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Q5QJE6 (TDIF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxynucleotidyltransferase terminal-interacting protein 2
Alternative name(s):
Estrogen receptor-binding protein
LPTS-interacting protein 2
Short name=LPTS-RP2
Terminal deoxynucleotidyltransferase-interacting factor 2
Short name=TdIF2
Short name=TdT-interacting factor 2
Gene names
Name:DNTTIP2
Synonyms:ERBP, TDIF2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length756 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates the transcriptional activity of DNTT and ESR1. May function as a chromatin remodeling protein. Ref.1 Ref.2

Subunit structure

Forms a ternary complex with DNTT and core histone; interaction with PCNA releases DNTT and H2A/H2B histones from this ternary complex. Interacts with ESR1, ESR2, PPARG and RXRA. Ref.1 Ref.2

Subcellular location

Nucleus Ref.1 Ref.2.

Tissue specificity

Widely expressed with higher levels in testis. Ref.1 Ref.2

Sequence caution

The sequence AAA50601.1 differs from that shown. Reason: Frameshift at positions 717 and 726.

The sequence AAH47688.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence CAI21812.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processregulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 756756Deoxynucleotidyltransferase terminal-interacting protein 2
PRO_0000318505

Regions

Region548 – 60558TdBR region; mediates interaction with DNTT
Coiled coil505 – 54238 Potential

Amino acid modifications

Modified residue211Phosphoserine Ref.13 Ref.16
Modified residue1171Phosphoserine Ref.10 Ref.13 Ref.16 Ref.17
Modified residue1291Phosphothreonine Ref.13
Modified residue1411Phosphoserine Ref.12 Ref.13 Ref.15 Ref.16 Ref.17
Modified residue1451Phosphoserine Ref.13
Modified residue1481Phosphoserine Ref.13
Modified residue1841Phosphoserine Ref.13 Ref.15
Modified residue1941Phosphoserine Ref.13
Modified residue2321Phosphothreonine Ref.11 Ref.13 Ref.16 Ref.17
Modified residue2511Phosphoserine Ref.16
Modified residue3241Phosphoserine Ref.13
Modified residue3301Phosphoserine Ref.16
Modified residue3811Phosphoserine Ref.13
Modified residue4341Phosphoserine Ref.16 Ref.17
Modified residue5121Phosphoserine Ref.16 Ref.17
Modified residue6101Phosphothreonine Ref.16

Natural variations

Natural variant3091E → D. Ref.1 Ref.4 Ref.8 Ref.9
Corresponds to variant rs3747965 [ dbSNP | Ensembl ].
VAR_038748
Natural variant3411T → A.
Corresponds to variant rs3179879 [ dbSNP | Ensembl ].
VAR_038749
Natural variant4301A → V.
Corresponds to variant rs35650636 [ dbSNP | Ensembl ].
VAR_038750
Natural variant4771G → E.
Corresponds to variant rs41292661 [ dbSNP | Ensembl ].
VAR_061710
Natural variant6761Y → F.
Corresponds to variant rs12748154 [ dbSNP | Ensembl ].
VAR_038751

Experimental info

Sequence conflict471A → D in AAQ95169. Ref.2
Sequence conflict471A → D in AAA50601. Ref.3
Sequence conflict671R → S in AAQ95169. Ref.2
Sequence conflict671R → S in AAA50601. Ref.3
Sequence conflict6481M → I in BAD96442. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q5QJE6 [UniParc].

Last modified February 5, 2008. Version 2.
Checksum: 5C58EFABA2B42E4B

FASTA75684,469
        10         20         30         40         50         60 
MVVTRSARAK ASIQAASAES SGQKSFAANG IQAHPESSTG SDARTTAESQ TTGKQSLIPR 

        70         80         90        100        110        120 
TPKARKRKSR TTGSLPKGTE PSTDGETSEA ESNYSVSEHH DTILRVTRRR QILIACSPVS 

       130        140        150        160        170        180 
SVRKKPKVTP TKESYTEEIV SEAESHVSGI SRIVLPTEKT TGARRSKAKS LTDPSQESHT 

       190        200        210        220        230        240 
EAISDAETSS SDISFSGIAT RRTRSMQRKL KAQTEKKDSK IVPGNEKQIV GTPVNSEDSD 

       250        260        270        280        290        300 
TRQTSHLQAR SLSEINKPNF YNNDFDDDFS HRSSENILTV HEQANVESLK ETKQNCKDLD 

       310        320        330        340        350        360 
EDANGITDEG KEINEKSSQL KNLSELQDTS LQQLVSQRHS TPQNKNAVSV HSNLNSEAVM 

       370        380        390        400        410        420 
KSLTQTFATV EVGRWNNNKK SPIKASDLTK FGDCGGSDDE EESTVISVSE DMNSEGNVDF 

