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Q9NW64

- RBM22_HUMAN

UniProt

Q9NW64 - RBM22_HUMAN

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Protein

Pre-mRNA-splicing factor RBM22

Gene

RBM22

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

Functioni

Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Involved in both translocations of the nuclear SLU7 to the cytoplasm and the cytosolic calcium-binding protein PDCD6 to the nucleus upon cellular stress responses.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri159 – 18628C3H1-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium-dependent protein binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. nucleocytoplasmic transporter activity Source: UniProtKB
  4. nucleotide binding Source: InterPro
  5. poly(A) RNA binding Source: UniProtKB
  6. pre-mRNA binding Source: UniProtKB
  7. snRNA binding Source: UniProtKB

GO - Biological processi

  1. cellular response to drug Source: UniProtKB
  2. mRNA cis splicing, via spliceosome Source: UniProtKB
  3. mRNA splicing, via spliceosome Source: UniProtKB
  4. positive regulation of intracellular protein transport Source: UniProtKB
  5. positive regulation of RNA splicing Source: UniProtKB
  6. protein import into nucleus, translocation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, Transport

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-splicing factor RBM22
Alternative name(s):
RNA-binding motif protein 22
Zinc finger CCCH domain-containing protein 16
Gene namesi
Name:RBM22
Synonyms:ZC3H16
ORF Names:199G4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:25503. RBM22.

Subcellular locationi

Nucleus. Cytoplasm
Note: Mainly located in the nucleus. Translocated from the nucleus to the cytoplasm after heat shock cell treatment. May be shuttling between the nucleus and the cytosol.

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi170 – 1701K → R: Accumulates in speckle-like structures. 1 Publication
Mutagenesisi324 – 3241K → R: Accumulates in speckle-like structures. 1 Publication

Organism-specific databases

PharmGKBiPA134982384.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 420419Pre-mRNA-splicing factor RBM22PRO_0000250546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei212 – 2121N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NW64.
PaxDbiQ9NW64.
PRIDEiQ9NW64.

PTM databases

PhosphoSiteiQ9NW64.

Expressioni

Gene expression databases

BgeeiQ9NW64.
CleanExiHS_RBM22.
ExpressionAtlasiQ9NW64. baseline and differential.
GenevestigatoriQ9NW64.

Organism-specific databases

HPAiHPA001634.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Interacts with PDCD6; the interaction induces translocation of PDCD6 in the cytoplasm.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PRNPP041561EBI-2602260,EBI-977302

Protein-protein interaction databases

BioGridi120821. 23 interactions.
IntActiQ9NW64. 11 interactions.
MINTiMINT-2819539.
STRINGi9606.ENSP00000199814.

Structurei

Secondary structure

1
420
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi234 – 2374
Turni240 – 2423
Helixi245 – 2539
Beta strandi258 – 2647
Helixi265 – 2673
Beta strandi269 – 2768
Helixi277 – 2859
Turni286 – 2905
Beta strandi300 – 3023

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YTCNMR-A227-304[»]
ProteinModelPortaliQ9NW64.
SMRiQ9NW64. Positions 227-304.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NW64.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini232 – 30574RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi327 – 40781Pro-richAdd
BLAST

Domaini

The C-terminus RRM domain and the zinc finger motif are necessary for RNA-binding.By similarity

Sequence similaritiesi

Belongs to the SLT11 family.Curated
Contains 1 C3H1-type zinc finger.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri159 – 18628C3H1-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG277760.
GeneTreeiENSGT00390000002792.
HOGENOMiHOG000171086.
HOVERGENiHBG083475.
InParanoidiQ9NW64.
KOiK12872.
OMAiHSRYGNG.
OrthoDBiEOG7K0ZCH.
PhylomeDBiQ9NW64.
TreeFamiTF314284.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00356. ZnF_C3H1. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NW64-1) [UniParc]FASTAAdd to Basket

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

        10         20         30         40         50
MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR
60 70 80 90 100
PFTVFRWCPG VRMRFKKTEV CQTCSKLKNV CQTCLLDLEY GLPIQVRDAG
110 120 130 140 150
LSFKDDMPKS DVNKEYYTQN MEREISNSDG TRPVGMLGKA TSTSDMLLKL
160 170 180 190 200
ARTTPYYKRN RPHICSFWVK GECKRGEECP YRHEKPTDPD DPLADQNIKD
210 220 230 240 250
RYYGINDPVA DKLLKRASTM PRLDPPEDKT ITTLYVGGLG DTITETDLRN
260 270 280 290 300
HFYQFGEIRT ITVVQRQQCA FIQFATRQAA EVAAEKSFNK LIVNGRRLNV
310 320 330 340 350
KWGRSQAARG KEKEKDGTTD SGIKLEPVPG LPGALPPPPA AEEEASANYF
360 370 380 390 400
NLPPSGPPAV VNIALPPPPG IAPPPPPGFG PHMFHPMGPP PPFMRAPGPI
410 420
HYPSQDPQRM GAHAGKHSSP
Length:420
Mass (Da):46,896
Last modified:October 1, 2000 - v1
Checksum:iA82549D8CC88C7D0
GO
Isoform 2 (identifier: Q9NW64-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-91: Missing.

Note: No experimental confirmation available.

