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Protein

Mitogen-activated protein kinase kinase kinase 12

Gene

MAP3K12

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

Functioni

May be an activator of the JNK/SAPK pathway. Phosphorylates beta-casein, histone 1 and myelin basic protein in vitro.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei152 – 1521ATPPROSITE-ProRule annotation
Active sitei236 – 2361Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi131 – 1399ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase kinase kinase activity Source: UniProtKB-EC
  3. protein homodimerization activity Source: UniProtKB
  4. protein kinase activity Source: ProtInc
  5. protein kinase binding Source: UniProtKB
  6. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. histone phosphorylation Source: UniProtKB
  2. intracellular signal transduction Source: ProtInc
  3. JNK cascade Source: UniProtKB
  4. peptidyl-serine phosphorylation Source: UniProtKB
  5. peptidyl-threonine phosphorylation Source: UniProtKB
  6. protein autophosphorylation Source: UniProtKB
  7. protein phosphorylation Source: UniProtKB
  8. regulation of mitochondrion degradation Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ12852.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase kinase kinase 12 (EC:2.7.11.25)
Alternative name(s):
Dual leucine zipper bearing kinase
Short name:
DLK
Leucine-zipper protein kinase
Short name:
ZPK
MAPK-upstream kinase
Short name:
MUK
Mixed lineage kinase
Gene namesi
Name:MAP3K12
Synonyms:ZPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:6851. MAP3K12.

Subcellular locationi

  1. Cytoplasm By similarity
  2. Membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  1. axon Source: Ensembl
  2. cytoplasm Source: ProtInc
  3. cytosol Source: UniProtKB
  4. growth cone Source: Ensembl
  5. membrane Source: UniProtKB
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30595.

Polymorphism and mutation databases

BioMutaiMAP3K12.
DMDMi116242624.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 859859Mitogen-activated protein kinase kinase kinase 12PRO_0000086261Add
BLAST

Post-translational modificationi

Autophosphorylated on Ser/Thr. Phosphorylated in cytosol under basal conditions and dephosphorylated when membrane-associated (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ12852.
PRIDEiQ12852.

PTM databases

PhosphoSiteiQ12852.

Expressioni

Tissue specificityi

Highly expressed in brain and kidney.

Gene expression databases

BgeeiQ12852.
CleanExiHS_MAP3K12.
ExpressionAtlasiQ12852. baseline and differential.
GenevestigatoriQ12852.

Organism-specific databases

HPAiHPA039936.

Interactioni

Subunit structurei

Interacts with MBIP.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FRA10AC1Q70Z532EBI-710223,EBI-710176

Protein-protein interaction databases

BioGridi113566. 13 interactions.
IntActiQ12852. 9 interactions.
MINTiMINT-1382019.
STRINGi9606.ENSP00000267079.

Structurei

3D structure databases

ProteinModelPortaliQ12852.
SMRiQ12852. Positions 68-418.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini125 – 366242Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni390 – 41122Leucine-zipper 1Add
BLAST
Regioni443 – 46422Leucine-zipper 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi665 – 6684Poly-Pro
Compositional biasi720 – 73112Glu-rich (acidic)Add
BLAST

Domaini

Interacts with MBIP through the leucine-zipper motif.

