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Q13325

- IFIT5_HUMAN

UniProt

Q13325 - IFIT5_HUMAN

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Protein
Interferon-induced protein with tetratricopeptide repeats 5
Gene
IFIT5, ISG58, RI58
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei33 – 331Interaction with PPP-RNA
Sitei37 – 371Interaction with PPP-RNA
Sitei41 – 411Interaction with PPP-RNA
Sitei150 – 1501Interaction with PPP-RNA
Sitei186 – 1861Interaction with PPP-RNA
Sitei250 – 2501Interaction with PPP-RNA
Sitei288 – 2881Interaction with the 5'-triphosphate group of PPP-RNA

GO - Molecular functioni

  1. RNA binding Source: UniProtKB
  2. poly(A) RNA binding Source: UniProtKB
  3. single-stranded RNA binding Source: UniProtKB
  4. tRNA binding Source: UniProtKB

GO - Biological processi

  1. defense response to virus Source: UniProtKB
  2. innate immune response Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

RNA-binding, tRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon-induced protein with tetratricopeptide repeats 5
Short name:
IFIT-5
Alternative name(s):
Interferon-induced 58 kDa protein
Retinoic acid- and interferon-inducible 58 kDa protein
Short name:
P58
Gene namesi
Name:IFIT5
Synonyms:ISG58, RI58
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:13328. IFIT5.

Subcellular locationi

Cell projectionruffle membrane
Note: Colocalized with DDX58/RIG-I at cell surface ruffles. Localizes to actin-rich protrusions from the apical cell surface.1 Publication

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. apical part of cell Source: UniProtKB
  3. ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi33 – 331E → A: Reduced PPP-RNA-binding. 1 Publication
Mutagenesisi37 – 371T → V: Abolishes PPP-RNA-binding.
Mutagenesisi41 – 411Q → E: Abolishes PPP-RNA-binding. 1 Publication
Mutagenesisi150 – 1501K → M: Abolishes PPP-RNA-binding. 1 Publication
Mutagenesisi156 – 1561Y → F: Reduced PPP-RNA-binding. 1 Publication
Mutagenesisi186 – 1861R → H: Abolishes PPP-RNA-binding. 1 Publication
Mutagenesisi250 – 2501Y → F: Abolishes PPP-RNA-binding. 1 Publication
Mutagenesisi253 – 2531R → M: Abolishes PPP-RNA-binding. 1 Publication
Mutagenesisi254 – 2541Y → F: Abolishes PPP-RNA-binding. 1 Publication
Mutagenesisi260 – 2601R → E: Abolishes PPP-RNA-binding. 1 Publication
Mutagenesisi287 – 2871H → A: Reduced PPP-RNA-binding. 1 Publication
Mutagenesisi288 – 2881Q → E: Abolishes PPP-RNA-binding. 1 Publication
Mutagenesisi291 – 2911L → A: Does not affect RNA-binding. 1 Publication
Mutagenesisi302 – 3021K → A: Reduced RNA-binding. 1 Publication
Mutagenesisi307 – 3071R → A: Reduced RNA-binding. 25 fold reduction in tRNA-binding. 1 Publication
Mutagenesisi309 – 3091K → A: Reduced RNA-binding. 1 Publication
Mutagenesisi337 – 3371F → A: Abolishes PPP-RNA-binding.
Mutagenesisi388 – 3892FH → AA: Reduced RNA-binding.
Mutagenesisi415 – 4151K → A: Reduced RNA-binding. 25 fold reduction in tRNA-binding. 1 Publication
Mutagenesisi422 – 4221K → A: Reduced RNA-binding. 1 Publication
Mutagenesisi426 – 4261K → A: Reduced RNA-binding. 5 fold reduction in tRNA-binding. 1 Publication

Organism-specific databases

PharmGKBiPA134988392.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482Interferon-induced protein with tetratricopeptide repeats 5
PRO_0000106351Add
BLAST

Proteomic databases

MaxQBiQ13325.
PaxDbiQ13325.
PeptideAtlasiQ13325.
PRIDEiQ13325.

PTM databases

PhosphoSiteiQ13325.

Expressioni

Inductioni

By interferons (IFNs).

Gene expression databases

ArrayExpressiQ13325.
BgeeiQ13325.
CleanExiHS_IFIT5.
GenevestigatoriQ13325.

