Skip Header

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

P46013

- KI67_HUMAN

UniProt

P46013 - KI67_HUMAN

(max 400 entries)x

Your basket is currently empty.

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

Protein

Antigen KI-67

Gene

MKI67

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Thought to be required for maintaining cell proliferation.

Regions

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

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:7107. MKI67.

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30825.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP46013.
PaxDbiP46013.
PRIDEiP46013.

PTM databases

PhosphoSiteiP46013.

Expressioni

Developmental stagei

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

Gene expression databases

BgeeiP46013.
CleanExiHS_MKI67.
GenevestigatoriP46013.

Organism-specific databases

HPAiCAB000058.
HPA000451.
HPA001164.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi110434. 27 interactions.
DIPiDIP-28132N.
IntActiP46013. 17 interactions.
MINTiMINT-137995.
STRINGi9606.ENSP00000357643.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP46013.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Contains 1 FHA domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00530000064425.
HOGENOMiHOG000113223.
HOVERGENiHBG006213.
InParanoidiP46013.
KOiK17582.
OMAiQTPKEKA.
OrthoDBiEOG76QFGJ.
PhylomeDBiP46013.
TreeFamiTF336000.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: P46013-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MWPTRRLVTI KRSGVDGPHF PLSLSTCLFG RGIECDIRIQ LPVVSKQHCK
60 70 80 90 100
IEIHEQEAIL HNFSSTNPTQ VNGSVIDEPV RLKHGDVITI IDRSFRYENE
110 120 130 140 150
SLQNGRKSTE FPRKIREQEP ARRVSRSSFS SDPDEKAQDS KAYSKITEGK
160 170 180 190 200
VSGNPQVHIK NVKEDSTADD SKDSVAQGTT NVHSSEHAGR NGRNAADPIS
210 220 230 240 250
GDFKEISSVK LVSRYGELKS VPTTQCLDNS KKNESPFWKL YESVKKELDV
260 270 280 290 300
KSQKENVLQY CRKSGLQTDY ATEKESADGL QGETQLLVSR KSRPKSGGSG
310 320 330 340 350
HAVAEPASPE QELDQNKGKG RDVESVQTPS KAVGASFPLY EPAKMKTPVQ
360 370 380 390 400
YSQQQNSPQK HKNKDLYTTG RRESVNLGKS EGFKAGDKTL TPRKLSTRNR
410 420 430 440 450
TPAKVEDAAD SATKPENLSS KTRGSIPTDV EVLPTETEIH NEPFLTLWLT
