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Q61846

- MELK_MOUSE

UniProt

Q61846 - MELK_MOUSE

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Protein

Maternal embryonic leucine zipper kinase

Gene

Melk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis.2 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation
ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by autophosphorylation of the T-loop at Thr-167 and Ser-171: in contrast to other members of the SNF1 subfamily, phosphorylation at Thr-167 is not mediated by STK11/LKB1 but via autophosphorylation instead. Inhibited by calcium-binding. Kinase activity is also regulated by reducing agents: dithiothreitol (DTT) or reduced glutathione are required for kinase activity in vitro; such dependence is however not due to the presence of disulfide bonds (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei40 – 401ATPPROSITE-ProRule annotation
Active sitei132 – 1321Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 259ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium ion binding Source: UniProtKB
  3. lipid binding Source: UniProtKB-KW
  4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  5. protein kinase activity Source: MGI
  6. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. cell cycle Source: UniProtKB-KW
  3. cell proliferation Source: UniProtKB
  4. hemopoiesis Source: UniProtKB
  5. intrinsic apoptotic signaling pathway in response to oxidative stress Source: MGI
  6. neural precursor cell proliferation Source: UniProtKB
  7. peptidyl-tyrosine phosphorylation Source: GOC
  8. positive regulation of apoptotic process Source: UniProtKB
  9. protein autophosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle

Keywords - Ligandi

ATP-binding, Calcium, Lipid-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Maternal embryonic leucine zipper kinase (EC:2.7.11.1)
Alternative name(s):
Protein kinase PK38
Short name:
mPK38
Tyrosine-protein kinase MELK (EC:2.7.10.2)
Gene namesi
Name:Melk
Synonyms:Kiaa0175, Pk38
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:106924. Melk.

Subcellular locationi

Cell membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  1. cell cortex Source: UniProtKB
  2. cytoplasm Source: MGI
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401K → R: Loss of kinase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 643643Maternal embryonic leucine zipper kinasePRO_0000086324Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 561Phosphothreonine; by autocatalysisBy similarity
Modified residuei163 – 1631Phosphotyrosine; by autocatalysisBy similarity
Modified residuei167 – 1671Phosphothreonine; by autocatalysisBy similarity
Modified residuei171 – 1711Phosphoserine; by autocatalysisBy similarity
Modified residuei253 – 2531Phosphoserine; by autocatalysisBy similarity
Modified residuei336 – 3361Phosphoserine; by autocatalysisBy similarity
Modified residuei343 – 3431Phosphoserine; by autocatalysisBy similarity
Modified residuei352 – 3521Phosphoserine; by autocatalysisBy similarity
Modified residuei399 – 3991Phosphoserine; by autocatalysisBy similarity
Modified residuei423 – 4231Phosphoserine; by autocatalysisBy similarity
Modified residuei486 – 4861Phosphothreonine; by autocatalysisBy similarity
Modified residuei490 – 4901PhosphoserineBy similarity
Modified residuei497 – 4971Phosphoserine; by autocatalysisBy similarity
Modified residuei510 – 5101PhosphothreonineBy similarity
Modified residuei521 – 5211Phosphoserine; alternate2 Publications
Modified residuei521 – 5211Phosphoserine; by autocatalysis; alternate2 Publications
Modified residuei531 – 5311Phosphothreonine; by autocatalysisBy similarity

Post-translational modificationi

Autophosphorylated: autophosphorylation of the T-loop at Thr-167 and Ser-171 is required for activation.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ61846.
PaxDbiQ61846.
PRIDEiQ61846.

PTM databases

PhosphoSiteiQ61846.

Expressioni

Tissue specificityi

Expressed in testis, ovary, thymus, spleen and T-cell. Expressed by neural progenitors: highly enriched in cultures containing multipotent progenitors.3 Publications

Developmental stagei

Expressed in the 2-cell-stage embryo, followed by a strong expression at 8-cell-stage.1 Publication

Gene expression databases

BgeeiQ61846.
CleanExiMM_MELK.
ExpressionAtlasiQ61846. baseline and differential.
GenevestigatoriQ61846.

