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Protein

Protein AATF

Gene

AATF

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

Functioni

May function as a general inhibitor of the histone deacetylase HDAC1. Binding to the pocket region of RB1 may displace HDAC1 from RB1/E2F complexes, leading to activation of E2F target genes and cell cycle progression. Conversely, displacement of HDAC1 from SP1 bound to the CDKN1A promoter leads to increased expression of this CDK inhibitor and blocks cell cycle progression. Also antagonizes PAWR mediated induction of aberrant amyloid peptide production in Alzheimer disease (presenile and senile dementia), although the molecular basis for this phenomenon has not been described to date.4 Publications

GO - Molecular functioni

  1. leucine zipper domain binding Source: UniProtKB
  2. poly(A) RNA binding Source: UniProtKB
  3. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. apoptotic signaling pathway Source: Reactome
  2. cell adhesion Source: Ensembl
  3. cellular response to DNA damage stimulus Source: UniProtKB
  4. embryonic cleavage Source: Ensembl
  5. negative regulation of amyloid precursor protein biosynthetic process Source: Ensembl
  6. negative regulation of apoptotic process Source: UniProtKB
  7. negative regulation of reactive oxygen species metabolic process Source: UniProtKB
  8. negative regulation of superoxide anion generation Source: UniProtKB
  9. neurotrophin TRK receptor signaling pathway Source: Reactome
  10. positive regulation of apoptotic process Source: Reactome
  11. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  12. regulation of mitotic cell cycle Source: Ensembl
  13. ribosome biogenesis Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_13638. NRAGE signals death through JNK.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein AATF
Alternative name(s):
Apoptosis-antagonizing transcription factor
Rb-binding protein Che-1
Gene namesi
Name:AATF
Synonyms:CHE1, DED
ORF Names:HSPC277
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:19235. AATF.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. centrosome Source: HPA
  2. cytoplasm Source: UniProtKB
  3. focal adhesion Source: HPA
  4. Golgi apparatus Source: Ensembl
  5. nucleolus Source: HPA
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128395780.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 560559Protein AATFPRO_0000056616Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei203 – 2031Phosphoserine2 Publications
Modified residuei316 – 3161Phosphoserine4 Publications
Modified residuei320 – 3201Phosphoserine4 Publications
Modified residuei321 – 3211Phosphoserine4 Publications

Post-translational modificationi

Hyperphosphorylated during the G1/S phase transition.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NY61.
PaxDbiQ9NY61.
PRIDEiQ9NY61.

2D gel databases

SWISS-2DPAGEQ9NY61.

PTM databases

PhosphoSiteiQ9NY61.

Expressioni

Tissue specificityi

Ubiquitously expressed. Expressed at high levels in brain, heart, kidney, placenta and thymus.2 Publications

Gene expression databases

BgeeiQ9NY61.
CleanExiHS_AATF.
GenevestigatoriQ9NY61.

Organism-specific databases

HPAiHPA004940.

Interactioni

Subunit structurei

Binds PAWR, POLR2J, RB1/RB, RBL1/P107, RBL2/P130, and SP1. May also bind MAPT.

Binary interactionsi

WithEntry#Exp.IntActNotes
ATMQ133153EBI-372428,EBI-495465
CHEK2O960174EBI-372428,EBI-1180783
Myl12aQ6ZWQ93EBI-372428,EBI-8034418From a different organism.
RELAQ042063EBI-372428,EBI-73886

Protein-protein interaction databases

BioGridi117743. 42 interactions.
IntActiQ9NY61. 16 interactions.
MINTiMINT-131397.
STRINGi9606.ENSP00000225402.

Structurei

3D structure databases

ProteinModelPortaliQ9NY61.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni273 – 31543POLR2J bindingAdd
BLAST
Regioni316 – 37257RB1 bindingAdd
BLAST
Regioni373 – 472100RB1 and SP1 bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi96 – 195100Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the AATF family.Curated

Phylogenomic databases

eggNOGiNOG270454.
GeneTreeiENSGT00390000000288.
HOGENOMiHOG000007555.
HOVERGENiHBG080805.
InParanoidiQ9NY61.
KOiK14782.
OMAiQLHPPDE.
OrthoDBiEOG7VDXQ2.
PhylomeDBiQ9NY61.
TreeFamiTF324341.

