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Q9NSY1

- BMP2K_HUMAN

UniProt

Q9NSY1 - BMP2K_HUMAN

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Protein

BMP-2-inducible protein kinase

Gene

BMP2K

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

Functioni

May be involved in osteoblast differentiation.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791ATPPROSITE-ProRule annotation
Active sitei180 – 1801Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi57 – 659ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphatase regulator activity Source: Ensembl
  3. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. regulation of bone mineralization Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9NSY1.

Names & Taxonomyi

Protein namesi
Recommended name:
BMP-2-inducible protein kinase (EC:2.7.11.1)
Short name:
BIKe
Gene namesi
Name:BMP2K
Synonyms:BIKE
ORF Names:HRIHFB2017
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:18041. BMP2K.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134992822.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11611161BMP-2-inducible protein kinasePRO_0000085663Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Phosphoserine1 Publication
Modified residuei834 – 8341Phosphothreonine1 Publication
Modified residuei928 – 9281PhosphoserineBy similarity
Modified residuei1029 – 10291Phosphoserine2 Publications
Modified residuei1031 – 10311PhosphoserineBy similarity
Modified residuei1032 – 10321Phosphoserine1 Publication
Modified residuei1076 – 10761Phosphoserine1 Publication
Modified residuei1107 – 11071Phosphoserine3 Publications
Modified residuei1111 – 11111Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NSY1.
PaxDbiQ9NSY1.
PRIDEiQ9NSY1.

PTM databases

PhosphoSiteiQ9NSY1.

Expressioni

Gene expression databases

BgeeiQ9NSY1.
CleanExiHS_BMP2K.
ExpressionAtlasiQ9NSY1. baseline and differential.
GenevestigatoriQ9NSY1.

Organism-specific databases

HPAiHPA026436.
HPA026451.
HPA026501.

Interactioni

Protein-protein interaction databases

BioGridi120735. 9 interactions.
IntActiQ9NSY1. 5 interactions.
STRINGi9606.ENSP00000334836.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4W9WX-ray1.72A39-344[»]
4W9XX-ray2.14A38-345[»]
ProteinModelPortaliQ9NSY1.
SMRiQ9NSY1. Positions 46-378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 316266Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi12 – 4029Gly-richAdd
BLAST
Compositional biasi425 – 559135Gln/His-richAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00510000046552.
HOGENOMiHOG000095243.
HOVERGENiHBG050703.
InParanoidiQ9NSY1.
KOiK08854.
OMAiVPFISHP.
OrthoDBiEOG7PP566.
PhylomeDBiQ9NSY1.
TreeFamiTF335936.

Family and domain databases

InterProiIPR026105. BMP-2-ind_kinase.
IPR028182. BMP2K_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22967:SF10. PTHR22967:SF10. 1 hit.
PfamiPF15282. BMP2K_C. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NSY1-1) [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
MKKFSRMPKS EGGSGGGAAG GGAGGAGAGA GCGSGGSSVG VRVFAVGRHQ
60 70 80 90 100
VTLEESLAEG GFSTVFLVRT HGGIRCALKR MYVNNMPDLN VCKREITIMK
110 120 130 140 150
ELSGHKNIVG YLDCAVNSIS DNVWEVLILM EYCRAGQVVN QMNKKLQTGF
160 170 180 190 200
TEPEVLQIFC DTCEAVARLH QCKTPIIHRD LKVENILLND GGNYVLCDFG
210 220 230 240 250
SATNKFLNPQ KDGVNVVEEE IKKYTTLSYR APEMINLYGG KPITTKADIW
260 270 280 290 300
ALGCLLYKLC FFTLPFGESQ VAICDGNFTI PDNSRYSRNI HCLIRFMLEP
310 320 330 340 350
DPEHRPDIFQ VSYFAFKFAK KDCPVSNINN SSIPSALPEP MTASEAAARK
360 370 380 390 400
SQIKARITDT IGPTETSIAP RQRPKANSAT TATPSVLTIQ SSATPVKVLA
410 420 430 440 450
PGEFGNHRPK GALRPGNGPE ILLGQGPPQQ PPQQHRVLQQ LQQGDWRLQQ
460 470 480 490 500
LHLQHRHPHQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQHHHH HHHHLLQDAY
510 520 530 540 550
MQQYQHATQQ QQMLQQQFLM HSVYQPQPSA SQYPTMMPQY QQAFFQQQML
560 570 580 590 600
AQHQPSQQQA SPEYLTSPQE FSPALVSYTS SLPAQVGTIM DSSYSANRSV
610 620 630 640 650
ADKEAIANFT NQKNISNPPD MSGWNPFGED NFSKLTEEEL LDREFDLLRS
660 670 680 690 700
NRLEERASSD KNVDSLSAPH NHPPEDPFGS VPFISHSGSP EKKAEHSSIN
710 720 730 740 750
QENGTANPIK NGKTSPASKD QRTGKKTSVQ GQVQKGNDES ESDFESDPPS
760 770 780 790 800
PKSSEEEEQD DEEVLQGEQG DFNDDDTEPE NLGHRPLLMD SEDEEEEEKH
810 820 830 840 850
SSDSDYEQAK AKYSDMSSVY RDRSGSGPTQ DLNTILLTSA QLSSDVAVET
860 870 880 890 900
PKQEFDVFGA VPFFAVRAQQ PQQEKNEKNL PQHRFPAAGL EQEEFDVFTK
910 920 930 940 950
APFSKKVNVQ ECHAVGPEAH TIPGYPKSVD VFGSTPFQPF LTSTSKSESN
960 970 980 990 1000
EDLFGLVPFD EITGSQQQKV KQRSLQKLSS RQRRTKQDMS KSNGKRHHGT
1010 1020 1030 1040 1050
PTSTKKTLKP TYRTPERARR HKKVGRRDSQ SSNEFLTISD SKENISVALT
1060 1070 1080 1090 1100
DGKDRGNVLQ PEESLLDPFG AKPFHSPDLS WHPPHQGLSD IRADHNTVLP
1110 1120 1130 1140 1150
GRPRQNSLHG SFHSADVLKM DDFGAVPFTE LVVQSITPHQ SQQSQPVELD
1160
PFGAAPFPSK Q
Length:1,161
Mass (Da):129,172
Last modified:August 22, 2003 - v2
Checksum:i5C38A86E95935EC2
GO
Isoform 2 (identifier: Q9NSY1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     651-662: NRLEERASSDKN → SKGHLKAYFASQ
     663-1161: Missing.

