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O60231

- DHX16_HUMAN

UniProt

O60231 - DHX16_HUMAN

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Protein

Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16

Gene
DHX16, DBP2, DDX16, KIAA0577
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Probable ATP-binding RNA helicase involved in pre-mRNA splicing.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi422 – 4298ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent helicase activity Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: IntAct
  5. RNA helicase activity Source: ProtInc

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
  2. RNA splicing Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16 (EC:3.6.4.13)
Alternative name(s):
ATP-dependent RNA helicase #3
DEAH-box protein 16
Gene namesi
Name:DHX16
Synonyms:DBP2, DDX16, KIAA0577
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:2739. DHX16.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27205.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10411041Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16PRO_0000055151Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei103 – 1031Phosphoserine7 Publications
Modified residuei106 – 1061Phosphoserine2 Publications
Modified residuei107 – 1071Phosphoserine3 Publications
Modified residuei160 – 1601Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO60231.
PaxDbiO60231.
PRIDEiO60231.

PTM databases

PhosphoSiteiO60231.

Expressioni

Gene expression databases

ArrayExpressiO60231.
BgeeiO60231.
CleanExiHS_DHX16.
GenevestigatoriO60231.

Organism-specific databases

HPAiHPA051455.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DHX38Q926202EBI-311446,EBI-1043041
GPKOWQ929172EBI-311446,EBI-746309
SF3B2Q134352EBI-311446,EBI-749111
XAB2Q9HCS72EBI-311446,EBI-295232

Protein-protein interaction databases

BioGridi114027. 32 interactions.
IntActiO60231. 11 interactions.
MINTiMINT-5003862.
STRINGi9606.ENSP00000390938.

Structurei

3D structure databases

ProteinModelPortaliO60231.
SMRiO60231. Positions 392-1033.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini409 – 573165Helicase ATP-bindingAdd
BLAST
Domaini598 – 771174Helicase C-terminalAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi520 – 5234DEAH box

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1643.
HOGENOMiHOG000175261.
HOVERGENiHBG039428.
InParanoidiO60231.
KOiK12813.
OMAiIEIESKW.
PhylomeDBiO60231.
TreeFamiTF313473.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O60231-1 [UniParc]FASTAAdd to Basket

« Hide

MATPAGLERW VQDELHSVLG LSERHVAQFL IGTAQRCTSA EEFVQRLRDT     50
DTLDLSGPAR DFALRLWNKV PRKAVVEKPA RAAEREARAL LEKNRSYRLL 100
EDSEESSEET VSRAGSSLQK KRKKRKHLRK KREEEEEEEA SEKGKKKTGG 150
SKQQTEKPES EDEWERTERE RLQDLEERDA FAERVRQRDK DRTRNVLERS 200
DKKAYEEAQK RLKMAEEDRK AMVPELRKKS RREYLAKRER EKLEDLEAEL 250
ADEEFLFGDV ELSRHERQEL KYKRRVRDLA REYRAAGEQE KLEATNRYHM 300
PKETRGQPAR AVDLVEEESG APGEEQRRWE EARLGAASLK FGARDAASQE 350
PKYQLVLEEE ETIEFVRATQ LQGDEEPSAP PTSTQAQQKE SIQAVRRSLP 400
VFPFREELLA AIANHQVLII EGETGSGKTT QIPQYLFEEG YTNKGMKIAC 450
TQPRRVAAMS VAARVAREMG VKLGNEVGYS IRFEDCTSER TVLRYMTDGM 500
LLREFLSEPD LASYSVVMVD EAHERTLHTD ILFGLIKDVA RFRPELKVLV 550
ASATMDTARF STFFDDAPVF RIPGRRFPVD IFYTKAPEAD YLEACVVSVL 600
QIHVTQPPGD ILVFLTGQEE IEAACEMLQD RCRRLGSKIR ELLVLPIYAN 650
LPSDMQARIF QPTPPGARKV VVATNIAETS LTIEGIIYVL DPGFCKQKSY 700
NPRTGMESLT VTPCSKASAN QRAGRAGRVA AGKCFRLYTA WAYQHELEET 750
TVPEIQRTSL GNVVLLLKSL GIHDLMHFDF LDPPPYETLL LALEQLYALG 800
ALNHLGELTT SGRKMAELPV DPMLSKMILA SEKYSCSEEI LTVAAMLSVN 850
NSIFYRPKDK VVHADNARVN FFLPGGDHLV LLNVYTQWAE SGYSSQWCYE 900
NFVQFRSMRR ARDVREQLEG LLERVEVGLS SCQGDYIRVR KAITAGYFYH 950
TARLTRSGYR TVKQQQTVFI HPNSSLFEQQ PRWLLYHELV LTTKEFMRQV 1000
LEIESSWLLE VAPHYYKAKE LEDPHAKKMP KKIGKTREEL G 1041
Length:1,041
Mass (Da):119,264
Last modified:November 28, 2002 - v2
Checksum:i5CAC4DBEF21A4E6D
GO

Sequence cautioni

The sequence BAA25503.2 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti352 – 3521K → E.
Corresponds to variant rs17189239 [ dbSNP | Ensembl ].
VAR_057236
Natural varianti502 – 5021L → F.
Corresponds to variant rs17189232 [ dbSNP | Ensembl ].
VAR_057237
Natural varianti566 – 5661D → G.1 Publication
Corresponds to variant rs9262138 [ dbSNP | Ensembl ].
VAR_057238

