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Protein

ESF1 homolog

Gene

ESF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May constitute a novel regulatory system for basal transcription. Negatively regulates ABT1 (By similarity).By similarity

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
ESF1 homolog
Alternative name(s):
ABT1-associated protein
Gene namesi
Name:ESF1
Synonyms:ABTAP, C20orf6
ORF Names:HDCMC28P
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15898. ESF1.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162385420.

Polymorphism and mutation databases

BioMutaiESF1.
DMDMi25452905.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 851850ESF1 homologPRO_0000079410Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei75 – 751PhosphoserineCombined sources
Modified residuei77 – 771PhosphoserineCombined sources
Modified residuei79 – 791PhosphoserineCombined sources
Modified residuei82 – 821PhosphoserineCombined sources
Modified residuei153 – 1531PhosphoserineCombined sources
Modified residuei179 – 1791PhosphoserineCombined sources
Modified residuei180 – 1801PhosphoserineCombined sources
Modified residuei198 – 1981PhosphoserineCombined sources
Modified residuei296 – 2961PhosphoserineCombined sources
Modified residuei298 – 2981PhosphoserineCombined sources
Modified residuei311 – 3111PhosphothreonineCombined sources
Modified residuei312 – 3121PhosphoserineCombined sources
Modified residuei313 – 3131PhosphoserineCombined sources
Modified residuei657 – 6571PhosphoserineCombined sources
Modified residuei663 – 6631PhosphoserineCombined sources
Modified residuei693 – 6931PhosphothreonineCombined sources
Modified residuei694 – 6941PhosphoserineCombined sources
Modified residuei735 – 7351PhosphoserineCombined sources
Modified residuei823 – 8231PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9H501.
MaxQBiQ9H501.
PaxDbiQ9H501.
PeptideAtlasiQ9H501.
PRIDEiQ9H501.

PTM databases

iPTMnetiQ9H501.
PhosphoSiteiQ9H501.

Expressioni

Gene expression databases

BgeeiQ9H501.
CleanExiHS_ESF1.
ExpressionAtlasiQ9H501. baseline and differential.
GenevisibleiQ9H501. HS.

Organism-specific databases

HPAiHPA047083.
HPA050396.

Interactioni

Subunit structurei

Interacts with ABT1. Forms a complex with ABT1 and suppresses the ABT1-induced activation of polymerase II-directed transcription in mammalian cells (By similarity).By similarity

Protein-protein interaction databases

BioGridi119620. 24 interactions.
IntActiQ9H501. 16 interactions.
MINTiMINT-252787.
STRINGi9606.ENSP00000202816.

Structurei

3D structure databases

ProteinModelPortaliQ9H501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili730 – 82495Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi87 – 17084Lys-richAdd
BLAST
Compositional biasi268 – 32154Asp-richAdd
BLAST
Compositional biasi567 – 851285Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the ESF1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2318. Eukaryota.
COG5638. LUCA.
GeneTreeiENSGT00390000004881.
HOGENOMiHOG000182523.
HOVERGENiHBG051149.
InParanoidiQ9H501.
OMAiIFENEPE.
OrthoDBiEOG7XDBFM.
PhylomeDBiQ9H501.
TreeFamiTF105822.

