH TEESMTDDKT 2470 2480 2490 2500 2510 2520 TKIPCKSSPE LEDTATSSKR RPRTRAQKVE VKEELLAVGK LTQTSGETTH TDKEPVGEGK 2530 2540 2550 2560 2570 2580 GTKAFKQPAK RKLDAEDVIG SRRQPRAPKE KAQPLEDLAS FQELSQTPGH TEELANGAAD 2590 2600 2610 2620 2630 2640 SFTSAPKQTP DSGKPLKISR RVLRAPKVEP VGDVVSTRDP VKSQSKSNTS LPPLPFKRGG 2650 2660 2670 2680 2690 2700 GKDGSVTGTK RLRCMPAPEE IVEELPASKK QRVAPRARGK SSEPVVIMKR SLRTSAKRIE 2710 2720 2730 2740 2750 2760 PAEELNSNDM KTNKEEHKLQ DSVPENKGIS LRSRRQNKTE AEQQITEVFV LAERIEINRN 2770 2780 2790 2800 2810 2820 EKKPMKTSPE MDIQNPDDGA RKPIPRDKVT ENKRCLRSAR QNESSQPKVA EESGGQKSAK 2830 2840 2850 2860 2870 2880 VLMQNQKGKG EAGNSDSMCL RSRKTKSQPA ASTLESKSVQ RVTRSVKRCA ENPKKAEDNV 2890 CVKKIRTRSH RDSEDI

ReferencesHide

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[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. , 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.

Web resourcesHide

Wikipedia

Ki-67 entry

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.

IPI

IPI00004233.
IPI00413173.

PIR

A48666.

RefSeq

NP_001139438.1.
NP_002408.3.

UniGene

Hs.689823
Hs.80976

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R21	NMR	-	A	1-120	[»]
2AFF	NMR	-	A	1-120	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-28132N.

IntAct

P46013. 7 interactions.

MINT

MINT-137995.

STRING

P46013.

PTM databases

PhosphoSite

P46013.

Proteomic databases

PRIDE

P46013.

Genome annotation databases

Ensembl

ENST00000368654; ENSP00000357643; ENSG00000148773; Homo sapiens. [Genome view]

GeneID

4288.

KEGG

hsa:4288.

UCSC

uc001lke.1. human.
uc001lkf.1. human.

Organism-specific databases

CTD

4288.

GeneCards

GC10M129784.

HGNC

HGNC:7107. MKI67.

HPA

CAB000058.
HPA000451.
HPA001164.

MIM

176741. gene.

PharmGKB

PA30825.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG04868.

HOGENOM

HBG283314.

HOVERGEN

HBG006213.

InParanoid

P46013.

OMA

QTPKEKA.

OrthoDB

EOG9H1DFV.

PhylomeDB

P46013.

Gene expression databases

ArrayExpress

P46013.

Bgee

P46013.

CleanEx

HS_MKI67.

Genevestigator

P46013.

GermOnline

ENSG00000148773. Homo sapiens.

Family and domain databases

InterPro

IPR000253. FHA_dom.
IPR012568. K167R.
IPR008984. SMAD_FHA_domain.
[Graphical view]

Pfam

PF00498. FHA. 1 hit.
PF08065. K167R. 16 hits.
[Graphical view]

SMART

SM00240. FHA. 1 hit.
[Graphical view]

SUPFAM

SSF49879. SMAD_FHA. 1 hit.

PROSITE

PS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

16881.

SOURCE

Search...

Entry informationHide

Entry name

KI67_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.