Organism-specific databases

HPAiHPA037957.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi117289. 22 interactions.
IntActiQ13325. 13 interactions.
MINTiMINT-1395756.
STRINGi9606.ENSP00000360860.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1513
Helixi19 – 213
Helixi26 – 283
Helixi31 – 4414
Beta strandi46 – 483
Helixi50 – 6314
Helixi67 – 8418
Helixi86 – 883
Helixi91 – 933
Helixi94 – 10613
Helixi110 – 12617
Beta strandi130 – 1334
Helixi138 – 15013
Helixi153 – 1553
Helixi156 – 16914
Helixi174 – 18916
Beta strandi193 – 1953
Helixi201 – 21010
Helixi215 – 22713
Helixi231 – 24414
Helixi249 – 26113
Helixi265 – 27814
Helixi283 – 30321
Turni304 – 3063
Helixi310 – 33324
Helixi338 – 35013
Helixi354 – 36512
Helixi372 – 38817
Helixi393 – 40614
Beta strandi408 – 4103
Helixi413 – 43018
Helixi435 – 44713
Helixi451 – 46414
Helixi469 – 48012

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZGQX-ray2.20A1-482[»]
4HOQX-ray2.07A1-482[»]
4HORX-ray1.86A1-482[»]
4HOSX-ray2.00A1-482[»]
4HOTX-ray2.50A1-482[»]
4J0UX-ray1.97A1-482[»]
ProteinModelPortaliQ13325.
SMRiQ13325. Positions 1-482.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati51 – 8434TPR 1
Add
BLAST
Repeati94 – 12734TPR 2
Add
BLAST
Repeati138 – 17336TPR 3
Add
BLAST
Repeati181 – 21434TPR 4
Add
BLAST
Repeati249 – 28234TPR 5
Add
BLAST
Repeati338 – 37134TPR 6
Add
BLAST
Repeati376 – 41035TPR 7
Add
BLAST
Repeati435 – 46834TPR 8
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni254 – 2607Interaction with the 5'-triphosphate group of PPP-RNA

Domaini

RNA recognition is mediated by a convoluted intramolecular fold of the TPR repeats (TPR eddy), which scaffolds unique additional helices that form an RNA binding cleft (1 Publication and 1 Publication). Undergoes a conformational change upon RNA-binding: unliganded exists in a more open conformation, facilitating RNA entry (1 Publication).

Sequence similaritiesi

Belongs to the IFIT family.
Contains 8 TPR repeats.

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiNOG311487.
HOGENOMiHOG000001558.
HOVERGENiHBG066330.
InParanoidiQ13325.
OMAiNTAIHHY.
OrthoDBiEOG71K62V.
PhylomeDBiQ13325.
TreeFamiTF342671.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR024125. Interferon_induced_IFIT5.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR10271:SF5. PTHR10271:SF5. 1 hit.
PfamiPF00515. TPR_1. 1 hit.
PF07719. TPR_2. 2 hits.
[Graphical view]
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13325-1 [UniParc]FASTAAdd to Basket

« Hide

MSEIRKDTLK AILLELECHF TWNLLKEDID LFEVEDTIGQ QLEFLTTKSR    50
LALYNLLAYV KHLKGQNKDA LECLEQAEEI IQQEHSDKEE VRSLVTWGNY 100
AWVYYHMDQL EEAQKYTGKI GNVCKKLSSP SNYKLECPET DCEKGWALLK 150
FGGKYYQKAK AAFEKALEVE PDNPEFNIGY AITVYRLDDS DREGSVKSFS 200
LGPLRKAVTL NPDNSYIKVF LALKLQDVHA EAEGEKYIEE ILDQISSQPY 250
VLRYAAKFYR RKNSWNKALE LLKKALEVTP TSSFLHHQMG LCYRAQMIQI 300
KKATHNRPKG KDKLKVDELI SSAIFHFKAA MERDSMFAFA YTDLANMYAE 350
GGQYSNAEDI FRKALRLENI TDDHKHQIHY HYGRFQEFHR KSENTAIHHY 400
LEALKVKDRS PLRTKLTSAL KKLSTKRLCH NALDVQSLSA LGFVYKLEGE 450
KRQAAEYYEK AQKIDPENAE FLTALCELRL SI 482
Length:482
Mass (Da):55,847
Last modified:November 1, 1996 - v1
Checksum:i8045BC100384BE05
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti215 – 2151S → N in CAG33312. 1 Publication
Sequence conflicti449 – 4491G → R in BAG35276. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U34605 mRNA. Translation: AAA84934.1.
AK312358 mRNA. Translation: BAG35276.1.
CR457031 mRNA. Translation: CAG33312.1.
AL353146 Genomic DNA. Translation: CAI12381.1.
CH471066 Genomic DNA. Translation: EAW50135.1.
BC025786 mRNA. Translation: AAH25786.1.
CCDSiCCDS7403.1.
PIRiG02058.
RefSeqiNP_036552.1. NM_012420.2.
UniGeneiHs.252839.

Genome annotation databases

EnsembliENST00000371795; ENSP00000360860; ENSG00000152778.
GeneIDi24138.
KEGGihsa:24138.
UCSCiuc010qnh.2. human.

Polymorphism databases

DMDMi6831571.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U34605 mRNA. Translation: AAA84934.1 .
AK312358 mRNA. Translation: BAG35276.1 .
CR457031 mRNA. Translation: CAG33312.1 .
AL353146 Genomic DNA. Translation: CAI12381.1 .
CH471066 Genomic DNA. Translation: EAW50135.1 .
BC025786 mRNA. Translation: AAH25786.1 .
CCDSi CCDS7403.1.
PIRi G02058.
RefSeqi NP_036552.1. NM_012420.2.
UniGenei Hs.252839.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ZGQ X-ray 2.20 A 1-482 [» ]
4HOQ X-ray 2.07 A 1-482 [» ]
4HOR X-ray 1.86 A 1-482 [» ]
4HOS X-ray 2.00 A 1-482 [» ]
4HOT X-ray 2.50 A 1-482 [» ]
4J0U X-ray 1.97 A 1-482 [» ]
ProteinModelPortali Q13325.
SMRi Q13325. Positions 1-482.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117289. 22 interactions.
IntActi Q13325. 13 interactions.
MINTi MINT-1395756.
STRINGi 9606.ENSP00000360860.

PTM databases

PhosphoSitei Q13325.

Polymorphism databases

DMDMi 6831571.

Proteomic databases

MaxQBi Q13325.
PaxDbi Q13325.
PeptideAtlasi Q13325.
PRIDEi Q13325.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371795 ; ENSP00000360860 ; ENSG00000152778 .
GeneIDi 24138.
KEGGi hsa:24138.
UCSCi uc010qnh.2. human.

Organism-specific databases

CTDi 24138.
GeneCardsi GC10P091164.
HGNCi HGNC:13328. IFIT5.
HPAi HPA037957.
neXtProti NX_Q13325.
PharmGKBi PA134988392.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG311487.
HOGENOMi HOG000001558.
HOVERGENi HBG066330.
InParanoidi Q13325.
OMAi NTAIHHY.
OrthoDBi EOG71K62V.
PhylomeDBi Q13325.
TreeFami TF342671.

Miscellaneous databases

GenomeRNAii 24138.
NextBioi 35467534.
PROi Q13325.

Gene expression databases

ArrayExpressi Q13325.
Bgeei Q13325.
CleanExi HS_IFIT5.
Genevestigatori Q13325.

Family and domain databases

Gene3Di 1.25.40.10. 2 hits.
InterProi IPR024125. Interferon_induced_IFIT5.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view ]
PANTHERi PTHR10271:SF5. PTHR10271:SF5. 1 hit.
Pfami PF00515. TPR_1. 1 hit.
PF07719. TPR_2. 2 hits.
[Graphical view ]
SMARTi SM00028. TPR. 5 hits.
[Graphical view ]
PROSITEi PS50005. TPR. 5 hits.
PS50293. TPR_REGION. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel interferon-inducible gene expressed during myeloid differentiation."
    Niikura T., Hirata R., Weil S.C.
    Blood Cells Mol. Dis. 23:337-349(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Tissue: Amygdala.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [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: Pancreas and Spleen.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: REVIEW.
  9. Cited for: RNA-BINDING.
  10. "tRNA binding, structure, and localization of the human interferon-induced protein IFIT5."
    Katibah G.E., Lee H.J., Huizar J.P., Vogan J.M., Alber T., Collins K.
    Mol. Cell 49:743-750(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF LEU-291; LYS-302; ARG-307; LYS-309; 388-PHE-HIS-389; LYS-415; LYS-422 AND LYS-426.
  11. "Structural basis for viral 5'-PPP-RNA recognition by human IFIT proteins."
    Abbas Y.M., Pichlmair A., Gorna M.W., Superti-Furga G., Nagar B.
    Nature 494:60-64(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PPP-RNA, FUNCTION, RNA-BINDING, MUTAGENESIS OF GLU-33; GLN-41; LYS-150; TYR-156; ARG-186; TYR-250; ARG-253; TYR-254; ARG-260; HIS-287 AND GLN-288.

Entry informationi

Entry nameiIFIT5_HUMAN
AccessioniPrimary (citable) accession number: Q13325
Secondary accession number(s): B2R5X9, Q5T7I9, Q6IAX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 127 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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