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Protein

BUB3-interacting and GLEBS motif-containing protein ZNF207

Gene

ZNF207

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

Functioni

Kinetochore- and microtubule-binding protein that plays a key role in spindle assembly (PubMed:24462186, PubMed:24462187, PubMed:26388440). ZNF207/BuGZ is mainly composed of disordered low-complexity regions and undergoes phase transition or coacervation to form temperature-dependent liquid droplets. Coacervation promotes microtubule bundling and concentrates tubulin, promoting microtubule polymerization and assembly of spindle and spindle matrix by concentrating its building blocks (PubMed:26388440). Also acts as a regulator of mitotic chromosome alignment by mediating the stability and kinetochore loading of BUB3 (PubMed:24462186, PubMed:24462187). Mechanisms by which BUB3 is protected are unclear: according to a first report, ZNF207/BuGZ may act by blocking ubiquitination and proteasomal degradation of BUB3 (PubMed:24462186). According to another report, the stabilization is independent of the proteasome (PubMed:24462187).3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri11 – 3424C2H2-type 1Add
BLAST
Zinc fingeri35 – 5824C2H2-type 2Add
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • heparin binding Source: Ensembl
  • microtubule binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • attachment of spindle microtubules to kinetochore Source: UniProtKB
  • cell division Source: UniProtKB-KW
  • microtubule bundle formation Source: UniProtKB
  • microtubule polymerization Source: UniProtKB
  • mitotic sister chromatid segregation Source: UniProtKB
  • mitotic spindle assembly Source: UniProtKB
  • mitotic spindle assembly checkpoint Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • regulation of chromosome segregation Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Mitosis

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
BUB3-interacting and GLEBS motif-containing protein ZNF2072 Publications
Short name:
BuGZ2 Publications
Short name:
hBuGZ1 Publication
Alternative name(s):
Zinc finger protein 207
Gene namesi
Name:ZNF207Imported
Synonyms:BUGZ2 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:12998. ZNF207.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB-KW
  • kinetochore Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • nucleolus Source: HPA
  • nucleus Source: UniProtKB
  • spindle Source: UniProtKB-SubCell
  • spindle matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi373 – 3742EE → AA in BuGZAA: Abolishes interaction with BUB3. 2 Publications

Organism-specific databases

PharmGKBiPA37578.

Polymorphism and mutation databases

BioMutaiZNF207.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478BUB3-interacting and GLEBS motif-containing protein ZNF207PRO_0000047453Add
BLAST

Proteomic databases

EPDiO43670.
MaxQBiO43670.
PaxDbiO43670.
PRIDEiO43670.

PTM databases

iPTMnetiO43670.
PhosphoSiteiO43670.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiO43670.
CleanExiHS_ZNF207.
ExpressionAtlasiO43670. baseline and differential.
GenevisibleiO43670. HS.

Organism-specific databases

HPAiHPA017013.
HPA063908.

Interactioni

Subunit structurei

Interacts (via GLEBS region) with BUB3.2 Publications

GO - Molecular functioni

  • microtubule binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113540. 25 interactions.
IntActiO43670. 20 interactions.
MINTiMINT-1661287.
STRINGi9606.ENSP00000378165.

Structurei

3D structure databases

ProteinModelPortaliO43670.
SMRiO43670. Positions 28-60.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9292Microtubule-binding region1 PublicationAdd
BLAST
Regioni359 – 39133GLEBS2 PublicationsAdd
BLAST

Domaini

The GLEBS region mediates interaction with BUB3 (PubMed:24462186, PubMed:24462187).2 Publications
The microtubule-binding region is required for efficient loading of BUB3 onto kinetochores and proper mitosis.1 Publication
Mainly composed of disordered low-complexity regions outside of the C2H2-type zinc fingers. Coacervation depends on hydrophobic and aromatic Phe and Tyr in the disordered low-complexity region, that may promote coacervation by forming intermolecular hydrophobic interactions.By similarity