Family and domain databases

InterProiIPR012580. NUC153.
[Graphical view]
PfamiPF08159. NUC153. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9H501-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKQEIMSD QRFRRVAKDP RFWEMPEKDR KVKIDKRFRA MFHDKKFKLN
60 70 80 90 100
YAVDKRGRPI SHSTTEDLKR FYDLSDSDSN LSGEDSKALS QKKIKKKKTQ
110 120 130 140 150
TKKEIDSKNL VEKKKETKKA NHKGSENKTD LDNSIGIKKM KTSCKFKIDS
160 170 180 190 200
NISPKKDSKE FTQKNKKEKK NIVQHTTDSS LEEKQRTLDS GTSEIVKSPR
210 220 230 240 250
IECSKTRREM QSVVQLIMTR DSDGYENSTD GEMCDKDALE EDSESVSEIG
260 270 280 290 300
SDEESENEIT SVGRASGDDD GSEDDEEEDE DEEEDEDEDS EDDDKSDSGP
310 320 330 340 350
DLARGKGNIE TSSEDEDDTA DLFPEESGFE HAWRELDKDA PRADEITRRL
360 370 380 390 400
AVCNMDWDRL KAKDLLALFN SFKPKGGVIF SVKIYPSEFG KERMKEEQVQ
410 420 430 440 450
GPVELLSIPE DAPEKDWTSR EKLRDYQFKR LKYYYAVVDC DSPETASKIY
460 470 480 490 500
EDCDGLEFES SCSFIDLRFI PDDITFDDEP KDVASEVNLT AYKPKYFTSA
510 520 530 540 550
AMGTSTVEIT WDETDHERIT MLNRKFKKEE LLDMDFQAYL ASSSEDEEEI
560 570 580 590 600
EEELQGDDGV NVEEDGKTKK SQKDDEEQIA KYRQLLQVIQ EKEKKGKEND
610 620 630 640 650
MEMEIKWVPG LKESAEEMVK NKLEGKDKLT PWEQFLEKKK EKKRLKRKQK
660 670 680 690 700
ALAEEASEEE LPSDVDLNDP YFAEEVKQIG INKKSVKSAK DGTSPEEEIE
710 720 730 740 750
IERQKAEMAL LMMDEDEDSK KHFNYNKIVE HQNLSKKKKK QLMKKKELIE
760 770 780 790 800
DDFEVNVNDA RFQAMYTSHL FNLDPSDPNF KKTKAMEKIL EEKARQRERK
810 820 830 840 850
EQELTQAIKK KESEIEKESQ RKSIDPALSM LIKSIKTKTE QFQARKKQKV

K
Length:851
Mass (Da):98,796
Last modified:March 1, 2001 - v1
Checksum:i1BA283E7A0A65432
GO

Sequence cautioni

The sequence AAF65504.1 differs from that shown. Reason: Frameshift at position 664. Curated
The sequence BAA91123.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAB14167.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1861R → K in AAF65504 (Ref. 4) Curated
Sequence conflicti198 – 1981S → T in BAB14023 (PubMed:14702039).Curated
Sequence conflicti228 – 2281S → P in BAA91123 (PubMed:14702039).Curated
Sequence conflicti298 – 2981S → G in AAF65504 (Ref. 4) Curated
Sequence conflicti336 – 3361L → S in BAA91123 (PubMed:14702039).Curated
Sequence conflicti351 – 3511A → V in AAF65504 (Ref. 4) Curated
Sequence conflicti390 – 3901G → R in AAF65504 (Ref. 4) Curated
Sequence conflicti469 – 4691F → Y in AAF65504 (Ref. 4) Curated
Sequence conflicti474 – 4741I → V in BAA91123 (PubMed:14702039).Curated
Sequence conflicti483 – 4831V → A in AAF65504 (Ref. 4) Curated
Sequence conflicti514 – 5141T → S in BAB14023 (PubMed:14702039).Curated
Sequence conflicti593 – 5931E → K in AAH46107 (PubMed:15489334).Curated
Sequence conflicti829 – 8291S → P in BAB14167 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti386 – 3861P → L.
Corresponds to variant rs6079171 [ dbSNP | Ensembl ].
VAR_053082
Natural varianti550 – 5501I → T.2 Publications
Corresponds to variant rs3180370 [ dbSNP | Ensembl ].
VAR_024331
Natural varianti824 – 8241I → L.
Corresponds to variant rs34414644 [ dbSNP | Ensembl ].
VAR_053083

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161659 Genomic DNA. Translation: CAC07199.1.
AK000375 mRNA. Translation: BAA91123.1. Sequence problems.
AK022369 mRNA. Translation: BAB14023.1.
AK022670 mRNA. Translation: BAB14167.1. Different initiation.
BC046107 mRNA. Translation: AAH46107.1.
AF068285 mRNA. Translation: AAF65504.1. Frameshift.
CCDSiCCDS13117.1.
RefSeqiNP_001263309.1. NM_001276380.1.
NP_057733.2. NM_016649.3.
UniGeneiHs.369284.

Genome annotation databases

EnsembliENST00000202816; ENSP00000202816; ENSG00000089048.
GeneIDi51575.
KEGGihsa:51575.
UCSCiuc002woj.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161659 Genomic DNA. Translation: CAC07199.1.
AK000375 mRNA. Translation: BAA91123.1. Sequence problems.
AK022369 mRNA. Translation: BAB14023.1.
AK022670 mRNA. Translation: BAB14167.1. Different initiation.
BC046107 mRNA. Translation: AAH46107.1.
AF068285 mRNA. Translation: AAF65504.1. Frameshift.
CCDSiCCDS13117.1.
RefSeqiNP_001263309.1. NM_001276380.1.
NP_057733.2. NM_016649.3.
UniGeneiHs.369284.

3D structure databases

ProteinModelPortaliQ9H501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119620. 24 interactions.
IntActiQ9H501. 16 interactions.
MINTiMINT-252787.
STRINGi9606.ENSP00000202816.

PTM databases

iPTMnetiQ9H501.
PhosphoSiteiQ9H501.

Polymorphism and mutation databases

BioMutaiESF1.
DMDMi25452905.

Proteomic databases

EPDiQ9H501.
MaxQBiQ9H501.
PaxDbiQ9H501.
PeptideAtlasiQ9H501.
PRIDEiQ9H501.

Protocols and materials databases

DNASUi51575.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000202816; ENSP00000202816; ENSG00000089048.
GeneIDi51575.
KEGGihsa:51575.
UCSCiuc002woj.3. human.

Organism-specific databases

CTDi51575.
GeneCardsiESF1.
H-InvDBHIX0015649.
HGNCiHGNC:15898. ESF1.
HPAiHPA047083.
HPA050396.
neXtProtiNX_Q9H501.
PharmGKBiPA162385420.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2318. Eukaryota.
COG5638. LUCA.
GeneTreeiENSGT00390000004881.
HOGENOMiHOG000182523.
HOVERGENiHBG051149.
InParanoidiQ9H501.
OMAiIFENEPE.
OrthoDBiEOG7XDBFM.
PhylomeDBiQ9H501.
TreeFamiTF105822.

Miscellaneous databases

ChiTaRSiESF1. human.
GeneWikiiESF1.
GenomeRNAii51575.
NextBioi55409.
PROiQ9H501.

Gene expression databases

BgeeiQ9H501.
CleanExiHS_ESF1.
ExpressionAtlasiQ9H501. baseline and differential.
GenevisibleiQ9H501. HS.

Family and domain databases

InterProiIPR012580. NUC153.
[Graphical view]
PfamiPF08159. NUC153. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] OF 1-681 AND 702-851, VARIANT THR-550.
    Tissue: Mammary gland.
  3. "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] OF 1-595, VARIANT THR-550.
    Tissue: Mammary gland.
  4. "A novel gene from human dendritic cell."
    Zhao Z., Huang X., Li N., Zhu X., Cao X.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 185-672.
    Tissue: Dendritic cell.
  5. "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 SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-77; SER-79; SER-82; SER-153; SER-179; SER-180; SER-198; THR-311; SER-312; SER-313; SER-657; SER-663; THR-693; SER-694 AND SER-823, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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-657 AND SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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-75; SER-77; SER-79; SER-82; SER-153; SER-198; SER-296; THR-311; SER-312; SER-313; SER-657; SER-663 AND SER-735, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-75; SER-82; SER-153; SER-296; SER-298; THR-311; SER-312; SER-313; SER-657; SER-663 AND SER-694, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiESF1_HUMAN
AccessioniPrimary (citable) accession number: Q9H501
Secondary accession number(s): Q86X92
, Q9H9Q5, Q9HA35, Q9NX93, Q9P1S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: March 1, 2001
Last modified: April 13, 2016
This is version 124 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 20
    Human chromosome 20: 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. 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.