460 470 480 490 500
QVERKIQKDS LSKPEKLGTT AGQMCSGLPG LSSVDINNFG DSINESEGIP
510 520 530 540 550
LKRRRVSFGG HLRPELFDEN LPPNTPLKRG EAPTKRKSLV MHTPPVLKKI
560 570 580 590 600
IKEQPQPSGK QESGSEIHVE VKAQSLVISP PAPSPRKTPV ASDQRRRSCK
610 620 630 640 650
TAPASSSKSQ TEVPKRGGRK SGNLPSKRVS ISRSQHDILQ MICSKRRSGA
660 670 680 690 700
SEANLIVAKS WADVVKLGAK QTQTKVIKHG PQRSMNKRQR RPATPKKPVG
710 720 730 740 750
EVHSQFSTGH ANSPCTIIIG KAHTEKVHVP ARPYRVLNNF ISNQKMDFKE
760 770 780 790 800
DLSGIAEMFK TPVKEQPQLT STCHIAISNS ENLLGKQFQG TDSGEEPLLP
810 820 830 840 850
TSESFGGNVF FSAQNAAKQP SDKCSASPPL RRQCIRENGN VAKTPRNTYK
860 870 880 890 900
MTSLETKTSD TETEPSKTVS TANRSGRSTE FRNIQKLPVE SKSEETNTEI
910 920 930 940 950
VECILKRGQK ATLLQQRREG EMKEIERPFE TYKENIELKE NDEKMKAMKR
960 970 980 990 1000
SRTWGQKCAP MSDLTDLKSL PDTELMKDTA RGQNLLQTQD HAKAPKSEKG
1010 1020 1030 1040 1050
KITKMPCQSL QPEPINTPTH TKQQLKASLG KVGVKEELLA VGKFTRTSGE
1060 1070 1080 1090 1100
TTHTHREPAG DGKSIRTFKE SPKQILDPAA RVTGMKKWPR TPKEEAQSLE
1110 1120 1130 1140 1150
DLAGFKELFQ TPGPSEESMT DEKTTKIACK SPPPESVDTP TSTKQWPKRS
1160 1170 1180 1190 1200
LRKADVEEEF LALRKLTPSA GKAMLTPKPA GGDEKDIKAF MGTPVQKLDL
1210 1220 1230 1240 1250
AGTLPGSKRQ LQTPKEKAQA LEDLAGFKEL FQTPGHTEEL VAAGKTTKIP
1260 1270 1280 1290 1300
CDSPQSDPVD TPTSTKQRPK RSIRKADVEG ELLACRNLMP SAGKAMHTPK
1310 1320 1330 1340 1350
PSVGEEKDII IFVGTPVQKL DLTENLTGSK RRPQTPKEEA QALEDLTGFK
1360 1370 1380 1390 1400
ELFQTPGHTE EAVAAGKTTK MPCESSPPES ADTPTSTRRQ PKTPLEKRDV
1410 1420 1430 1440 1450
QKELSALKKL TQTSGETTHT DKVPGGEDKS INAFRETAKQ KLDPAASVTG
1460 1470 1480 1490 1500
SKRHPKTKEK AQPLEDLAGL KELFQTPVCT DKPTTHEKTT KIACRSQPDP
1510 1520 1530 1540 1550
VDTPTSSKPQ SKRSLRKVDV EEEFFALRKR TPSAGKAMHT PKPAVSGEKN
1560 1570 1580 1590 1600
IYAFMGTPVQ KLDLTENLTG SKRRLQTPKE KAQALEDLAG FKELFQTRGH
1610 1620 1630 1640 1650
TEESMTNDKT AKVACKSSQP DPDKNPASSK RRLKTSLGKV GVKEELLAVG
1660 1670 1680 1690 1700
KLTQTSGETT HTHTEPTGDG KSMKAFMESP KQILDSAASL TGSKRQLRTP
1710 1720 1730 1740 1750
KGKSEVPEDL AGFIELFQTP SHTKESMTNE KTTKVSYRAS QPDLVDTPTS
1760 1770 1780 1790 1800
SKPQPKRSLR KADTEEEFLA FRKQTPSAGK AMHTPKPAVG EEKDINTFLG
1810 1820 1830 1840 1850
TPVQKLDQPG NLPGSNRRLQ TRKEKAQALE ELTGFRELFQ TPCTDNPTTD
1860 1870 1880 1890 1900
