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Q9BYG3

- MK67I_HUMAN

UniProt

Q9BYG3 - MK67I_HUMAN

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Protein
MKI67 FHA domain-interacting nucleolar phosphoprotein
Gene
NIFK, MKI67IP, NOPP34
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. RNA binding Source: UniProtKB
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. protein 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 MKI67.2 Publications

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 – 11Removed1 Publication
Chaini2 – 293292MKI67 FHA domain-interacting nucleolar phosphoprotein
PRO_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.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BYG3.
PaxDbiQ9BYG3.
PeptideAtlasiQ9BYG3.
PRIDEiQ9BYG3.

2D gel databases

SWISS-2DPAGEQ9BYG3.

PTM databases

PhosphoSiteiQ9BYG3.

Expressioni

Gene expression databases

ArrayExpressiQ9BYG3.
BgeeiQ9BYG3.
CleanExiHS_MKI67IP.
GenevestigatoriQ9BYG3.

Organism-specific databases

HPAiCAB015382.
HPA035735.
HPA035736.

Interactioni

Subunit structurei

Binds to the FHA domain of MKI67; this interaction is enhanced in mitosis.2 Publications

Protein-protein interaction databases

BioGridi124066. 42 interactions.
DIPiDIP-28134N.
IntActiQ9BYG3. 6 interactions.
MINTiMINT-1031770.
STRINGi9606.ENSP00000285814.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AFFNMR-B226-269[»]
ProteinModelPortaliQ9BYG3.
SMRiQ9BYG3. Positions 41-107, 228-267.

Miscellaneous databases

EvolutionaryTraceiQ9BYG3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 12379RRM
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni226 – 26944Interaction with MKI67
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG244773.
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

MATFSGPAGP ILSLNPQEDV EFQKEVAQVR KRITQRKKQE QLTPGVVYVR    50
HLPNLLDETQ IFSYFSQFGT VTRFRLSRSK RTGNSKGYAF VEFESEDVAK 100
IVAETMNNYL FGERLLECHF MPPEKVHKEL FKDWNIPFKQ PSYPSVKRYN 150
RNRTLTQKLR MEERFKKKER LLRKKLAKKG IDYDFPSLIL QKTESISKTN 200
RQTSTKGQVL RKKKKKVSGT LDTPEKTVDS QGPTPVCTPT FLERRKSQVA 250
ELNDDDKDDE IVFKQPISCV KEEIQETQTP THSRKKRRRS SNQ 293
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2135.1.
RefSeqi NP_115766.3. NM_032390.4.
UniGenei Hs.367842.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AFF NMR - B 226-269 [» ]
ProteinModelPortali Q9BYG3.
SMRi Q9BYG3. Positions 41-107, 228-267.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124066. 42 interactions.
DIPi DIP-28134N.
IntActi Q9BYG3. 6 interactions.
MINTi MINT-1031770.
STRINGi 9606.ENSP00000285814.

PTM databases

PhosphoSitei Q9BYG3.

Polymorphism databases

DMDMi 71151919.

2D gel databases

SWISS-2DPAGE Q9BYG3.

Proteomic databases

MaxQBi Q9BYG3.
PaxDbi Q9BYG3.
PeptideAtlasi Q9BYG3.
PRIDEi Q9BYG3.

Protocols and materials databases

DNASUi 84365.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000285814 ; ENSP00000285814 ; ENSG00000155438 .
GeneIDi 84365.
KEGGi hsa:84365.
UCSCi uc002tnk.3. human.

Organism-specific databases

CTDi 84365.
GeneCardsi GC02M122484.
HGNCi HGNC:17838. NIFK.
HPAi CAB015382.
HPA035735.
HPA035736.
MIMi 611970. gene.
neXtProti NX_Q9BYG3.
PharmGKBi PA38470.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG244773.
HOGENOMi HOG000242795.
HOVERGENi HBG057796.
InParanoidi Q9BYG3.
KOi K14838.
OMAi GIDYNFP.
OrthoDBi EOG7W6WNN.
PhylomeDBi Q9BYG3.
TreeFami TF315137.

Miscellaneous databases

EvolutionaryTracei Q9BYG3.
GeneWikii MKI67IP.
GenomeRNAii 84365.
NextBioi 74141.
PROi Q9BYG3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9BYG3.
Bgeei Q9BYG3.
CleanExi HS_MKI67IP.
Genevestigatori Q9BYG3.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR021043. hNIFK_FHA_Ki67_binding.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF12196. hNIFK_binding. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 121 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