Sequence similaritiesi

Contains 2 C2H2-type zinc fingers.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri11 – 3424C2H2-type 1Add
BLAST
Zinc fingeri35 – 5824C2H2-type 2Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2893. Eukaryota.
ENOG410ZJGQ. LUCA.
GeneTreeiENSGT00730000111057.
HOVERGENiHBG054182.
InParanoidiO43670.
OrthoDBiEOG7V4B11.
PhylomeDBiO43670.
TreeFamiTF313844.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 2 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: O43670-1) [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
MGRKKKKQLK PWCWYCNRDF DDEKILIQHQ KAKHFKCHIC HKKLYTGPGL
60 70 80 90 100
AIHCMQVHKE TIDAVPNAIP GRTDIELEIY GMEGIPEKDM DERRRLLEQK
110 120 130 140 150
TQESQKKKQQ DDSDEYDDDD SAASTSFQPQ PVQPQQGYIP PMAQPGLPPV
160 170 180 190 200
PGAPGMPPGI PPLMPGVPPL MPGMPPVMPG MPPGMMPMGG MMPPGPGIPP
210 220 230 240 250
LMPGMPPGMP PPVPRPGIPP MTQAQAVSAP GILNRPPAPT ATVPAPQPPV
260 270 280 290 300
TKPLFPSAGQ MGTPVTSSST ASSNSESLSA SSKALFPSTA QAQAAVQGPV
310 320 330 340 350
GTDFKPLNST PATTTEPPKP TFPAYTQSTA STTSTTNSTA AKPAASITSK
360 370 380 390 400
PATLTTTSAT SKLIHPDEDI SLEERRAQLP KYQRNLPRPG QAPIGNPPVG
410 420 430 440 450
PIGGMMPPQP GIPQQQGMRP PMPPHGQYGG HHQGMPGYLP GAMPPYGQGP
460 470
PMVPPYQGGP PRPPMGMRPP VMSQGGRY
Length:478
Mass (Da):50,751
Last modified:June 1, 1998 - v1
Checksum:i308B0303059052F7
GO
Isoform 2 (identifier: O43670-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     184-184: G → GLHHQRKYTQSFCGENI
     261-291: Missing.

Show »
Length:463
Mass (Da):49,692
Checksum:i21DC067E59CD808C
GO
Isoform 3 (identifier: O43670-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     48-146: Missing.
     184-184: G → GLHHQRKYTQSFCGENI

Show »
Length:395
Mass (Da):41,559
Checksum:i626A315EA03A5C3E
GO
Isoform 4 (identifier: O43670-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     184-184: G → GLHHQRKYTQSFCGENI

Note: No experimental confirmation available.
Show »
Length:494
Mass (Da):52,694
Checksum:iB77B795197A9D6E1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241A → S.
Corresponds to variant rs3795244 [ dbSNP | Ensembl ].
VAR_019974

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei48 – 14699Missing in isoform 3. 2 PublicationsVSP_006903Add
BLAST
Alternative sequencei184 – 1841G → GLHHQRKYTQSFCGENI in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_006904
Alternative sequencei261 – 29131Missing in isoform 2. 1 PublicationVSP_006905Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF046001 mRNA. Translation: AAC78561.1.
BT007365 mRNA. Translation: AAP36029.1.
AK291801 mRNA. Translation: BAF84490.1.
AK226172 mRNA. No translation available.
AC005899 Genomic DNA. No translation available.
CH471147 Genomic DNA. Translation: EAW80231.1.
CH471147 Genomic DNA. Translation: EAW80233.1.
CH471147 Genomic DNA. Translation: EAW80234.1.
CH471147 Genomic DNA. Translation: EAW80235.1.
CH471147 Genomic DNA. Translation: EAW80236.1.
CH471147 Genomic DNA. Translation: EAW80237.1.
BC002372 mRNA. Translation: AAH02372.1.
BC008023 mRNA. Translation: AAH08023.1.
CCDSiCCDS11271.1. [O43670-1]
CCDS32614.1. [O43670-2]
CCDS42294.1. [O43670-4]
RefSeqiNP_001027464.1. NM_001032293.2. [O43670-2]
NP_001091977.1. NM_001098507.1. [O43670-4]
NP_003448.1. NM_003457.3. [O43670-1]
UniGeneiHs.500775.

