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Q9H611

- PIF1_HUMAN

UniProt

Q9H611 - PIF1_HUMAN

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Protein

ATP-dependent DNA helicase PIF1

Gene
PIF1, C15orf20
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Possesses an intrinsic strand annealing activity.7 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

Cofactori

Magnesium.1 Publication

Kineticsi

  1. KM=0.17 mM for ATP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi228 – 2358ATP Reviewed prediction
DNA bindingi577 – 59620 Reviewed predictionAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: HGNC
  2. ATP-dependent 5'-3' DNA/RNA helicase activity Source: BHF-UCL
  3. ATP-dependent 5'-3' DNA helicase activity Source: HGNC
  4. G-quadruplex DNA binding Source: UniProtKB-HAMAP
  5. magnesium ion binding Source: HGNC
  6. single-stranded DNA-dependent ATP-dependent DNA helicase activity Source: HGNC
  7. telomerase inhibitor activity Source: UniProtKB-HAMAP
  8. telomeric DNA binding Source: HGNC

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. DNA duplex unwinding Source: GOC
  3. DNA recombination Source: UniProtKB-HAMAP
  4. DNA repair Source: UniProtKB-HAMAP
  5. mitochondrial genome maintenance Source: UniProtKB-HAMAP
  6. negative regulation of telomerase activity Source: HGNC
  7. negative regulation of telomere maintenance via telomerase Source: UniProtKB-HAMAP
  8. regulation of telomere maintenance Source: HGNC
  9. telomere maintenance Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent DNA helicase PIF1 (EC:3.6.4.12)
Alternative name(s):
DNA repair and recombination helicase PIF1
PIF1/RRM3 DNA helicase-like protein
Gene namesi
Name:PIF1
Synonyms:C15orf20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:26220. PIF1.

Subcellular locationi

Nucleus 4 Publications
Isoform 4 : Mitochondrion 4 Publications

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
  2. nuclear chromosome, telomeric region Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi234 – 2341K → A: Loss of ATPase activity. Lower activity for single-stranded DNA. 1 Publication

Organism-specific databases

PharmGKBiPA162399475.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 641641ATP-dependent DNA helicase PIF1UniRule annotationPRO_0000089980Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271Phosphoserine1 Publication
Modified residuei151 – 1511Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9H611.
PRIDEiQ9H611.

PTM databases

PhosphoSiteiQ9H611.

Expressioni

Tissue specificityi

Weak ubiquitous expression.

Inductioni

Tightly cell cycle regulated and expressed in late S/G2 phase.1 Publication

Gene expression databases

ArrayExpressiQ9H611.
BgeeiQ9H611.
CleanExiHS_PIF1.
GenevestigatoriQ9H611.

Organism-specific databases

HPAiCAB018701.

Interactioni

Subunit structurei

Monomer. Interacts with telomerase.2 Publications

Protein-protein interaction databases

STRINGi9606.ENSP00000268043.

Structurei

3D structure databases

ProteinModelPortaliQ9H611.
SMRiQ9H611. Positions 222-247.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 180180PINTUniRule annotationAdd
BLAST
Regioni167 – 641475Hydrolyzes ATP in the presence of both magnesium and single-stranded DNA; weak activity in the presence of RNA or double-stranded DNA; No unwinding activityUniRule annotationAdd
BLAST

Domaini

The PIF1 N-terminal (PINT) domain enhances the interaction with ssDNA through intrinsic binding activity, it also harbors DNA strand-annealing activity.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0507.
HOGENOMiHOG000132960.
HOVERGENiHBG106706.
KOiK15255.
OMAiAMDSNPE.
OrthoDBiEOG7RZ5PJ.
PhylomeDBiQ9H611.
TreeFamiTF319207.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
HAMAPiMF_03176. PIF1.
InterProiIPR003840. DNA_helicase.
IPR010285. DNA_helicase_pif1_like.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF02689. Herpes_Helicase. 1 hit.
PF05970. PIF1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. Align

Isoform 1 (identifier: Q9H611-1) [UniParc]FASTAAdd to Basket

Also known as: Isoform alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MLSGIEAAAG EYEDSELRCR VAVEELSPGG QPRRRQALRT AELSLGRNER    50
RELMLRLQAP GPAGRPRCFP LRAARLFTRF AEAGRSTLRL PAHDTPGAGA 100
VQLLLSDCPP DRLRRFLRTL RLKLAAAPGP GPASARAQLL GPRPRDFVTI 150
SPVQPEERRL RAATRVPDTT LVKRPVEPQA GAEPSTEAPR WPLPVKRLSL 200
PSTKPQLSEE QAAVLRAVLK GQSIFFTGSA GTGKSYLLKR ILGSLPPTGT 250
VATASTGVAA CHIGGTTLHA FAGIGSGQAP LAQCVALAQR PGVRQGWLNC 300
QRLVIDEISM VEADLFDKLE AVARAVRQQN KPFGGIQLII CGDFLQLPPV 350
TKGSQPPRFC FQSKSWKRCV PVTLELTKVW RQADQTFISL LQAVRLGRCS 400
DEVTRQLQAT ASHKVGRDGI VATRLCTHQD DVALTNERRL QELPGKVHRF 450
EAMDSNPELA STLDAQCPVS QLLQLKLGAQ VMLVKNLSVS RGLVNGARGV 500
VVGFEAEGRG LPQVRFLCGV TEVIHADRWT VQATGGQLLS RQQLPLQLAW 550
AMSIHKSQGM TLDCVEISLG RVFASGQAYV ALSRARSLQG LRVLDFDPMA 600
VRCDPRVLHF YATLRRGRSL SLESPDDDEA ASDQENMDPI L 641
Length:641
Mass (Da):69,799
Last modified:July 10, 2007 - v2
Checksum:iD755470008BA3CA8
GO
Isoform 2 (identifier: Q9H611-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     232-266: TGKSYLLKRILGSLPPTGTVATASTGVAACHIGGT → SGGREEVGGQWWGGIEEQGDLSNFAPVQEQGSHIC
     267-641: Missing.

Show »
Length:266
Mass (Da):28,907
Checksum:i0A291FB7E1339D56
GO
Isoform 3 (identifier: Q9H611-3) [UniParc]FASTAAdd to Basket

Also known as: Isoform beta

The sequence of this isoform differs from the canonical sequence as follows:
     623-641: ESPDDDEAASDQENMDPIL → AAEGRGNEDR...FQGINSVWGH

Show »
Length:707
Mass (Da):77,125
Checksum:iDA015E47D50F8541
GO
Isoform 4 (identifier: Q9H611-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: Missing.

Note: Produced by alternative initiation of isoform 1.

Show »
Length:588
Mass (Da):63,889
Checksum:i706C693424557525
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti640 – 6401I → N.
Corresponds to variant rs17802279 [ dbSNP | Ensembl ].
VAR_033206

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5353Missing in isoform 4. VSP_047457Add
BLAST
Alternative sequencei232 – 26635TGKSY…HIGGT → SGGREEVGGQWWGGIEEQGD LSNFAPVQEQGSHIC in isoform 2. VSP_026715Add
BLAST
Alternative sequencei267 – 641375Missing in isoform 2. VSP_026716Add
BLAST
Alternative sequencei623 – 64119ESPDD…MDPIL → AAEGRGNEDRCSGSSIRALG GDWWGLRLGAASKQRTELRC VSTARPSLAQPRTNTLQSLT KEHKLQNVHPYFKLLFQGIN SVWGH in isoform 3. VSP_026717Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ437529 mRNA. Translation: ABD92708.1.
EU084033 mRNA. Translation: ABW71293.1.
AY498716 mRNA. Translation: AAS77398.1.
AB185926 mRNA. Translation: BAE47454.1.
AB185927 mRNA. Translation: BAE47455.1.
AK026345 mRNA. Translation: BAB15456.1.
BC137503 mRNA. Translation: AAI37504.1.
BC137504 mRNA. Translation: AAI37505.1.
CCDSiCCDS10195.2. [Q9H611-1]
CCDS66797.1. [Q9H611-3]
RefSeqiNP_001273425.1. NM_001286496.1. [Q9H611-1]
NP_001273426.1. NM_001286497.1. [Q9H611-3]
NP_001273428.1. NM_001286499.1. [Q9H611-4]
NP_079325.2. NM_025049.3. [Q9H611-1]
UniGeneiHs.112160.

Genome annotation databases

EnsembliENST00000268043; ENSP00000268043; ENSG00000140451. [Q9H611-1]
ENST00000333425; ENSP00000328174; ENSG00000140451. [Q9H611-3]
ENST00000559239; ENSP00000452792; ENSG00000140451. [Q9H611-1]
GeneIDi80119.
KEGGihsa:80119.
UCSCiuc002ans.2. human. [Q9H611-1]
uc002anu.3. human. [Q9H611-2]

Polymorphism databases

DMDMi152031656.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ437529 mRNA. Translation: ABD92708.1 .
EU084033 mRNA. Translation: ABW71293.1 .
AY498716 mRNA. Translation: AAS77398.1 .
AB185926 mRNA. Translation: BAE47454.1 .
AB185927 mRNA. Translation: BAE47455.1 .
AK026345 mRNA. Translation: BAB15456.1 .
BC137503 mRNA. Translation: AAI37504.1 .
BC137504 mRNA. Translation: AAI37505.1 .
CCDSi CCDS10195.2. [Q9H611-1 ]
CCDS66797.1. [Q9H611-3 ]
RefSeqi NP_001273425.1. NM_001286496.1. [Q9H611-1 ]
NP_001273426.1. NM_001286497.1. [Q9H611-3 ]
NP_001273428.1. NM_001286499.1. [Q9H611-4 ]
NP_079325.2. NM_025049.3. [Q9H611-1 ]
UniGenei Hs.112160.