Family and domain databases

InterProiIPR025160. AATF.
IPR012617. AATF_C.
[Graphical view]
PfamiPF13339. AATF-Che1. 1 hit.
PF08164. TRAUB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9NY61-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGPQPLALQ LEQLLNPRPS EADPEADPEE ATAARVIDRF DEGEDGEGDF
60 70 80 90 100
LVVGSIRKLA SASLLDTDKR YCGKTTSRKA WNEDHWEQTL PGSSDEEISD
110 120 130 140 150
EEGSGDEDSE GLGLEEYDED DLGAAEEQEC GDHRESKKSR SHSAKTPGFS
160 170 180 190 200
VQSISDFEKF TKGMDDLGSS EEEEDEESGM EEGDDAEDSQ GESEEDRAGD
210 220 230 240 250
RNSEDDGVVM TFSSVKVSEE VEKGRAVKNQ IALWDQLLEG RIKLQKALLT
260 270 280 290 300
TNQLPQPDVF PLFKDKGGPE FSSALKNSHK ALKALLRSLV GLQEELLFQY
310 320 330 340 350
PDTRYLVDGT KPNAGSEEIS SEDDELVEEK KQQRRRVPAK RKLEMEDYPS
360 370 380 390 400
FMAKRFADFT VYRNRTLQKW HDKTKLASGK LGKGFGAFER SILTQIDHIL
410 420 430 440 450
MDKERLLRRT QTKRSVYRVL GKPEPAAQPV PESLPGEPEI LPQAPANAHL
460 470 480 490 500
KDLDEEIFDD DDFYHQLLRE LIERKTSSLD PNDQVAMGRQ WLAIQKLRSK
510 520 530 540 550
IHKKVDRKAS KGRKLRFHVL SKLLSFMAPI DHTTMNDDAR TELYRSLFGQ
560
LHPPDEGHGD
Length:560
Mass (Da):63,133
Last modified:October 1, 2000 - v1
Checksum:iEC493EF3B4C3A199
GO

Sequence cautioni

The sequence AAD52016.1 differs from that shown. Reason: Frameshift at positions 355, 365, 487, 498 and 503. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 32AG → GR in AAD52016 (PubMed:10783144).Curated
Sequence conflicti4 – 52Missing in AAD52016 (PubMed:10783144).Curated
Sequence conflicti139 – 1391S → T in AAD52016 (PubMed:10783144).Curated
Sequence conflicti262 – 2621L → V in AAD52016 (PubMed:10783144).Curated
Sequence conflicti272 – 2721S → A in AAD52016 (PubMed:10783144).Curated
Sequence conflicti306 – 3061L → V in AAD52016 (PubMed:10783144).Curated
Sequence conflicti402 – 4021D → C in AAD52016 (PubMed:10783144).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ249940 mRNA. Translation: CAB57451.2.
AF083208 mRNA. Translation: AAD52016.1. Frameshift.
AK057229 mRNA. Translation: BAG51888.1.
AC003103 Genomic DNA. No translation available.
CH471199 Genomic DNA. Translation: EAW57575.1.
BC000591 mRNA. Translation: AAH00591.1.
AF161395 mRNA. Translation: AAF28955.1.
CCDSiCCDS32632.1.
RefSeqiNP_036270.1. NM_012138.3.
UniGeneiHs.195740.

Genome annotation databases

EnsembliENST00000619387; ENSP00000477848; ENSG00000275700.
ENST00000620004; ENSP00000481894; ENSG00000276072.
GeneIDi26574.
KEGGihsa:26574.
UCSCiuc002hni.3. human.

Polymorphism databases

DMDMi71152211.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ249940 mRNA. Translation: CAB57451.2.
AF083208 mRNA. Translation: AAD52016.1. Frameshift.
AK057229 mRNA. Translation: BAG51888.1.
AC003103 Genomic DNA. No translation available.
CH471199 Genomic DNA. Translation: EAW57575.1.
BC000591 mRNA. Translation: AAH00591.1.
AF161395 mRNA. Translation: AAF28955.1.
CCDSiCCDS32632.1.
RefSeqiNP_036270.1. NM_012138.3.
UniGeneiHs.195740.

3D structure databases

ProteinModelPortaliQ9NY61.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117743. 42 interactions.
IntActiQ9NY61. 16 interactions.
MINTiMINT-131397.
STRINGi9606.ENSP00000225402.