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118807.
HOGENOMiHOG000113435.
HOVERGENiHBG052383.
InParanoidiQ12852.
KOiK04423.
OMAiSMRKLDP.
OrthoDBiEOG7B8S3P.
PhylomeDBiQ12852.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR017419. MAP3K12_MAP3K13.
IPR027257. MAPKKK12.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500741. MAPKKK12. 1 hit.
PIRSF038165. MAPKKK12_MAPKKK13. 1 hit.
PRINTSiPR00109. TYRKINASE.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q12852-1) [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
MACLHETRTP SPSFGGFVST LSEASMRKLD PDTSDCTPEK DLTPTHVLQL
60 70 80 90 100
HEQDAGGPGG AAGSPESRAS RVRADEVRLQ CQSGSGFLEG LFGCLRPVWT
110 120 130 140 150
MIGKAYSTEH KQQQEDLWEV PFEEILDLQW VGSGAQGAVF LGRFHGEEVA
160 170 180 190 200
VKKVRDLKET DIKHLRKLKH PNIITFKGVC TQAPCYCILM EFCAQGQLYE
210 220 230 240 250
VLRAGRPVTP SLLVDWSMGI AGGMNYLHLH KIIHRDLKSP NMLITYDDVV
260 270 280 290 300
KISDFGTSKE LSDKSTKMSF AGTVAWMAPE VIRNEPVSEK VDIWSFGVVL
310 320 330 340 350
WELLTGEIPY KDVDSSAIIW GVGSNSLHLP VPSSCPDGFK ILLRQCWNSK
360 370 380 390 400
PRNRPSFRQI LLHLDIASAD VLSTPQETYF KSQAEWREEV KLHFEKIKSE
410 420 430 440 450
GTCLHRLEEE LVMRRREELR HALDIREHYE RKLERANNLY MELNALMLQL
460 470 480 490 500
ELKERELLRR EQALERRCPG LLKPHPSRGL LHGNTMEKLI KKRNVPQKLS
510 520 530 540 550
PHSKRPDILK TESLLPKLDA ALSGVGLPGC PKGPPSPGRS RRGKTRHRKA
560 570 580 590 600
SAKGSCGDLP GLRTAVPPHE PGGPGSPGGL GGGPSAWEAC PPALRGLHHD
610 620 630 640 650
LLLRKMSSSS PDLLSAALGS RGRGATGGAG DPGSPPPARG DTPPSEGSAP
660 670 680 690 700
GSTSPDSPGG AKGEPPPPVG PGEGVGLLGT GREGTSGRGG SRAGSQHLTP
710 720 730 740 750
AALLYRAAVT RSQKRGISSE EEEGEVDSEV ELTSSQRWPQ SLNMRQSLST
760 770 780 790 800
FSSENPSDGE EGTASEPSPS GTPEVGSTNT DERPDERSDD MCSQGSEIPL
810 820 830 840 850
DPPPSEVIPG PEPSSLPIPH QELLRERGPP NSEDSDCDST ELDNSNSVDA

LRPPASLPP
Length:859
Mass (Da):93,219
Last modified:October 17, 2006 - v2
Checksum:i1E1BCAD2F6DFCFE8
GO
Isoform 2 (identifier: Q12852-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     46-46: H → QCVLRDVVPLGGQGGGGPSPSPGGEPPPEPFANS

Note: No experimental confirmation available.

Show »
Length:892
Mass (Da):96,322
Checksum:iEA0C10CFE2461876
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti355 – 3551P → S in BAG52841 (PubMed:14702039).Curated
Sequence conflicti498 – 4981K → N in AAA67343 (PubMed:8037767).Curated
Sequence conflicti504 – 5041K → Q in AAA67343 (PubMed:8037767).Curated
Sequence conflicti511 – 5111T → A in AAA67343 (PubMed:8037767).Curated
Sequence conflicti533 – 5331G → A in AAA67343 (PubMed:8037767).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti409 – 4091E → K in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication
VAR_040705
Natural varianti628 – 6281G → R.1 Publication
Corresponds to variant rs34366500 [ dbSNP | Ensembl ].
VAR_040706
Natural varianti640 – 6401G → S.1 Publication
Corresponds to variant rs55794887 [ dbSNP | Ensembl ].
VAR_040707

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei46 – 461H → QCVLRDVVPLGGQGGGGPSP SPGGEPPPEPFANS in isoform 2. 1 PublicationVSP_044646

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07358 mRNA. Translation: AAA67343.1.
AF283475 Genomic DNA. Translation: AAL67158.1.
AK094195 mRNA. Translation: BAG52841.1.
AC023509 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96715.1.
BC050050 mRNA. Translation: AAH50050.1. Sequence problems.
CCDSiCCDS55831.1. [Q12852-2]
CCDS8860.1. [Q12852-1]
PIRiJC2363.
RefSeqiNP_001180440.1. NM_001193511.1. [Q12852-2]
NP_006292.3. NM_006301.3. [Q12852-1]
XP_005269195.1. XM_005269138.2. [Q12852-2]
XP_006719651.1. XM_006719588.2. [Q12852-2]
UniGeneiHs.713539.

Genome annotation databases

EnsembliENST00000267079; ENSP00000267079; ENSG00000139625. [Q12852-1]
ENST00000547035; ENSP00000448689; ENSG00000139625. [Q12852-2]
ENST00000547488; ENSP00000449038; ENSG00000139625. [Q12852-2]
GeneIDi7786.
KEGGihsa:7786.
UCSCiuc001sdm.2. human. [Q12852-1]
uc001sdn.2. human.

