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Q9NRH2

- SNRK_HUMAN

UniProt

Q9NRH2 - SNRK_HUMAN

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Protein
SNF-related serine/threonine-protein kinase
Gene
SNRK, KIAA0096, SNFRK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May play a role in hematopoietic cell proliferation or differentiation. Potential mediator of neuronal apoptosis.By similarity3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Cofactori

Magnesium.2 Publications

Enzyme regulationi

Activated by phosphorylation on Thr-173.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451ATP By similarityBy similarity
Active sitei139 – 1391Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 309ATP By similarityBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. myeloid cell differentiation Source: UniProtKB
  2. protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9NRH2.

Names & Taxonomyi

Protein namesi
Recommended name:
SNF-related serine/threonine-protein kinase (EC:2.7.11.1)
Alternative name(s):
SNF1-related kinase
Gene namesi
Name:SNRK
Synonyms:KIAA0096, SNFRK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:30598. SNRK.

Subcellular locationi

Nucleus By similarity By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi173 – 1731T → A or E: Prevents phosphorylation and activation by STK11/LKB1 complex. 1 Publication

Organism-specific databases

PharmGKBiPA142670894.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 765765SNF-related serine/threonine-protein kinase
PRO_0000225605Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei173 – 1731Phosphothreonine; by LKB11 Publication
Modified residuei390 – 3901Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylated. Phosphorylation on Thr-173 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NRH2.
PaxDbiQ9NRH2.
PRIDEiQ9NRH2.

PTM databases

PhosphoSiteiQ9NRH2.

Expressioni

Tissue specificityi

Expressed in hematopoietic progenitor cells and leukemic cell lines. Weakly expressed in the testis.3 Publications

Gene expression databases

ArrayExpressiQ9NRH2.
BgeeiQ9NRH2.
CleanExiHS_SNRK.
GenevestigatoriQ9NRH2.

Organism-specific databases

HPAiHPA042163.

Interactioni

Protein-protein interaction databases

BioGridi120211. 4 interactions.
IntActiQ9NRH2. 1 interaction.
MINTiMINT-1338450.
STRINGi9606.ENSP00000296088.

Structurei

3D structure databases

ProteinModelPortaliQ9NRH2.
SMRiQ9NRH2. Positions 14-335.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 269254Protein kinase
Add
BLAST
Domaini291 – 33444UBA
Add
BLAST

Sequence similaritiesi

Contains 1 UBA domain.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000059616.
HOVERGENiHBG093970.
InParanoidiQ9NRH2.
KOiK08802.
OMAiTTSGRKC.
OrthoDBiEOG7CZK55.
PhylomeDBiQ9NRH2.
TreeFamiTF351991.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 13 Publications (identifier: Q9NRH2-1) [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

MAGFKRGYDG KIAGLYDLDK TLGRGHFAVV KLARHVFTGE KVAVKVIDKT    50
KLDTLATGHL FQEVRCMKLV QHPNIVRLYE VIDTQTKLYL ILELGDGGDM 100
FDYIMKHEEG LNEDLAKKYF AQIVHAISYC HKLHVVHRDL KPENVVFFEK 150
QGLVKLTDFG FSNKFQPGKK LTTSCGSLAY SAPEILLGDE YDAPAVDIWS 200
LGVILFMLVC GQPPFQEAND SETLTMIMDC KYTVPSHVSK ECKDLITRML 250
QRDPKRRASL EEIENHPWLQ GVDPSPATKY NIPLVSYKNL SEEEHNSIIQ 300
RMVLGDIADR DAIVEALETN RYNHITATYF LLAERILREK QEKEIQTRSA 350
SPSNIKAQFR QSWPTKIDVP QDLEDDLTAT PLSHATVPQS PARAADSVLN 400
GHRSKGLCDS AKKDDLPELA GPALSTVPPA SLKPTASGRK CLFRVEEDEE 450
EDEEDKKPMS LSTQVVLRRK PSVTNRLTSR KSAPVLNQIF EEGESDDEFD 500
MDENLPPKLS RLKMNIASPG TVHKRYHRRK SQGRGSSCSS SETSDDDSES 550
RRRLDKDSGF TYSWHRRDSS EGPPGSEGDG GGQSKPSNAS GGVDKASPSE 600
NNAGGGSPSS GSGGNPTNTS GTTRRCAGPS NSMQLASRSA GELVESLKLM 650
SLCLGSQLHG STKYIIDPQN GLSFSSVKVQ EKSTWKMCIS STGNAGQVPA 700
VGGIKFFSDH MADTTTELER IKSKNLKNNV LQLPLCEKTI SVNIQRNPKE 750
GLLCASSPAS CCHVI 765
Length:765
Mass (Da):84,276
Last modified:March 7, 2006 - v2
Checksum:i06EF88CF7F8A393D
GO
Isoform 21 Publication (identifier: Q9NRH2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     244-244: D → E
     245-765: Missing.