PTM databases

PhosphoSiteiQ9NY61.

Polymorphism databases

DMDMi71152211.

2D gel databases

SWISS-2DPAGEQ9NY61.

Proteomic databases

MaxQBiQ9NY61.
PaxDbiQ9NY61.
PRIDEiQ9NY61.

Protocols and materials databases

DNASUi26574.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000619387; ENSP00000477848; ENSG00000275700.
ENST00000620004; ENSP00000481894; ENSG00000276072.
GeneIDi26574.
KEGGihsa:26574.
UCSCiuc002hni.3. human.

Organism-specific databases

CTDi26574.
GeneCardsiGC17P035306.
HGNCiHGNC:19235. AATF.
HPAiHPA004940.
MIMi608463. gene.
neXtProtiNX_Q9NY61.
PharmGKBiPA128395780.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG270454.
GeneTreeiENSGT00390000000288.
HOGENOMiHOG000007555.
HOVERGENiHBG080805.
InParanoidiQ9NY61.
KOiK14782.
OMAiQLHPPDE.
OrthoDBiEOG7VDXQ2.
PhylomeDBiQ9NY61.
TreeFamiTF324341.

Enzyme and pathway databases

ReactomeiREACT_13638. NRAGE signals death through JNK.

Miscellaneous databases

ChiTaRSiAATF. human.
GeneWikiiApoptosis-antagonizing_transcription_factor.
GenomeRNAii26574.
NextBioi48910.
PROiQ9NY61.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NY61.
CleanExiHS_AATF.
GenevestigatoriQ9NY61.

Family and domain databases

InterProiIPR025160. AATF.
IPR012617. AATF_C.
[Graphical view]
PfamiPF13339. AATF-Che1. 1 hit.
PF08164. TRAUB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of novel transcription factor-like gene from human intestinal cells."
    Lindfors K., Halttunen T., Huotari P., Nupponen N., Vihinen M., Visakorpi T., Maki M., Kainulainen H.
    Biochem. Biophys. Res. Commun. 276:660-666(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Identification of a novel partner of RNA polymerase II subunit 11, Che-1, which interacts with and affects the growth suppression function of Rb."
    Fanciulli M., Bruno T., Di Padova M., De Angelis R., Iezzi S., Iacobini C., Floridi A., Passananti C.
    FASEB J. 14:904-912(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH POLR2J AND RB1, TISSUE SPECIFICITY.
    Tissue: Skeletal muscle.
  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].
    Tissue: Testis.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Skin.
  7. "Human partial CDS from CD34+ stem cells."
    Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 361-560.
    Tissue: Umbilical cord blood.
  8. Cited for: FUNCTION, PHOSPHORYLATION AT THE G1/S TRANSITION, INTERACTION WITH RB1; RBL1 AND RBL2.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter."
    Di Padova M., Bruno T., De Nicola F., Iezzi S., D'Angelo C., Gallo R., Nicosia D., Corbi N., Biroccio A., Floridi A., Passananti C., Fanciulli M.
    J. Biol. Chem. 278:36496-36504(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SP1.
  11. "Rb binding protein Che-1 interacts with Tau in cerebellar granule neurons. Modulation during neuronal apoptosis."
    Barbato C., Corbi N., Canu N., Fanciulli M., Serafino A., Ciotti M., Libri V., Bruno T., Amadoro G., De Angelis R., Calissano P., Passananti C.
    Mol. Cell. Neurosci. 24:1038-1050(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPT.
  12. "AATF inhibits aberrant production of amyloid beta peptide 1-42 by interacting directly with Par-4."
    Guo Q., Xie J.
    J. Biol. Chem. 279:4596-4603(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PAWR.
  13. "AATF protects neural cells against oxidative damage induced by amyloid beta-peptide."
    Xie J., Guo Q.
    Neurobiol. Dis. 16:150-157(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-320 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "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-316; SER-320 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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-203; SER-316; SER-320 AND SER-321, 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-203; SER-316; SER-320 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAATF_HUMAN
AccessioniPrimary (citable) accession number: Q9NY61
Secondary accession number(s): A6NCJ6
, B3KQ26, Q9P0A4, Q9UNX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: October 1, 2000
Last modified: March 4, 2015
This is version 116 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.