Show »
Length:662
Mass (Da):73,838
Checksum:iED443E4DC0696FF3
GO
Isoform 3 (identifier: Q9NSY1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     330-340: NSSIPSALPEP → KCCKQLLRHGALLTEILLFLQLFLNR
     651-662: NRLEERASSDKN → SKGHLKAYFASQ
     663-1161: Missing.

Note: No experimental confirmation available.

Show »
Length:677
Mass (Da):75,812
Checksum:iFF17E464DB5F952C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti342 – 3421T → A in AAH36021. (PubMed:15489334)Curated
Sequence conflicti471 – 48616Missing in CAB70863. (PubMed:17974005)CuratedAdd
BLAST
Sequence conflicti478 – 4781Q → R in AAH36021. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681V → M in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
VAR_040388
Natural varianti212 – 2121D → V.1 Publication
Corresponds to variant rs56143363 [ dbSNP | Ensembl ].
VAR_040389
Natural varianti288 – 2881R → H.1 Publication
Corresponds to variant rs55782848 [ dbSNP | Ensembl ].
VAR_040390
Natural varianti405 – 4051G → S.1 Publication
Corresponds to variant rs2288255 [ dbSNP | Ensembl ].
VAR_051618
Natural varianti486 – 4861Q → H.
Corresponds to variant rs2114202 [ dbSNP | Ensembl ].
VAR_059765
Natural varianti1002 – 10021T → S.
Corresponds to variant rs12507099 [ dbSNP | Ensembl ].
VAR_051619

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei330 – 34011NSSIPSALPEP → KCCKQLLRHGALLTEILLFL QLFLNR in isoform 3. 1 PublicationVSP_008093Add
BLAST
Alternative sequencei651 – 66212NRLEE…SSDKN → SKGHLKAYFASQ in isoform 2 and isoform 3. 4 PublicationsVSP_008091Add
BLAST
Alternative sequencei663 – 1161499Missing in isoform 2 and isoform 3. 4 PublicationsVSP_008092Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK075278 mRNA. Translation: BAC11515.1.
AK292147 mRNA. Translation: BAF84836.1.
AL137275 mRNA. Translation: CAB70673.1.
AL137661 mRNA. Translation: CAB70863.1.
AC098818 Genomic DNA. Translation: AAY40926.1.
BC036021 mRNA. Translation: AAH36021.1.
AF527532 mRNA. Translation: AAM88867.1.
AB015331 mRNA. Translation: BAA34790.1.
CCDSiCCDS34019.1. [Q9NSY1-2]
CCDS47083.1. [Q9NSY1-1]
PIRiT46347.
T46364.
RefSeqiNP_060063.2. NM_017593.3. [Q9NSY1-2]
NP_942595.1. NM_198892.1. [Q9NSY1-1]
UniGeneiHs.146551.