Polymorphism and mutation databases

BioMutaiMAP3K12.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07358 mRNA. Translation: AAA67343.1.
AF283475 Genomic DNA. Translation: AAL67158.1.
AK094195 mRNA. Translation: BAG52841.1.
AC023509 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96715.1.
BC050050 mRNA. Translation: AAH50050.1. Sequence problems.
CCDSiCCDS55831.1. [Q12852-2]
CCDS8860.1. [Q12852-1]
PIRiJC2363.
RefSeqiNP_001180440.1. NM_001193511.1. [Q12852-2]
NP_006292.3. NM_006301.3. [Q12852-1]
XP_005269195.1. XM_005269138.2. [Q12852-2]
XP_006719651.1. XM_006719588.2. [Q12852-2]
UniGeneiHs.713539.

3D structure databases

ProteinModelPortaliQ12852.
SMRiQ12852. Positions 68-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113566. 13 interactions.
IntActiQ12852. 9 interactions.
MINTiMINT-1382019.
STRINGi9606.ENSP00000267079.

Chemistry

BindingDBiQ12852.
ChEMBLiCHEMBL1908389.
GuidetoPHARMACOLOGYi2072.

PTM databases

PhosphoSiteiQ12852.

Polymorphism and mutation databases

BioMutaiMAP3K12.
DMDMi116242624.

Proteomic databases

PaxDbiQ12852.
PRIDEiQ12852.

Protocols and materials databases

DNASUi7786.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267079; ENSP00000267079; ENSG00000139625. [Q12852-1]
ENST00000547035; ENSP00000448689; ENSG00000139625. [Q12852-2]
ENST00000547488; ENSP00000449038; ENSG00000139625. [Q12852-2]
GeneIDi7786.
KEGGihsa:7786.
UCSCiuc001sdm.2. human. [Q12852-1]
uc001sdn.2. human.

Organism-specific databases

CTDi7786.
GeneCardsiGC12M053870.
H-InvDBHIX0010672.
HGNCiHGNC:6851. MAP3K12.
HPAiHPA039936.
MIMi600447. gene.
neXtProtiNX_Q12852.
PharmGKBiPA30595.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118807.
HOGENOMiHOG000113435.
HOVERGENiHBG052383.
InParanoidiQ12852.
KOiK04423.
OMAiSMRKLDP.
OrthoDBiEOG7B8S3P.
PhylomeDBiQ12852.

Enzyme and pathway databases

SignaLinkiQ12852.

Miscellaneous databases

ChiTaRSiMAP3K12. human.
GeneWikiiMAP3K12.
GenomeRNAii7786.
NextBioi30143.
PROiQ12852.
SOURCEiSearch...

Gene expression databases

BgeeiQ12852.
CleanExiHS_MAP3K12.
ExpressionAtlasiQ12852. baseline and differential.
GenevestigatoriQ12852.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR017419. MAP3K12_MAP3K13.
IPR027257. MAPKKK12.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500741. MAPKKK12. 1 hit.
PIRSF038165. MAPKKK12_MAPKKK13. 1 hit.
PRINTSiPR00109. TYRKINASE.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a novel putative protein kinase having a leucine zipper domain from human brain."
    Reddy U.R., Pleasure D.
    Biochem. Biophys. Res. Commun. 202:613-620(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Teratocarcinoma.
  2. "SP3 acts as a positive regulator on the core promoter of human ZPK gene."
    Itoh A., Wang Z., Ito Y., Reddy U.R., Itoh T.
    Biochem. Biophys. Res. Commun. 313:612-618(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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).
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Testis.
  7. "MAPK upstream kinase (MUK)-binding inhibitory protein, a negative regulator of MUK/Dual leucine zipper-bearing kinase/leucine zipper protein kinase."
    Fukuyama K., Yoshida M., Yamashita A., Deyama T., Baba M., Suzuki A., Mohri H., Ikezawa Z., Nakajima H., Hirai S., Ohno S.
    J. Biol. Chem. 275:21247-21254(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MBIP.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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] LYS-409; ARG-628 AND SER-640.

Entry informationi

Entry nameiM3K12_HUMAN
AccessioniPrimary (citable) accession number: Q12852
Secondary accession number(s): B3KSS9
, G3V1Y2, Q86VQ5, Q8WY25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 17, 2006
Last modified: April 29, 2015
This is version 146 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 12
    Human chromosome 12: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.