Note: No experimental confirmation available.

Show »
Length:244
Mass (Da):27,481
Checksum:iC800B93190F76B4E
GO

Sequence cautioni

The sequence BAA07744.2 differs from that shown. Reason: Erroneous initiation.
The sequence CAH18415.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti260 – 2601L → S.1 Publication
Corresponds to variant rs35624204 [ dbSNP | Ensembl ].
VAR_041096
Natural varianti391 – 3911P → S.1 Publication
Corresponds to variant rs56104180 [ dbSNP | Ensembl ].
VAR_041097
Natural varianti611 – 6111G → S in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
VAR_041098
Natural varianti748 – 7481P → L in an ovarian serous carcinoma sample; somatic mutation. 1 Publication
VAR_041099
Natural varianti765 – 7651I → M in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication
VAR_041100

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei244 – 2441D → E in isoform 2. 1 Publication
VSP_051959
Alternative sequencei245 – 765521Missing in isoform 2. 1 Publication
VSP_051960Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971G → E in AAF86944. 1 Publication
Sequence conflicti116 – 1161A → P in AAF86944. 1 Publication
Sequence conflicti124 – 1241V → A in CAH18415. 1 Publication
Sequence conflicti181 – 1811S → P in CAH18415. 1 Publication
Sequence conflicti196 – 1961V → A in CAH18415. 1 Publication
Sequence conflicti211 – 2111G → E in BAA91023. 1 Publication
Sequence conflicti219 – 2191N → D in CAH18415. 1 Publication
Sequence conflicti259 – 2591S → Y in AAH71567. 1 Publication
Sequence conflicti445 – 4451V → A in CAH18415. 1 Publication
Sequence conflicti482 – 4821S → G in CAH18415. 1 Publication
Sequence conflicti486 – 4861L → V in AAH71567. 1 Publication
Sequence conflicti636 – 6361A → V in CAH18415. 1 Publication
Sequence conflicti722 – 7221K → R in AAH71567. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D43636 mRNA. Translation: BAA07744.2. Different initiation.
AF226044 mRNA. Translation: AAF86944.1.
AK000231 mRNA. Translation: BAA91023.1.
AK314376 mRNA. Translation: BAG37003.1.
CR749621 mRNA. Translation: CAH18415.1. Different initiation.
CH471055 Genomic DNA. Translation: EAW64693.1.
BC071567 mRNA. Translation: AAH71567.1.
CCDSiCCDS43075.1. [Q9NRH2-1]
RefSeqiNP_001094064.1. NM_001100594.1. [Q9NRH2-1]
NP_060189.3. NM_017719.4. [Q9NRH2-1]
XP_005265302.1. XM_005265245.1. [Q9NRH2-1]
XP_005265303.1. XM_005265246.1. [Q9NRH2-1]
UniGeneiHs.476052.

Genome annotation databases

EnsembliENST00000296088; ENSP00000296088; ENSG00000163788. [Q9NRH2-1]
ENST00000429705; ENSP00000411375; ENSG00000163788. [Q9NRH2-1]
ENST00000454177; ENSP00000401246; ENSG00000163788. [Q9NRH2-1]
GeneIDi54861.
KEGGihsa:54861.
UCSCiuc003cms.4. human. [Q9NRH2-1]
uc003cmu.3. human. [Q9NRH2-2]