EKTTKKILCK SPQSDPADTP TNTKQRPKRS LKKADVEEEF LAFRKLTPSA
1910 1920 1930 1940 1950
GKAMHTPKAA VGEEKDINTF VGTPVEKLDL LGNLPGSKRR PQTPKEKAKA
1960 1970 1980 1990 2000
LEDLAGFKEL FQTPGHTEES MTDDKITEVS CKSPQPDPVK TPTSSKQRLK
2010 2020 2030 2040 2050
ISLGKVGVKE EVLPVGKLTQ TSGKTTQTHR ETAGDGKSIK AFKESAKQML
2060 2070 2080 2090 2100
DPANYGTGME RWPRTPKEEA QSLEDLAGFK ELFQTPDHTE ESTTDDKTTK
2110 2120 2130 2140 2150
IACKSPPPES MDTPTSTRRR PKTPLGKRDI VEELSALKQL TQTTHTDKVP
2160 2170 2180 2190 2200
GDEDKGINVF RETAKQKLDP AASVTGSKRQ PRTPKGKAQP LEDLAGLKEL
2210 2220 2230 2240 2250
FQTPICTDKP TTHEKTTKIA CRSPQPDPVG TPTIFKPQSK RSLRKADVEE
2260 2270 2280 2290 2300
ESLALRKRTP SVGKAMDTPK PAGGDEKDMK AFMGTPVQKL DLPGNLPGSK
2310 2320 2330 2340 2350
RWPQTPKEKA QALEDLAGFK ELFQTPGTDK PTTDEKTTKI ACKSPQPDPV
2360 2370 2380 2390 2400
DTPASTKQRP KRNLRKADVE EEFLALRKRT PSAGKAMDTP KPAVSDEKNI
2410 2420 2430 2440 2450
NTFVETPVQK LDLLGNLPGS KRQPQTPKEK AEALEDLVGF KELFQTPGHT
2460 2470 2480 2490 2500
EESMTDDKIT EVSCKSPQPE SFKTSRSSKQ RLKIPLVKVD MKEEPLAVSK
2510 2520 2530 2540 2550
LTRTSGETTQ THTEPTGDSK SIKAFKESPK QILDPAASVT GSRRQLRTRK
2560 2570 2580 2590 2600
EKARALEDLV DFKELFSAPG HTEESMTIDK NTKIPCKSPP PELTDTATST
2610 2620 2630 2640 2650
KRCPKTRPRK EVKEELSAVE RLTQTSGQST HTHKEPASGD EGIKVLKQRA
2660 2670 2680 2690 2700
KKKPNPVEEE PSRRRPRAPK EKAQPLEDLA GFTELSETSG HTQESLTAGK
2710 2720 2730 2740 2750
ATKIPCESPP LEVVDTTAST KRHLRTRVQK VQVKEEPSAV KFTQTSGETT
2760 2770 2780 2790 2800
DADKEPAGED KGIKALKESA KQTPAPAASV TGSRRRPRAP RESAQAIEDL
2810 2820 2830 2840 2850
AGFKDPAAGH TEESMTDDKT TKIPCKSSPE LEDTATSSKR RPRTRAQKVE
2860 2870 2880 2890 2900
VKEELLAVGK LTQTSGETTH TDKEPVGEGK GTKAFKQPAK RKLDAEDVIG
2910 2920 2930 2940 2950
SRRQPRAPKE KAQPLEDLAS FQELSQTPGH TEELANGAAD SFTSAPKQTP
2960 2970 2980 2990 3000
DSGKPLKISR RVLRAPKVEP VGDVVSTRDP VKSQSKSNTS LPPLPFKRGG
3010 3020 3030 3040 3050
GKDGSVTGTK RLRCMPAPEE IVEELPASKK QRVAPRARGK SSEPVVIMKR
3060 3070 3080 3090 3100
SLRTSAKRIE PAEELNSNDM KTNKEEHKLQ DSVPENKGIS LRSRRQNKTE
3110 3120 3130 3140 3150
AEQQITEVFV LAERIEINRN EKKPMKTSPE MDIQNPDDGA RKPIPRDKVT
3160 3170 3180 3190 3200
ENKRCLRSAR QNESSQPKVA EESGGQKSAK VLMQNQKGKG EAGNSDSMCL
3210 3220 3230 3240 3250
RSRKTKSQPA ASTLESKSVQ RVTRSVKRCA ENPKKAEDNV CVKKIRTRSH