Interactioni

Subunit structurei

Monomer. Interacts with ZNF622 and PPP1R8 (By similarity).By similarity

Protein-protein interaction databases

BioGridi201390. 9 interactions.

Structurei

Secondary structure

1
643
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 75Combined sources
Turni8 – 103Combined sources
Beta strandi11 – 199Combined sources
Beta strandi21 – 3010Combined sources
Turni31 – 333Combined sources
Beta strandi36 – 438Combined sources
Helixi44 – 474Combined sources
Helixi48 – 514Combined sources
Helixi52 – 6211Combined sources
Beta strandi72 – 776Combined sources
Beta strandi79 – 879Combined sources
Helixi94 – 1018Combined sources
Helixi106 – 12520Combined sources
Helixi135 – 1373Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi146 – 1483Combined sources
Helixi172 – 1743Combined sources
Helixi177 – 1793Combined sources
Helixi188 – 20417Combined sources
Helixi214 – 22310Combined sources
Helixi234 – 24310Combined sources
Turni248 – 2503Combined sources
Helixi254 – 2585Combined sources
Helixi261 – 2644Combined sources
Helixi284 – 29411Combined sources
Helixi298 – 3058Combined sources
Helixi312 – 32615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BFMX-ray2.35A1-326[»]
4CQGX-ray2.57A1-326[»]
ProteinModelPortaliQ61846.
SMRiQ61846. Positions 2-312, 546-643.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 263253Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini594 – 64350KA1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni282 – 32140UBA-likeBy similarityAdd
BLAST
Regioni326 – 643318Autoinhibitory regionBy similarityAdd
BLAST

Domaini

The KA1 domain mediates binding to phospholipids and targeting to membranes.By similarity

Sequence similaritiesi

Contains 1 KA1 (kinase-associated) domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118892.
HOGENOMiHOG000233023.
HOVERGENiHBG106273.
InParanoidiQ61846.
KOiK08799.
OMAiWQSKNPF.
OrthoDBiEOG7CK36C.
TreeFamiTF314032.

Family and domain databases

Gene3Di3.30.310.80. 1 hit.
InterProiIPR028375. KA1/Ssp2_C.
IPR001772. KA1_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50032. KA1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q61846-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKDYDELLKY YELYETIGTG GFAKVKLACH VLTGEMVAIK IMDKNALGSD
60 70 80 90 100
LPRVKTEIDA LKSLRHQHIC QLYHVLETKN KIFMVLEYCP GGELFDYIIS
110 120 130 140 150
QDRLSEEETR VVFRQILSAV AYVHSQGYAH RDLKPENLLF DENHKLKLID
160 170 180 190 200
FGLCAKPKGN KDYHLQTCCG SLAYAAPELI QGKSYLGSEA DVWSMGILLY
210 220 230 240 250
VLMCGFLPFD DDNVMALYKK IMRGKYEVPK WLSPSSILLL QQMLQVDPKK
260 270 280 290 300
RISMRNLLNH PWVMQDYSCP VEWQSKTPLT HLDEDCVTEL SVHHRSSRQT
310 320 330 340 350
MEDLISSWQY DHLTATYLLL LAKKARGKPA RLQLLSFSCG TASTTPKSKN
360 370 380 390 400
LSLEDMSTSD DNCVAGLIDY ELCEDKLLAP KTPQVTKHLA ESNHAASKSP
410 420 430 440 450
APGVRRAVAN KLMDKENVCT PKSSVKNEEQ FVFSEPKIPV SKNQYKREIP
460 470 480 490 500
ASPTRFPTPA KARAQCLREA PVRTPGNSAG ADTLTTGVIS PERRCRSMDV
510 520 530 540 550
DLNQAHMEDT PKKKGTNVFG SLERGLDKVL TALTRNKKKG SARDGPRKRK
560 570 580 590 600
LHYNVTTTRL VNPDQLLSEI MAILPKKNVD FVQKGYTLKC QTQSDFGKVT
610 620 630 640
MQFELEVCQL QRPDVVGIRR QRLKGDAWVY KRLVEDILSG CKM
Length:643
Mass (Da):72,729
Last modified:July 27, 2011 - v2
Checksum:i5637D2A4E8CFA216
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti335 – 3351L → P in CAA64641. (PubMed:9136115)Curated
Sequence conflicti335 – 3351L → P in BAC97886. (PubMed:14621295)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76158 mRNA. Translation: AAB72030.1.
X95351 mRNA. Translation: CAA64641.1.
AK011932 mRNA. Translation: BAB27923.1.
AK145316 mRNA. Translation: BAE26362.1.
AK164138 mRNA. Translation: BAE37644.1.
AK129076 mRNA. Translation: BAC97886.1.
AL805952, AL807399 Genomic DNA. Translation: CAM14393.1.
AL807399, AL805952 Genomic DNA. Translation: CAM22652.1.
CCDSiCCDS18124.1.
RefSeqiNP_034920.2. NM_010790.2.
UniGeneiMm.268668.