       430        440        450        460        470        480 
ECDTKLYTSA PNTSQGKDNS VLLVLSSDES QQSENSENEE DTLCFVENSG QRESLSGDTG 

       490        500        510        520        530        540 
SLSCDNALFV IDTTPGMSAD KNFYLEEEDK ASEVAIEEEK EEEEDEKSEE DSSDHDENED 

       550        560        570        580        590        600 
EFSDEEDFLN STKAKLLKLT SSSIDPGLSI KQLGGLYINF NADKLQSNKR TLTQIKEKKK 

       610        620        630        640        650        660 
NELLQKAVIT PDFEKNHCVP PYSESKYQLQ KKRRKERQKT AGDGWFGMKA PEMTNELKND 

       670        680        690        700        710        720 
LKALKMRASM DPKRFYKKND RDGFPKYFQI GTIVDNPADF YHSRIPKKQR KRTIVEELLA 

       730        740        750 
DSEFRRYNRR KYSEIMAEKA ANAAGKKFRK KKKFRN 

« Hide

References

« Hide 'large scale' references
[1]"Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone."
Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K., Fujisaki S., Hayano T., Koiwai O.
Genes Cells 8:559-571(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-309, FUNCTION, IDENTIFICATION IN A COMPLEX WITH DNTT; PCNA AND CORE HISTONE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Thymus.
[2]"ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor."
Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M., Zhu Y.-J.
Biochem. Biophys. Res. Commun. 317:54-59(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1; ESR2; PPARG AND RXRA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"cDNA encoding an acidic 82 kDa protein."
Carlsson P.
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[4]"LPTS-RP2, one LPTS-interacting protein."
Song H., Zhao M., Li T.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-309.
Tissue: Liver.
[5]"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. expand/collapse author list , 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.
[6]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon.
[7]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-309.
[9]"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 ASP-309.
Tissue: Brain and Skin.
[10]"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-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-117; THR-129; SER-141; SER-145; SER-148; SER-184; SER-194; THR-232; SER-324 AND SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"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-141 AND SER-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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-21; SER-117; SER-141; THR-232; SER-251; SER-330; SER-434; SER-512 AND THR-610, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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-117; SER-141; THR-232; SER-434 AND SER-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB046574 mRNA. Translation: BAD08331.1.
AY394925 mRNA. Translation: AAQ95169.1.
U15552 mRNA. Translation: AAA50601.1. Frameshift.
AY336729 mRNA. Translation: AAR02407.1.
AK292379 mRNA. Translation: BAF85068.1.
AK222722 mRNA. Translation: BAD96442.1.
AL049796 Genomic DNA. Translation: CAI21812.1. Sequence problems.
CH471097 Genomic DNA. Translation: EAW73064.1.
BC047688 mRNA. Translation: AAH47688.1. Sequence problems.
BC130622 mRNA. Translation: AAI30623.1.
CCDSCCDS44174.1.
PIRG01522.
RefSeqNP_055412.2. NM_014597.4.
UniGeneHs.601998.
Hs.85769.

3D structure databases

ProteinModelPortalQ5QJE6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119052. 16 interactions.
IntActQ5QJE6. 3 interactions.
MINTMINT-3026940.
STRING9606.ENSP00000352137.

PTM databases

PhosphoSiteQ5QJE6.

Polymorphism databases

DMDM166987398.

Proteomic databases

MaxQBQ5QJE6.
PaxDbQ5QJE6.
PRIDEQ5QJE6.

Protocols and materials databases

DNASU30836.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000436063; ENSP00000411010; ENSG00000067334.
GeneID30836.
KEGGhsa:30836.
UCSCuc001dqf.3. human.

Organism-specific databases

CTD30836.
GeneCardsGC01M094331.
H-InvDBHIX0023574.
HGNCHGNC:24013. DNTTIP2.
HPAHPA044502.
MIM611199. gene.
neXtProtNX_Q5QJE6.
PharmGKBPA142671963.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG273245.
HOVERGENHBG106308.
InParanoidQ5QJE6.
OMAEAESHVS.
OrthoDBEOG76T9SJ.
PhylomeDBQ5QJE6.
TreeFamTF105964.

Gene expression databases

ArrayExpressQ5QJE6.
BgeeQ5QJE6.
CleanExHS_DNTTIP2.
GenevestigatorQ5QJE6.

Family and domain databases

InterProIPR014810. Fcf2.
[Graphical view]
PfamPF08698. Fcf2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNTTIP2. human.
GeneWikiDNTTIP2.
GenomeRNAi30836.
NextBio52954.
PROQ5QJE6.
SOURCESearch...

Entry information

Entry nameTDIF2_HUMAN
AccessionPrimary (citable) accession number: Q5QJE6
Secondary accession number(s): Q12987 expand/collapse secondary AC list , Q53H59, Q5TFJ4, Q6TLI0, Q76MJ8, Q86WX9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: July 9, 2014
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM