GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

CHICK:Q90YL2

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Gallus gallus (Chicken). (9031)
Gene Name(s) No Information Provided.
Protein Name(s) Cardiac muscle factor 1 (ECO:0000313 with EMBL:AAK60425.1)
External Links
UniProt Q90YL2
EMBL AY035224
UniGene Gga.3705
Gga.49793
ProteinModelPortal Q90YL2
STRING 9031.ENSGALP00000015880
PaxDb Q90YL2
eggNOG NOG12793
HOGENOM HOG000169807
HOVERGEN HBG075257
PhylomeDB Q90YL2
GO GO:0000775
GO:0000940
GO:0005737
GO:0005635
GO:0016363
GO:0005634
GO:0000922
GO:0045502
GO:0042803
GO:0008134
GO:0007059
GO:0051310
GO:0000278
GO:0045892
GO:0016202
InterPro IPR018302
IPR019513
Pfam PF10490
PF10473

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0051310

metaphase plate congression

PMID:15870278[1]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P49454

P

Seeded From UniProt

complete

involved_in

GO:0045892

negative regulation of transcription, DNA-templated

PMID:15677469[2]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P49454

P

Seeded From UniProt

complete

enables

GO:0070840

dynein complex binding

PMID:12974617[3]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P49454

F

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

PMID:7642639[4]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P49454

F

Seeded From UniProt

complete

part_of

GO:0016363

nuclear matrix

PMID:7542657[5]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P49454

C

Seeded From UniProt

complete

involved_in

GO:0016202

regulation of striated muscle tissue development

PMID:10373470[6]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q9QZ84

P

Seeded From UniProt

complete

enables

GO:0008134

transcription factor binding

PMID:15677469[2]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P49454

F

Seeded From UniProt

complete

involved_in

GO:0007059

chromosome segregation

PMID:16252009[7]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P49454

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:12974617[3]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P49454

C

Seeded From UniProt

complete

part_of

GO:0005635

nuclear envelope

PMID:12154071[8]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P49454

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:7542657[5]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P49454

C

Seeded From UniProt

complete

part_of

GO:0000940

condensed chromosome outer kinetochore

PMID:7542657[5]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P49454

C

Seeded From UniProt

complete

part_of

GO:0000922

spindle pole

PMID:7542657[5]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P49454

C

Seeded From UniProt

complete

part_of

GO:0000775

chromosome, centromeric region

PMID:7542657[5]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P49454

C

Seeded From UniProt

complete

involved_in

GO:0000278

mitotic cell cycle

PMID:7542657[5]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P49454

P

Seeded From UniProt

complete

enables

GO:0008134

transcription factor binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR019513

F

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR019513

F

Seeded From UniProt

complete

enables

GO:0070840

dynein complex binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR019513

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Yang, Z et al. (2005) Silencing mitosin induces misaligned chromosomes, premature chromosome decondensation before anaphase onset, and mitotic cell death. Mol. Cell. Biol. 25 4062-74 PubMed GONUTS page
  2. 2.0 2.1 Zhou, X et al. (2005) Mitosin/CENP-F as a negative regulator of activating transcription factor-4. J. Biol. Chem. 280 13973-7 PubMed GONUTS page
  3. 3.0 3.1 Yang, ZY et al. (2003) Mitosin/CENP-F is a conserved kinetochore protein subjected to cytoplasmic dynein-mediated poleward transport. Cell Res. 13 275-83 PubMed GONUTS page
  4. Zhu, X et al. (1995) The C terminus of mitosin is essential for its nuclear localization, centromere/kinetochore targeting, and dimerization. J. Biol. Chem. 270 19545-50 PubMed GONUTS page
  5. 5.0 5.1 5.2 5.3 5.4 5.5 Liao, H et al. (1995) CENP-F is a protein of the nuclear matrix that assembles onto kinetochores at late G2 and is rapidly degraded after mitosis. J. Cell Biol. 130 507-18 PubMed GONUTS page
  6. Goodwin, RL et al. (1999) The cloning and analysis of LEK1 identifies variations in the LEK/centromere protein F/mitosin gene family. J. Biol. Chem. 274 18597-604 PubMed GONUTS page
  7. Bomont, P et al. (2005) Unstable microtubule capture at kinetochores depleted of the centromere-associated protein CENP-F. EMBO J. 24 3927-39 PubMed GONUTS page
  8. Hussein, D & Taylor, SS (2002) Farnesylation of Cenp-F is required for G2/M progression and degradation after mitosis. J. Cell. Sci. 115 3403-14 PubMed GONUTS page