Show »
Length:371
Mass (Da):41,152
Checksum:iCD43CE9BAD03CE15
GO

Sequence cautioni

The sequence AAC99998.1 differs from that shown. Reason: Chimera.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei43 – 9149Missing in isoform 2. 1 PublicationVSP_036832Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL136933 mRNA. Translation: CAB66867.1.
AK001152 mRNA. Translation: BAA91521.1.
AK297019 mRNA. Translation: BAG59551.1.
AC008453 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61711.1.
BC003402 mRNA. Translation: AAH03402.1.
U39402 mRNA. Translation: AAC99998.1. Sequence problems.
CCDSiCCDS34278.1. [Q9NW64-1]
RefSeqiNP_060517.1. NM_018047.2. [Q9NW64-1]
UniGeneiHs.713564.

Genome annotation databases

EnsembliENST00000199814; ENSP00000199814; ENSG00000086589. [Q9NW64-1]
ENST00000447771; ENSP00000412118; ENSG00000086589. [Q9NW64-2]
GeneIDi55696.
KEGGihsa:55696.
UCSCiuc003lst.3. human. [Q9NW64-1]

Polymorphism databases

DMDMi74762758.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL136933 mRNA. Translation: CAB66867.1 .
AK001152 mRNA. Translation: BAA91521.1 .
AK297019 mRNA. Translation: BAG59551.1 .
AC008453 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61711.1 .
BC003402 mRNA. Translation: AAH03402.1 .
U39402 mRNA. Translation: AAC99998.1 . Sequence problems.
CCDSi CCDS34278.1. [Q9NW64-1 ]
RefSeqi NP_060517.1. NM_018047.2. [Q9NW64-1 ]
UniGenei Hs.713564.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YTC NMR - A 227-304 [» ]
ProteinModelPortali Q9NW64.
SMRi Q9NW64. Positions 227-304.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120821. 23 interactions.
IntActi Q9NW64. 11 interactions.
MINTi MINT-2819539.
STRINGi 9606.ENSP00000199814.

PTM databases

PhosphoSitei Q9NW64.

Polymorphism databases

DMDMi 74762758.

Proteomic databases

MaxQBi Q9NW64.
PaxDbi Q9NW64.
PRIDEi Q9NW64.

Protocols and materials databases

DNASUi 55696.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000199814 ; ENSP00000199814 ; ENSG00000086589 . [Q9NW64-1 ]
ENST00000447771 ; ENSP00000412118 ; ENSG00000086589 . [Q9NW64-2 ]
GeneIDi 55696.
KEGGi hsa:55696.
UCSCi uc003lst.3. human. [Q9NW64-1 ]

Organism-specific databases

CTDi 55696.
GeneCardsi GC05M150050.
HGNCi HGNC:25503. RBM22.
HPAi HPA001634.
MIMi 612430. gene.
neXtProti NX_Q9NW64.
PharmGKBi PA134982384.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG277760.
GeneTreei ENSGT00390000002792.
HOGENOMi HOG000171086.
HOVERGENi HBG083475.
InParanoidi Q9NW64.
KOi K12872.
OMAi HSRYGNG.
OrthoDBi EOG7K0ZCH.
PhylomeDBi Q9NW64.
TreeFami TF314284.

Miscellaneous databases

EvolutionaryTracei Q9NW64.
GeneWikii RBM22.
GenomeRNAii 55696.
NextBioi 60521.
PROi Q9NW64.
SOURCEi Search...

Gene expression databases

Bgeei Q9NW64.
CleanExi HS_RBM22.
ExpressionAtlasi Q9NW64. baseline and differential.
Genevestigatori Q9NW64.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR000571. Znf_CCCH.
[Graphical view ]
Pfami PF00076. RRM_1. 1 hit.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
SM00356. ZnF_C3H1. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Uterus.
  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] (ISOFORMS 1 AND 2).
    Tissue: Mammary gland and Umbilical cord blood.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Placenta.
  6. "Transcriptional map of the Treacher Collins candidate gene region."
    Loftus S.K., Dixon J., Koprivnikar K., Dixon M.J., Wasmuth J.J.
    Genome Res. 6:26-34(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 126-420.
    Tissue: Brain.
  7. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  8. "Nuclear translocation of the calcium-binding protein ALG-2 induced by the RNA-binding protein RBM22."
    Montaville P., Dai Y., Cheung C.Y., Giller K., Becker S., Michalak M., Webb S.E., Miller A.L., Krebs J.
    Biochim. Biophys. Acta 1763:1335-1343(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PDCD6.
  9. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "The influence of calcium signaling on the regulation of alternative splicing."
    Krebs J.
    Biochim. Biophys. Acta 1793:979-984(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-170 AND LYS-324.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Stress induced subcellular distribution of ALG-2, RBM22 and hSlu7."
    Janowicz A., Michalak M., Krebs J.
    Biochim. Biophys. Acta 1813:1045-1049(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. "Cwc2 and its human homologue RBM22 promote an active conformation of the spliceosome catalytic centre."
    Rasche N., Dybkov O., Schmitzova J., Akyildiz B., Fabrizio P., Luhrmann R.
    EMBO J. 31:1591-1604(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.
  15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Solution structure of RNA binding domain in pre-mRNA-splicing factor RBM22."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 227-304.

Entry informationi

Entry nameiRBM22_HUMAN
AccessioniPrimary (citable) accession number: Q9NW64
Secondary accession number(s): A6NDM5, B4DLI9, O95607
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 125 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3