3D structure databases

ProteinModelPortali Q9H611.
SMRi Q9H611. Positions 222-247.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000268043.

PTM databases

PhosphoSitei Q9H611.

Polymorphism databases

DMDMi 152031656.

Proteomic databases

PaxDbi Q9H611.
PRIDEi Q9H611.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000268043 ; ENSP00000268043 ; ENSG00000140451 . [Q9H611-1 ]
ENST00000333425 ; ENSP00000328174 ; ENSG00000140451 . [Q9H611-3 ]
ENST00000559239 ; ENSP00000452792 ; ENSG00000140451 . [Q9H611-1 ]
GeneIDi 80119.
KEGGi hsa:80119.
UCSCi uc002ans.2. human. [Q9H611-1 ]
uc002anu.3. human. [Q9H611-2 ]

Organism-specific databases

CTDi 80119.
GeneCardsi GC15M065107.
H-InvDB HIX0017918.
HGNCi HGNC:26220. PIF1.
HPAi CAB018701.
MIMi 610953. gene.
neXtProti NX_Q9H611.
PharmGKBi PA162399475.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0507.
HOGENOMi HOG000132960.
HOVERGENi HBG106706.
KOi K15255.
OMAi AMDSNPE.
OrthoDBi EOG7RZ5PJ.
PhylomeDBi Q9H611.
TreeFami TF319207.

Miscellaneous databases

GenomeRNAii 80119.
NextBioi 70350.
PROi Q9H611.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9H611.
Bgeei Q9H611.
CleanExi HS_PIF1.
Genevestigatori Q9H611.

Family and domain databases

Gene3Di 3.40.50.300. 3 hits.
HAMAPi MF_03176. PIF1.
InterProi IPR003840. DNA_helicase.
IPR010285. DNA_helicase_pif1_like.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF02689. Herpes_Helicase. 1 hit.
PF05970. PIF1. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 3 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human Pif1 helicase, a potential Escherichia coli RecD homologue, inhibits telomerase activity."
    Zhang D.-H., Zhou B., Huang Y., Xu L.-X., Zhou J.-Q.
    Nucleic Acids Res. 34:1393-1404(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, REGION, MUTAGENESIS OF LYS-234, SUBCELLULAR LOCATION, COFACTOR.
  2. "Biochemical analysis of human PIF1 helicase and functions of its N-terminal domain."
    Gu Y., Masuda Y., Kamiya K.
    Nucleic Acids Res. 36:6295-6308(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, PINT DOMAIN.
  3. Snow B.E., Erdmann N., Harrington L.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Human PIF1 DNA helicase."
    Futami K., Furuichi Y., Shimamoto A.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
  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.
    , 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] (ISOFORM 2).
    Tissue: Small intestine.
  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: Brain and Testis.
  7. "Human PIF helicase is cell cycle regulated and associates with telomerase."
    Mateyak M.K., Zakian V.A.
    Cell Cycle 5:2796-2804(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TELOMERASE, INDUCTION.
  8. "Mitochondrial and nuclear localization of human Pif1 helicase."
    Futami K., Shimamoto A., Furuichi Y.
    Biol. Pharm. Bull. 30:1685-1692(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Human Pif1 helicase unwinds synthetic DNA structures resembling stalled DNA replication forks."
    George T., Wen Q., Griffiths R., Ganesh A., Meuth M., Sanders C.M.
    Nucleic Acids Res. 37:6491-6502(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  11. "Human Pif1 helicase is a G-quadruplex DNA-binding protein with G-quadruplex DNA-unwinding activity."
    Sanders C.M.
    Biochem. J. 430:119-128(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN G4-UNWINDING.
  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-27 AND SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Pif1 family helicases suppress genome instability at G-quadruplex motifs."
    Paeschke K., Bochman M.L., Garcia P.D., Cejka P., Friedman K.L., Kowalczykowski S.C., Zakian V.A.
    Nature 497:458-462(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN G4-UNWINDING AND TELOMERE LENGTH REGULATION.
  15. Cited for: ALTERNATIVE INITIATION (ISOFORM 4), SUBCELLULAR LOCATION (ISOFORM 4).

Entry informationi

Entry nameiPIF1_HUMAN
AccessioniPrimary (citable) accession number: Q9H611
Secondary accession number(s): B2RPL7
, Q1W5B6, Q330H5, Q33E24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 10, 2007
Last modified: July 9, 2014
This is version 88 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 15
    Human chromosome 15: 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

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