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Protein

MKI67 FHA domain-interacting nucleolar phosphoprotein

Gene

NIFK

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

Functioni

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of phosphatase activity Source: UniProtKB
  2. protein complex assembly Source: UniProtKB
  3. rRNA metabolic process Source: UniProtKB
  4. rRNA transcription Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
MKI67 FHA domain-interacting nucleolar phosphoprotein
Alternative name(s):
Nucleolar phosphoprotein Nopp34
Nucleolar protein interacting with the FHA domain of pKI-67
Short name:
hNIFK
Gene namesi
Name:NIFK
Synonyms:MKI67IP, NOPP34
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:17838. NIFK.

Subcellular locationi

Nucleusnucleolus. Chromosome
Note: Localizes to mitotic chromosomes in conjunction with MKI67.

GO - Cellular componenti

  1. condensed nuclear chromosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. nucleolus Source: UniProtKB
  4. nucleoplasm Source: UniProtKB
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi230 – 2301S → A: Loss of phosphorylation site. 1 Publication
Mutagenesisi234 – 2341T → A: Loss of phosphorylation site. Abrogates interaction with MKI67. 2 Publications
Mutagenesisi235 – 2351P → A: Reduces phosphorylation at T-234. 1 Publication
Mutagenesisi238 – 2381T → A: Loss of phosphorylation site. Abrogates interaction with MKI67. 2 Publications
Mutagenesisi239 – 2391P → A: Reduces phosphorylation at T-234 and T-238. 1 Publication

Organism-specific databases

PharmGKBiPA38470.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 293292MKI67 FHA domain-interacting nucleolar phosphoproteinPRO_0000081629Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei218 – 2181Phosphoserine2 Publications
Modified residuei223 – 2231Phosphothreonine3 Publications
Modified residuei230 – 2301Phosphoserine1 Publication
Modified residuei234 – 2341Phosphothreonine3 Publications
Modified residuei238 – 2381Phosphothreonine2 Publications
Modified residuei247 – 2471Phosphoserine1 Publication
Modified residuei279 – 2791Phosphothreonine1 Publication

Post-translational modificationi

Sequentially phosphorylated on Thr-238, Thr-234 and Ser-230. Thr-234 is phosphorylated only when Thr-238 is phosphorylated. Likewise, phosphorylation at Ser-230 requires that Thr-234 and Thr-238 are phosphorylated. Phosphorylation enhances MKI67 binding.7 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BYG3.
PaxDbiQ9BYG3.
PeptideAtlasiQ9BYG3.
PRIDEiQ9BYG3.

2D gel databases

SWISS-2DPAGEQ9BYG3.

PTM databases

PhosphoSiteiQ9BYG3.

Expressioni

Gene expression databases

BgeeiQ9BYG3.
CleanExiHS_MKI67IP.
ExpressionAtlasiQ9BYG3. baseline and differential.
GenevestigatoriQ9BYG3.

Organism-specific databases

HPAiCAB015382.
HPA035735.
HPA035736.

Interactioni

Subunit structurei

Binds to the FHA domain of MKI67; this interaction is enhanced in mitosis.1 Publication

Protein-protein interaction databases

BioGridi124066. 130 interactions.
DIPiDIP-28134N.
IntActiQ9BYG3. 6 interactions.
MINTiMINT-1031770.
STRINGi9606.ENSP00000285814.

Structurei

Secondary structure

1
293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi239 – 25113Combined sources
Helixi254 – 2574Combined sources
Beta strandi260 – 2656Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AFFNMR-B226-269[»]
ProteinModelPortaliQ9BYG3.
SMRiQ9BYG3. Positions 41-107, 228-267.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BYG3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 12379RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni226 – 26944Interaction with MKI67Add
BLAST

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG244773.
GeneTreeiENSGT00390000011515.
HOGENOMiHOG000242795.
HOVERGENiHBG057796.
InParanoidiQ9BYG3.
KOiK14838.
OMAiGIDYNFP.
OrthoDBiEOG7W6WNN.
PhylomeDBiQ9BYG3.
TreeFamiTF315137.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR021043. hNIFK_FHA_Ki67_binding.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF12196. hNIFK_binding. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9BYG3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATFSGPAGP ILSLNPQEDV EFQKEVAQVR KRITQRKKQE QLTPGVVYVR
60 70 80 90 100
HLPNLLDETQ IFSYFSQFGT VTRFRLSRSK RTGNSKGYAF VEFESEDVAK
110 120 130 140 150
IVAETMNNYL FGERLLECHF MPPEKVHKEL FKDWNIPFKQ PSYPSVKRYN
160 170 180 190 200
RNRTLTQKLR MEERFKKKER LLRKKLAKKG IDYDFPSLIL QKTESISKTN
210 220 230 240 250
RQTSTKGQVL RKKKKKVSGT LDTPEKTVDS QGPTPVCTPT FLERRKSQVA
260 270 280 290
ELNDDDKDDE IVFKQPISCV KEEIQETQTP THSRKKRRRS SNQ
Length:293
Mass (Da):34,222
Last modified:June 1, 2001 - v1
Checksum:i9D288ECF2B4CE119
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti144 – 1441P → Q.1 Publication
Corresponds to variant rs17852212 [ dbSNP | Ensembl ].
VAR_027182