Genome annotation databases

EnsembliENST00000335016; ENSP00000334836; ENSG00000138756. [Q9NSY1-1]
ENST00000502871; ENSP00000421768; ENSG00000138756. [Q9NSY1-2]
GeneIDi55589.
KEGGihsa:55589.
UCSCiuc003hlk.3. human. [Q9NSY1-1]

Polymorphism databases

DMDMi34222653.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK075278 mRNA. Translation: BAC11515.1 .
AK292147 mRNA. Translation: BAF84836.1 .
AL137275 mRNA. Translation: CAB70673.1 .
AL137661 mRNA. Translation: CAB70863.1 .
AC098818 Genomic DNA. Translation: AAY40926.1 .
BC036021 mRNA. Translation: AAH36021.1 .
AF527532 mRNA. Translation: AAM88867.1 .
AB015331 mRNA. Translation: BAA34790.1 .
CCDSi CCDS34019.1. [Q9NSY1-2 ]
CCDS47083.1. [Q9NSY1-1 ]
PIRi T46347.
T46364.
RefSeqi NP_060063.2. NM_017593.3. [Q9NSY1-2 ]
NP_942595.1. NM_198892.1. [Q9NSY1-1 ]
UniGenei Hs.146551.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4W9W X-ray 1.72 A 39-344 [» ]
4W9X X-ray 2.14 A 38-345 [» ]
ProteinModelPortali Q9NSY1.
SMRi Q9NSY1. Positions 46-378.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120735. 9 interactions.
IntActi Q9NSY1. 5 interactions.
STRINGi 9606.ENSP00000334836.

Chemistry

BindingDBi Q9NSY1.
ChEMBLi CHEMBL4522.
GuidetoPHARMACOLOGYi 1941.

PTM databases

PhosphoSitei Q9NSY1.

Polymorphism databases

DMDMi 34222653.

Proteomic databases

MaxQBi Q9NSY1.
PaxDbi Q9NSY1.
PRIDEi Q9NSY1.

Protocols and materials databases

DNASUi 55589.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000335016 ; ENSP00000334836 ; ENSG00000138756 . [Q9NSY1-1 ]
ENST00000502871 ; ENSP00000421768 ; ENSG00000138756 . [Q9NSY1-2 ]
GeneIDi 55589.
KEGGi hsa:55589.
UCSCi uc003hlk.3. human. [Q9NSY1-1 ]

Organism-specific databases

CTDi 55589.
GeneCardsi GC04P079697.
HGNCi HGNC:18041. BMP2K.
HPAi HPA026436.
HPA026451.
HPA026501.
neXtProti NX_Q9NSY1.
PharmGKBi PA134992822.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00510000046552.
HOGENOMi HOG000095243.
HOVERGENi HBG050703.
InParanoidi Q9NSY1.
KOi K08854.
OMAi VPFISHP.
OrthoDBi EOG7PP566.
PhylomeDBi Q9NSY1.
TreeFami TF335936.

Enzyme and pathway databases

SignaLinki Q9NSY1.

Miscellaneous databases

ChiTaRSi BMP2K. human.
GeneWikii BMP2K.
GenomeRNAii 55589.
NextBioi 60112.
PROi Q9NSY1.

Gene expression databases

Bgeei Q9NSY1.
CleanExi HS_BMP2K.
ExpressionAtlasi Q9NSY1. baseline and differential.
Genevestigatori Q9NSY1.

Family and domain databases

InterProi IPR026105. BMP-2-ind_kinase.
IPR028182. BMP2K_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR22967:SF10. PTHR22967:SF10. 1 hit.
Pfami PF15282. BMP2K_C. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 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 2).
    Tissue: Synovium and Thyroid.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Testis.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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 2), VARIANT SER-405.
    Tissue: Testis.
  5. Guo J.H., Yu L.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 537-1161 (ISOFORM 2).
    Tissue: Ovary.
  6. "Selection system for genes encoding nuclear-targeted proteins."
    Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
    Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 946-1161 (ISOFORM 1), SUBCELLULAR LOCATION.
    Tissue: Brain.
  7. "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-1107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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 THR-834 AND SER-1076, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-1107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-1029 AND SER-1032, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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-1029; SER-1107 AND SER-1111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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] MET-68; VAL-212 AND HIS-288.

Entry informationi

Entry nameiBMP2K_HUMAN
AccessioniPrimary (citable) accession number: Q9NSY1
Secondary accession number(s): O94791
, Q4W5H2, Q8IYF2, Q8N2G7, Q8NHG9, Q9NTG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: August 22, 2003
Last modified: October 29, 2014
This is version 129 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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