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Q9BVS4

- RIOK2_HUMAN

UniProt

Q9BVS4 - RIOK2_HUMAN

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Protein
Serine/threonine-protein kinase RIO2
Gene
RIOK2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231ATP By similarity
Active sitei228 – 2281Proton acceptor By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase RIO2 (EC:2.7.11.1)
Alternative name(s):
RIO kinase 2
Gene namesi
Name:RIOK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:18999. RIOK2.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134885533.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 552552Serine/threonine-protein kinase RIO2
PRO_0000213527Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei332 – 3321Phosphoserine4 Publications
Modified residuei335 – 3351Phosphoserine4 Publications
Modified residuei337 – 3371Phosphoserine5 Publications
Modified residuei350 – 3501Phosphoserine1 Publication
Modified residuei362 – 3621Phosphoserine1 Publication
Modified residuei380 – 3801Phosphoserine2 Publications
Modified residuei382 – 3821Phosphoserine2 Publications
Modified residuei385 – 3851Phosphoserine3 Publications
Modified residuei390 – 3901Phosphoserine4 Publications
Modified residuei412 – 4121Phosphoserine1 Publication
Modified residuei417 – 4171Phosphoserine1 Publication
Modified residuei442 – 4421Phosphoserine3 Publications
Modified residuei445 – 4451Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BVS4.
PaxDbiQ9BVS4.
PRIDEiQ9BVS4.

PTM databases

PhosphoSiteiQ9BVS4.

Expressioni

Gene expression databases

ArrayExpressiQ9BVS4.
BgeeiQ9BVS4.
CleanExiHS_RIOK2.
GenevestigatoriQ9BVS4.

Organism-specific databases

HPAiHPA005681.

Interactioni

Protein-protein interaction databases

BioGridi120896. 24 interactions.
IntActiQ9BVS4. 18 interactions.
STRINGi9606.ENSP00000283109.

Structurei

3D structure databases

ProteinModelPortaliQ9BVS4.
SMRiQ9BVS4. Positions 3-314.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini271 – 552282Protein kinase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0478.
HOGENOMiHOG000225685.
HOVERGENiHBG056045.
InParanoidiQ9BVS4.
KOiK07179.
OMAiVAKLRYM.
OrthoDBiEOG754HP9.
PhylomeDBiQ9BVS4.
TreeFamiTF321400.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR018934. RIO-like_kinase.
IPR015285. RIO2_kinase_winged_hlx_N.
IPR018935. RIO_kinase_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01163. RIO1. 1 hit.
PF09202. Rio2_N. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01245. RIO1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BVS4-1) [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

MGKVNVAKLR YMSRDDFRVL TAVEMGMKNH EIVPGSLIAS IASLKHGGCN    50
KVLRELVKHK LIAWERTKTV QGYRLTNAGY DYLALKTLSS RQVVESVGNQ 100
MGVGKESDIY IVANEEGQQF ALKLHRLGRT SFRNLKNKRD YHKHRHNVSW 150
LYLSRLSAMK EFAYMKALYE RKFPVPKPID YNRHAVVMEL INGYPLCQIH 200
HVEDPASVYD EAMELIVKLA NHGLIHGDFN EFNLILDESD HITMIDFPQM 250
VSTSHPNAEW YFDRDVKCIK DFFMKRFSYE SELFPTFKDI RREDTLDVEV 300
SASGYTKEMQ ADDELLHPLG PDDKNIETKE GSEFSFSDGE VAEKAEVYGS 350
ENESERNCLE ESEGCYCRSS GDPEQIKEDS LSEESADARS FEMTEFNQAL 400
EEIKGQVVEN NSVTEFSEEK NRTENYNRQD GQRVQGGVPA GSDEYEDECP 450
HLIALSSLNR EFRPFRDEEN VGAMNQYRTR TLSITSSGSA VSCSTIPPEL 500
VKQKVKRQLT KQQKSAVRRR LQKGEANIFT KQRRENMQNI KSSLEAASFW 550
GE 552
Length:552
Mass (Da):63,283
Last modified:April 3, 2007 - v2
Checksum:i6EB260E72DDB78D7
GO
Isoform 2 (identifier: Q9BVS4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     467-552: DEENVGAMNQ...SLEAASFWGE → YRLLSIAF

Note: No experimental confirmation available.

Show »
Length:474
Mass (Da):54,508
Checksum:i4B396021BE81BE84
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961S → C.1 Publication
Corresponds to variant rs2544773 [ dbSNP | Ensembl ].
VAR_042347
Natural varianti144 – 1441H → R.1 Publication
Corresponds to variant rs35165987 [ dbSNP | Ensembl ].
VAR_042348
Natural varianti144 – 1441H → Y.1 Publication
Corresponds to variant rs17849382 [ dbSNP | Ensembl ].
VAR_031597
Natural varianti155 – 1551R → H.1 Publication
Corresponds to variant rs34916955 [ dbSNP | Ensembl ].
VAR_042349
Natural varianti175 – 1751V → I.1 Publication
Corresponds to variant rs35713904 [ dbSNP | Ensembl ].
VAR_042350
Natural varianti216 – 2161I → T in a renal clear cell carcinoma sample; somatic mutation. 1 Publication
VAR_042351
Natural varianti244 – 2441M → V.1 Publication
Corresponds to variant rs33996030 [ dbSNP | Ensembl ].
VAR_042352
Natural varianti349 – 3491G → R.2 Publications
Corresponds to variant rs160632 [ dbSNP | Ensembl ].
VAR_031598
Natural varianti397 – 3971N → S.1 Publication
Corresponds to variant rs12188395 [ dbSNP | Ensembl ].
VAR_031599
Natural varianti409 – 4091E → D.1 Publication
Corresponds to variant rs35829000 [ dbSNP | Ensembl ].
VAR_042353
Natural varianti507 – 5071R → H.1 Publication
Corresponds to variant rs34555783 [ dbSNP | Ensembl ].
VAR_042354