Polymorphism databases

DMDMi90185235.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D43636 mRNA. Translation: BAA07744.2 . Different initiation.
AF226044 mRNA. Translation: AAF86944.1 .
AK000231 mRNA. Translation: BAA91023.1 .
AK314376 mRNA. Translation: BAG37003.1 .
CR749621 mRNA. Translation: CAH18415.1 . Different initiation.
CH471055 Genomic DNA. Translation: EAW64693.1 .
BC071567 mRNA. Translation: AAH71567.1 .
CCDSi CCDS43075.1. [Q9NRH2-1 ]
RefSeqi NP_001094064.1. NM_001100594.1. [Q9NRH2-1 ]
NP_060189.3. NM_017719.4. [Q9NRH2-1 ]
XP_005265302.1. XM_005265245.1. [Q9NRH2-1 ]
XP_005265303.1. XM_005265246.1. [Q9NRH2-1 ]
UniGenei Hs.476052.

3D structure databases

ProteinModelPortali Q9NRH2.
SMRi Q9NRH2. Positions 14-335.
ModBasei Search...

Protein-protein interaction databases

BioGridi 120211. 4 interactions.
IntActi Q9NRH2. 1 interaction.
MINTi MINT-1338450.
STRINGi 9606.ENSP00000296088.

Chemistry

BindingDBi Q9NRH2.
ChEMBLi CHEMBL1908384.
GuidetoPHARMACOLOGYi 2202.

PTM databases

PhosphoSitei Q9NRH2.

Polymorphism databases

DMDMi 90185235.

Proteomic databases

MaxQBi Q9NRH2.
PaxDbi Q9NRH2.
PRIDEi Q9NRH2.

Protocols and materials databases

DNASUi 54861.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296088 ; ENSP00000296088 ; ENSG00000163788 . [Q9NRH2-1 ]
ENST00000429705 ; ENSP00000411375 ; ENSG00000163788 . [Q9NRH2-1 ]
ENST00000454177 ; ENSP00000401246 ; ENSG00000163788 . [Q9NRH2-1 ]
GeneIDi 54861.
KEGGi hsa:54861.
UCSCi uc003cms.4. human. [Q9NRH2-1 ]
uc003cmu.3. human. [Q9NRH2-2 ]

Organism-specific databases

CTDi 54861.
GeneCardsi GC03P043303.
HGNCi HGNC:30598. SNRK.
HPAi HPA042163.
MIMi 612760. gene.
neXtProti NX_Q9NRH2.
PharmGKBi PA142670894.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000059616.
HOVERGENi HBG093970.
InParanoidi Q9NRH2.
KOi K08802.
OMAi TTSGRKC.
OrthoDBi EOG7CZK55.
PhylomeDBi Q9NRH2.
TreeFami TF351991.

Enzyme and pathway databases

SignaLinki Q9NRH2.

Miscellaneous databases

ChiTaRSi SNRK. human.
GeneWikii SNRK.
GenomeRNAii 54861.
NextBioi 57744.
PROi Q9NRH2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NRH2.
Bgeei Q9NRH2.
CleanExi HS_SNRK.
Genevestigatori Q9NRH2.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of human and mouse SNRK sucrose non-fermenting protein (SNF-1)-related kinases."
    Kertesz N., Samson J., Debacker C., Wu H., Labastie M.-C.
    Gene 294:13-24(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION.
  2. "Identification of the sucrose non-fermenting related kinase SNRK, as a novel LKB1 substrate."
    Jaleel M., McBride A., Lizcano J.M., Deak M., Toth R., Morrice N.A., Alessi D.R.
    FEBS Lett. 579:1417-1423(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-173, MUTAGENESIS OF THR-173.
  3. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
    DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  5. Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adrenal gland.
  6. "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: Brain and Colon mucosa.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Liver.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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: Brain.
  10. "Molecular cloning and characterization of a novel mammalian protein kinase harboring a homology domain that defines a subfamily of serine/threonine kinases."
    Becker W., Heukelbach J., Kentrup H., Joost H.G.
    Eur. J. Biochem. 235:736-743(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "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].
  12. "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-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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] SER-260; SER-391; SER-611; LEU-748 AND MET-765.

Entry informationi

Entry nameiSNRK_HUMAN
AccessioniPrimary (citable) accession number: Q9NRH2
Secondary accession number(s): B2RAV6
, Q14706, Q68D15, Q6IQ46, Q9NXI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 113 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 3
    Human chromosome 3: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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