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB044971 mRNA. Translation: BAB41210.1.
AK291903 mRNA. Translation: BAF84592.1.
AC018737 Genomic DNA. Translation: AAY14830.1.
CH471103 Genomic DNA. Translation: EAW95261.1.
BC012457 mRNA. Translation: AAH12457.1.
BC022990 mRNA. Translation: AAH22990.1.
BC024238 mRNA. Translation: AAH24238.1.
CCDSiCCDS2135.1.
RefSeqiNP_115766.3. NM_032390.4.
UniGeneiHs.367842.

Genome annotation databases

EnsembliENST00000285814; ENSP00000285814; ENSG00000155438.
GeneIDi84365.
KEGGihsa:84365.
UCSCiuc002tnk.3. human.

Polymorphism databases

DMDMi71151919.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB044971 mRNA. Translation: BAB41210.1.
AK291903 mRNA. Translation: BAF84592.1.
AC018737 Genomic DNA. Translation: AAY14830.1.
CH471103 Genomic DNA. Translation: EAW95261.1.
BC012457 mRNA. Translation: AAH12457.1.
BC022990 mRNA. Translation: AAH22990.1.
BC024238 mRNA. Translation: AAH24238.1.
CCDSiCCDS2135.1.
RefSeqiNP_115766.3. NM_032390.4.
UniGeneiHs.367842.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AFFNMR-B226-269[»]
ProteinModelPortaliQ9BYG3.
SMRiQ9BYG3. Positions 41-107, 228-267.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124066. 130 interactions.
DIPiDIP-28134N.
IntActiQ9BYG3. 6 interactions.
MINTiMINT-1031770.
STRINGi9606.ENSP00000285814.

PTM databases

PhosphoSiteiQ9BYG3.

Polymorphism databases

DMDMi71151919.

2D gel databases

SWISS-2DPAGEQ9BYG3.

Proteomic databases

MaxQBiQ9BYG3.
PaxDbiQ9BYG3.
PeptideAtlasiQ9BYG3.
PRIDEiQ9BYG3.

Protocols and materials databases

DNASUi84365.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000285814; ENSP00000285814; ENSG00000155438.
GeneIDi84365.
KEGGihsa:84365.
UCSCiuc002tnk.3. human.

Organism-specific databases

CTDi84365.
GeneCardsiGC02M122485.
HGNCiHGNC:17838. NIFK.
HPAiCAB015382.
HPA035735.
HPA035736.
MIMi611970. gene.
neXtProtiNX_Q9BYG3.
PharmGKBiPA38470.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG244773.
GeneTreeiENSGT00390000011515.
HOGENOMiHOG000242795.
HOVERGENiHBG057796.
InParanoidiQ9BYG3.
KOiK14838.
OMAiGIDYNFP.
OrthoDBiEOG7W6WNN.
PhylomeDBiQ9BYG3.
TreeFamiTF315137.

Miscellaneous databases

EvolutionaryTraceiQ9BYG3.
GeneWikiiMKI67IP.
GenomeRNAii84365.
NextBioi74141.
PROiQ9BYG3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BYG3.
CleanExiHS_MKI67IP.
ExpressionAtlasiQ9BYG3. baseline and differential.
GenevestigatoriQ9BYG3.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR021043. hNIFK_FHA_Ki67_binding.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF12196. hNIFK_binding. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MKI67, MUTAGENESIS OF THR-234 AND THR-238, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skeletal muscle.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-144.
    Tissue: Brain, Lung and Placenta.
  6. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-24; 87-114; 180-192; 227-244 AND 272-284, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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: PHOSPHORYLATION AT THR-234, INTERACTION WITH MKI67.
  9. "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-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234; THR-238 AND THR-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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-218 AND THR-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-218; THR-223 AND SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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 226-269 IN COMPLEX WITH MKI67, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-230; THR-234; PRO-235; THR-238 AND PRO-239, PHOSPHORYLATION AT SER-230; THR-234 AND THR-238.

Entry informationi

Entry nameiMK67I_HUMAN
AccessioniPrimary (citable) accession number: Q9BYG3
Secondary accession number(s): A8K788, Q8TB66, Q96ED4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 126 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.