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei467 – 55286DEENV…SFWGE → YRLLSIAF in isoform 2.
VSP_046388Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK002021 mRNA. Translation: BAA92040.1.
AK225348 mRNA. No translation available.
AC008865 Genomic DNA. No translation available.
AC008883 Genomic DNA. No translation available.
BC000953 mRNA. Translation: AAH00953.1.
CCDSiCCDS4089.1. [Q9BVS4-1]
CCDS54884.1. [Q9BVS4-2]
RefSeqiNP_001153221.1. NM_001159749.1. [Q9BVS4-2]
NP_060813.2. NM_018343.2. [Q9BVS4-1]
UniGeneiHs.27021.

Genome annotation databases

EnsembliENST00000283109; ENSP00000283109; ENSG00000058729. [Q9BVS4-1]
ENST00000508447; ENSP00000420932; ENSG00000058729. [Q9BVS4-2]
GeneIDi55781.
KEGGihsa:55781.
UCSCiuc003kmz.3. human. [Q9BVS4-1]

Polymorphism databases

DMDMi143811448.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK002021 mRNA. Translation: BAA92040.1 .
AK225348 mRNA. No translation available.
AC008865 Genomic DNA. No translation available.
AC008883 Genomic DNA. No translation available.
BC000953 mRNA. Translation: AAH00953.1 .
CCDSi CCDS4089.1. [Q9BVS4-1 ]
CCDS54884.1. [Q9BVS4-2 ]
RefSeqi NP_001153221.1. NM_001159749.1. [Q9BVS4-2 ]
NP_060813.2. NM_018343.2. [Q9BVS4-1 ]
UniGenei Hs.27021.

3D structure databases

ProteinModelPortali Q9BVS4.
SMRi Q9BVS4. Positions 3-314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120896. 24 interactions.
IntActi Q9BVS4. 18 interactions.
STRINGi 9606.ENSP00000283109.

Chemistry

BindingDBi Q9BVS4.
ChEMBLi CHEMBL6000.
GuidetoPHARMACOLOGYi 2187.

PTM databases

PhosphoSitei Q9BVS4.

Polymorphism databases

DMDMi 143811448.

Proteomic databases

MaxQBi Q9BVS4.
PaxDbi Q9BVS4.
PRIDEi Q9BVS4.

Protocols and materials databases

DNASUi 55781.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000283109 ; ENSP00000283109 ; ENSG00000058729 . [Q9BVS4-1 ]
ENST00000508447 ; ENSP00000420932 ; ENSG00000058729 . [Q9BVS4-2 ]
GeneIDi 55781.
KEGGi hsa:55781.
UCSCi uc003kmz.3. human. [Q9BVS4-1 ]

Organism-specific databases

CTDi 55781.
GeneCardsi GC05M096496.
HGNCi HGNC:18999. RIOK2.
HPAi HPA005681.
neXtProti NX_Q9BVS4.
PharmGKBi PA134885533.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0478.
HOGENOMi HOG000225685.
HOVERGENi HBG056045.
InParanoidi Q9BVS4.
KOi K07179.
OMAi VAKLRYM.
OrthoDBi EOG754HP9.
PhylomeDBi Q9BVS4.
TreeFami TF321400.

Miscellaneous databases

GenomeRNAii 55781.
NextBioi 60867.
PROi Q9BVS4.

Gene expression databases

ArrayExpressi Q9BVS4.
Bgeei Q9BVS4.
CleanExi HS_RIOK2.
Genevestigatori Q9BVS4.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR018934. RIO-like_kinase.
IPR015285. RIO2_kinase_winged_hlx_N.
IPR018935. RIO_kinase_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF01163. RIO1. 1 hit.
PF09202. Rio2_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01245. RIO1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "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 1), VARIANT ARG-349.
    Tissue: Placenta.
  2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Hepatoma.
  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. "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), VARIANT TYR-144.
    Tissue: Placenta.
  5. "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-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337; SER-390; SER-417 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350; SER-380; SER-382; SER-385 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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].
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337; SER-362; SER-385; SER-390; SER-442 AND TYR-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-332; SER-335; SER-337; SER-380; SER-382; SER-385 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-332; SER-335; SER-337 AND SER-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-337, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-96; ARG-144; HIS-155; ILE-175; THR-216; VAL-244; ARG-349; SER-397; ASP-409 AND HIS-507.

Entry informationi

Entry nameiRIOK2_HUMAN
AccessioniPrimary (citable) accession number: Q9BVS4
Secondary accession number(s): D6RDI3, Q9NUT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: April 3, 2007
Last modified: September 3, 2014
This is version 119 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 5
    Human chromosome 5: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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