RDSEDI
Length:3,256
Mass (Da):358,694
Last modified:November 28, 2006 - v2
Checksum:i1332BC6C799AD64D
GO
Isoform Short (identifier: P46013-2) [UniParc]FASTAAdd to Basket

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

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

Experimental Info

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

Natural variant

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

Alternative sequence

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

Sequence databases

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

Genome annotation databases

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

Polymorphism databases

DMDMi118572663.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Ki-67 entry

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

BioGridi 110434. 27 interactions.
DIPi DIP-28132N.
IntActi P46013. 17 interactions.
MINTi MINT-137995.
STRINGi 9606.ENSP00000357643.

PTM databases

PhosphoSitei P46013.

Polymorphism databases

DMDMi 118572663.

Proteomic databases

MaxQBi P46013.
PaxDbi P46013.
PRIDEi P46013.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00530000064425.
HOGENOMi HOG000113223.
HOVERGENi HBG006213.
InParanoidi P46013.
KOi K17582.
OMAi QTPKEKA.
OrthoDBi EOG76QFGJ.
PhylomeDBi P46013.
TreeFami TF336000.

Miscellaneous databases

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

Gene expression databases

Bgeei P46013.
CleanExi HS_MKI67.
Genevestigatori P46013.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The cell proliferation-associated antigen of antibody Ki-67: a very large, ubiquitous nuclear protein with numerous repeated elements, representing a new kind of cell cycle-maintaining proteins."
    Schlueter C., Duchrow M., Wohlenberg C., Becker M.H.G., Key G., Flad H.-D., Gerdes J.
    J. Cell Biol. 123:513-522(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SHORT AND LONG), VARIANTS VAL-872; TRP-1470; LEU-1622; ALA-1849 AND ASP-3097.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Sequence of the human Ki-67 protein gene 5' and promoter region."
    Gerdes J.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
  4. "The forkhead-associated domain of Ki-67 antigen interacts with the novel kinesin-like protein Hklp2."
    Sueishi M., Takagi M., Yoneda Y.
    J. Biol. Chem. 275:28888-28892(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIF15.
  5. "A novel nucleolar protein, NIFK, interacts with the forkhead associated domain of Ki-67 antigen in mitosis."
    Takagi M., Sueishi M., Saiwaki T., Kametaka A., Yoneda Y.
    J. Biol. Chem. 276:25386-25391(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NIFK.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2406 AND SER-2708, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328; SER-357; SER-579; SER-584; SER-1131; THR-1327; THR-1569; THR-1801; THR-1923 AND THR-2406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1233; THR-1355; SER-1679 AND THR-1764, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357; SER-579; SER-584 AND SER-1861, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-357; SER-579; SER-648 AND SER-1679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-264; SER-308; THR-328; THR-347; SER-357; THR-401; SER-579; SER-584; SER-648; THR-761; SER-859; THR-1017; SER-1071; THR-1091; SER-1098; THR-1111; SER-1131; THR-1139; SER-1142; SER-1207; SER-1253; SER-1256; THR-1261; THR-1298; THR-1315; THR-1327; SER-1329; THR-1335; THR-1355; SER-1376; THR-1383; THR-1503; SER-1506; THR-1540; TYR-1552; THR-1557; THR-1569; SER-1571; SER-1679; SER-1689; THR-1719; SER-1721; SER-1740; THR-1747; THR-1784; THR-1801; THR-1841; SER-1861; SER-1864; THR-1869; THR-1923; THR-2065; SER-2072; THR-2085; SER-2105; THR-2113; THR-2203; SER-2223; THR-2231; SER-2239; THR-2285; THR-2325; THR-2328; THR-2333; SER-2344; THR-2352; THR-2389; SER-2395; THR-2406; SER-2528; SER-2588; SER-2708; SER-2827; SER-2828 AND SER-3041, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation."
    Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.
    J. Biol. Chem. 284:7542-7552(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH ASCL2; C11ORF30; HCFC1; HSPA8; CCAR2; MATR3; RBBP5; TUBB2A; WDR5 AND ZNF335.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648; SER-1131; THR-1335; THR-1557; THR-1764; SER-1937; THR-2406 AND SER-2420, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1639 AND LYS-2005, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-357; SER-579; SER-584; SER-648; THR-1091; SER-1098; SER-1131; THR-1167; THR-1193; SER-1207; THR-1233; THR-1315; THR-1327; SER-1329; THR-1335; THR-1355; THR-1557; THR-1569; SER-1571; SER-1679; THR-1747; THR-1801; SER-1815; SER-1861; THR-1897; THR-1923; SER-1937; THR-1963; SER-1983; THR-2065; SER-2072; THR-2085; SER-2105; SER-2135; SER-2223; THR-2231; THR-2233; SER-2239; THR-2268; THR-2285; THR-2325; SER-2344; THR-2389; SER-2395; THR-2406; SER-2420; THR-2446; SER-2528; SER-2588; SER-2708 AND SER-3128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-352; SER-357; SER-1098; SER-1131; SER-1496; SER-1861; SER-1983; SER-2072; SER-2105; SER-2344; SER-2528; SER-2588 AND SER-2708, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: INTERACTION WITH ZNF335.
  20. "Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
    Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
    Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  21. "Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions."
    Li H., Byeon I.-J., Ju Y., Tsai M.-D.
    J. Mol. Biol. 335:371-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-120 IN COMPLEX WITH NIFK.
  22. "Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67."
    Byeon I.-J., Li H., Song H., Gronenborn A.M., Tsai M.-D.
    Nat. Struct. Mol. Biol. 12:987-993(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-120 IN COMPLEX WITH NIFK.

Entry informationi

Entry nameiKI67_HUMAN
AccessioniPrimary (citable) accession number: P46013
Secondary accession number(s): Q5VWH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 28, 2006
Last modified: October 29, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3