Genome annotation databases

EnsembliENSMUST00000045607; ENSMUSP00000043806; ENSMUSG00000035683.
GeneIDi17279.
KEGGimmu:17279.
UCSCiuc008srv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76158 mRNA. Translation: AAB72030.1 .
X95351 mRNA. Translation: CAA64641.1 .
AK011932 mRNA. Translation: BAB27923.1 .
AK145316 mRNA. Translation: BAE26362.1 .
AK164138 mRNA. Translation: BAE37644.1 .
AK129076 mRNA. Translation: BAC97886.1 .
AL805952 , AL807399 Genomic DNA. Translation: CAM14393.1 .
AL807399 , AL805952 Genomic DNA. Translation: CAM22652.1 .
CCDSi CCDS18124.1.
RefSeqi NP_034920.2. NM_010790.2.
UniGenei Mm.268668.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BFM X-ray 2.35 A 1-326 [» ]
4CQG X-ray 2.57 A 1-326 [» ]
ProteinModelPortali Q61846.
SMRi Q61846. Positions 2-312, 546-643.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201390. 9 interactions.

PTM databases

PhosphoSitei Q61846.

Proteomic databases

MaxQBi Q61846.
PaxDbi Q61846.
PRIDEi Q61846.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000045607 ; ENSMUSP00000043806 ; ENSMUSG00000035683 .
GeneIDi 17279.
KEGGi mmu:17279.
UCSCi uc008srv.1. mouse.

Organism-specific databases

CTDi 9833.
MGIi MGI:106924. Melk.
Rougei Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118892.
HOGENOMi HOG000233023.
HOVERGENi HBG106273.
InParanoidi Q61846.
KOi K08799.
OMAi WQSKNPF.
OrthoDBi EOG7CK36C.
TreeFami TF314032.

Miscellaneous databases

NextBioi 291778.
PROi Q61846.
SOURCEi Search...

Gene expression databases

Bgeei Q61846.
CleanExi MM_MELK.
ExpressionAtlasi Q61846. baseline and differential.
Genevestigatori Q61846.

Family and domain databases

Gene3Di 3.30.310.80. 1 hit.
InterProi IPR028375. KA1/Ssp2_C.
IPR001772. KA1_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50032. KA1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a cDNA encoding a novel protein serine/threonine kinase predominantly expressed in hematopoietic cells."
    Gil M., Yang Y., Lee Y., Choi I., Ha H.
    Gene 195:295-301(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Keratinocyte.
  2. "New member of the Snf1/AMPK kinase family, Melk, is expressed in the mouse egg and preimplantation embryo."
    Heyer B.S., Warsowe J., Solter D., Knowles B.B., Ackerman S.L.
    Mol. Reprod. Dev. 47:148-156(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: C57BL/6 X DBA/2.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Spinal cord.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic tail.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. Cited for: FUNCTION, TISSUE SPECIFICITY.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Murine protein serine/threonine kinase 38 activates apoptosis signal-regulating kinase 1 via Thr 838 phosphorylation."
    Jung H., Seong H.A., Ha H.
    J. Biol. Chem. 283:34541-34553(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MAP3K5, MUTAGENESIS OF LYS-40.
  9. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMELK_MOUSE
AccessioniPrimary (citable) accession number: Q61846
Secondary accession number(s): Q3TPU1, Q61804, Q6ZQH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3