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti223 – 2231V → I in BAA25908. 1 Publication
Sequence conflicti631 – 6311R → P in BAA25908. 1 Publication
Sequence conflicti681 – 6811L → P in BAA25908. 1 Publication
Sequence conflicti792 – 7921A → T in BAA25908. 1 Publication
Sequence conflicti899 – 8991Y → C in BAA25908. 1 Publication
Sequence conflicti1032 – 10321K → KK in AAH08825. 1 Publication
Sequence conflicti1032 – 10321K → KK in AAH09392. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB001601 mRNA. Translation: BAA25908.1.
BA000025 Genomic DNA. Translation: BAB63323.1.
AB011149 mRNA. Translation: BAA25503.2. Different initiation.
AL845353 Genomic DNA. Translation: CAI41883.1.
BC008825 mRNA. Translation: AAH08825.1.
BC009392 mRNA. Translation: AAH09392.1.
CCDSiCCDS4685.1.
RefSeqiNP_001157711.1. NM_001164239.1.
NP_003578.2. NM_003587.4.
UniGeneiHs.485060.

Genome annotation databases

EnsembliENST00000376442; ENSP00000365625; ENSG00000204560.
ENST00000383577; ENSP00000373071; ENSG00000206486.
ENST00000417308; ENSP00000390938; ENSG00000233561.
ENST00000421095; ENSP00000396193; ENSG00000226171.
ENST00000424672; ENSP00000389862; ENSG00000233418.
ENST00000451456; ENSP00000408956; ENSG00000233049.
ENST00000458094; ENSP00000393958; ENSG00000231377.
GeneIDi8449.
KEGGihsa:8449.
UCSCiuc003nqz.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB001601 mRNA. Translation: BAA25908.1 .
BA000025 Genomic DNA. Translation: BAB63323.1 .
AB011149 mRNA. Translation: BAA25503.2 . Different initiation.
AL845353 Genomic DNA. Translation: CAI41883.1 .
BC008825 mRNA. Translation: AAH08825.1 .
BC009392 mRNA. Translation: AAH09392.1 .
CCDSi CCDS4685.1.
RefSeqi NP_001157711.1. NM_001164239.1.
NP_003578.2. NM_003587.4.
UniGenei Hs.485060.

3D structure databases

ProteinModelPortali O60231.
SMRi O60231. Positions 392-1033.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114027. 32 interactions.
IntActi O60231. 11 interactions.
MINTi MINT-5003862.
STRINGi 9606.ENSP00000390938.

PTM databases

PhosphoSitei O60231.

Proteomic databases

MaxQBi O60231.
PaxDbi O60231.
PRIDEi O60231.

Protocols and materials databases

DNASUi 8449.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376442 ; ENSP00000365625 ; ENSG00000204560 .
ENST00000383577 ; ENSP00000373071 ; ENSG00000206486 .
ENST00000417308 ; ENSP00000390938 ; ENSG00000233561 .
ENST00000421095 ; ENSP00000396193 ; ENSG00000226171 .
ENST00000424672 ; ENSP00000389862 ; ENSG00000233418 .
ENST00000451456 ; ENSP00000408956 ; ENSG00000233049 .
ENST00000458094 ; ENSP00000393958 ; ENSG00000231377 .
GeneIDi 8449.
KEGGi hsa:8449.
UCSCi uc003nqz.3. human.

Organism-specific databases

CTDi 8449.
GeneCardsi GC06M030620.
GC06Mj30610.
GC06Mk30611.
GC06Ml30665.
GC06Mm30699.
GC06Mn30610.
GC06Mo30612.
HGNCi HGNC:2739. DHX16.
HPAi HPA051455.
MIMi 603405. gene.
neXtProti NX_O60231.
PharmGKBi PA27205.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1643.
HOGENOMi HOG000175261.
HOVERGENi HBG039428.
InParanoidi O60231.
KOi K12813.
OMAi IEIESKW.
PhylomeDBi O60231.
TreeFami TF313473.

Miscellaneous databases

GeneWikii DHX16.
GenomeRNAii 8449.
NextBioi 31614.
PROi O60231.
SOURCEi Search...

Gene expression databases

ArrayExpressi O60231.
Bgeei O60231.
CleanExi HS_DHX16.
Genevestigatori O60231.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a human DEAH-box RNA helicase, a functional homolog of fission yeast Cdc28/Prp8."
    Imamura O., Saiki K., Tani T., Ohshima Y., Sugawara M., Furuichi Y.
    Nucleic Acids Res. 26:2063-2068(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
    Shiina S., Tamiya G., Oka A., Inoko H.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-566.
  5. "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: Brain.
  6. "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-103 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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 SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-106 AND SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "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].
  11. "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-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-103; SER-106; SER-107 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-103; SER-107 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDHX16_HUMAN
AccessioniPrimary (citable) accession number: O60231
Secondary accession number(s): O60322
, Q5JP45, Q969X7, Q96QC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 28, 2002
Last modified: September 3, 2014
This is version 154 of the entry and version 2 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 6
    Human chromosome 6: 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

External Data

Dasty 3

Similar proteinsi