Genome annotation databases

EnsembliENST00000321233; ENSP00000322777; ENSG00000010244. [O43670-1]
ENST00000394670; ENSP00000378165; ENSG00000010244. [O43670-4]
ENST00000394673; ENSP00000378168; ENSG00000010244. [O43670-2]
GeneIDi7756.
KEGGihsa:7756.
UCSCiuc002hhh.5. human. [O43670-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF046001 mRNA. Translation: AAC78561.1.
BT007365 mRNA. Translation: AAP36029.1.
AK291801 mRNA. Translation: BAF84490.1.
AK226172 mRNA. No translation available.
AC005899 Genomic DNA. No translation available.
CH471147 Genomic DNA. Translation: EAW80231.1.
CH471147 Genomic DNA. Translation: EAW80233.1.
CH471147 Genomic DNA. Translation: EAW80234.1.
CH471147 Genomic DNA. Translation: EAW80235.1.
CH471147 Genomic DNA. Translation: EAW80236.1.
CH471147 Genomic DNA. Translation: EAW80237.1.
BC002372 mRNA. Translation: AAH02372.1.
BC008023 mRNA. Translation: AAH08023.1.
CCDSiCCDS11271.1. [O43670-1]
CCDS32614.1. [O43670-2]
CCDS42294.1. [O43670-4]
RefSeqiNP_001027464.1. NM_001032293.2. [O43670-2]
NP_001091977.1. NM_001098507.1. [O43670-4]
NP_003448.1. NM_003457.3. [O43670-1]
UniGeneiHs.500775.

3D structure databases

ProteinModelPortaliO43670.
SMRiO43670. Positions 28-60.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113540. 25 interactions.
IntActiO43670. 20 interactions.
MINTiMINT-1661287.
STRINGi9606.ENSP00000378165.

PTM databases

iPTMnetiO43670.
PhosphoSiteiO43670.

Polymorphism and mutation databases

BioMutaiZNF207.

Proteomic databases

EPDiO43670.
MaxQBiO43670.
PaxDbiO43670.
PRIDEiO43670.

Protocols and materials databases

DNASUi7756.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321233; ENSP00000322777; ENSG00000010244. [O43670-1]
ENST00000394670; ENSP00000378165; ENSG00000010244. [O43670-4]
ENST00000394673; ENSP00000378168; ENSG00000010244. [O43670-2]
GeneIDi7756.
KEGGihsa:7756.
UCSCiuc002hhh.5. human. [O43670-1]

Organism-specific databases

CTDi7756.
GeneCardsiZNF207.
HGNCiHGNC:12998. ZNF207.
HPAiHPA017013.
HPA063908.
MIMi603428. gene.
neXtProtiNX_O43670.
PharmGKBiPA37578.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2893. Eukaryota.
ENOG410ZJGQ. LUCA.
GeneTreeiENSGT00730000111057.
HOVERGENiHBG054182.
InParanoidiO43670.
OrthoDBiEOG7V4B11.
PhylomeDBiO43670.
TreeFamiTF313844.

Miscellaneous databases

ChiTaRSiZNF207. human.
GenomeRNAii7756.
PROiO43670.
SOURCEiSearch...

Gene expression databases

BgeeiO43670.
CleanExiHS_ZNF207.
ExpressionAtlasiO43670. baseline and differential.
GenevisibleiO43670. HS.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 2 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ZNF207, a ubiquitously expressed zinc finger gene on chromosome 6p21.3."
    Pahl P.M.B., Hodges Y.K., Meltesen L., Perryman M.B., Horwitz K.B., Horwitz L.D.
    Genomics 53:410-412(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  3. "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] (ISOFORM 1).
    Tissue: Prostate.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Brain.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORMS 2 AND 3).
    Tissue: Lung.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "A microtubule-associated zinc finger protein, BuGZ, regulates mitotic chromosome alignment by ensuring Bub3 stability and kinetochore targeting."
    Jiang H., He X., Wang S., Jia J., Wan Y., Wang Y., Zeng R., Yates J. III, Zhu X., Zheng Y.
    Dev. Cell 28:268-281(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BUB3, MUTAGENESIS OF 373-GLU-GLU-374, MICROTUBULE-BINDING.
  10. "BuGZ is required for Bub3 stability, Bub1 kinetochore function, and chromosome alignment."
    Toledo C.M., Herman J.A., Olsen J.B., Ding Y., Corrin P., Girard E.J., Olson J.M., Emili A., Deluca J.G., Paddison P.J.
    Dev. Cell 28:282-294(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BUB3, MUTAGENESIS OF 373-GLU-GLU-374.
  11. "Phase transition of spindle-associated protein regulate spindle apparatus assembly."
    Jiang H., Wang S., Huang Y., He X., Cui H., Zhu X., Zheng Y.
    Cell 163:108-122(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiZN207_HUMAN
AccessioniPrimary (citable) accession number: O43670
Secondary accession number(s): A8K6Y6
, E1P660, E1P661, E1P662, Q53XS9, Q96HW5, Q9BUQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 149 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.