Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mitogen-activated protein kinase kinase kinase MLT

Gene

Zak

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

Functioni

Stress-activated component of a protein kinase signal transduction cascade. Regulates the JNK and p38 pathways. Pro-apoptotic. Role in regulation of S and G2 cell cycle checkpoint by direct phosphorylation of CHEK2. Isoform 1, but not isoform 2, phosphorylates histone H3 at 'Ser-28'.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Mg2+1 Publication

Enzyme regulationi

Activated by phosphorylation by PKN1 and autophosphorylation on Thr-161 and Ser-165.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451ATPBy similarityPROSITE-ProRule annotation
Active sitei133 – 1331Proton acceptorBy similarityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 309ATPBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. MAP kinase kinase kinase activity Source: MGI
  4. poly(A) RNA binding Source: MGI
  5. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. activation of JUN kinase activity Source: MGI
  2. activation of MAPKK activity Source: GOC
  3. cell cycle arrest Source: MGI
  4. cell cycle checkpoint Source: UniProtKB
  5. cytoskeleton organization Source: MGI
  6. DNA damage checkpoint Source: MGI
  7. intracellular signal transduction Source: UniProtKB
  8. positive regulation of apoptotic process Source: UniProtKB
  9. protein phosphorylation Source: UniProtKB
  10. response to radiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase kinase kinase MLT (EC:2.7.11.25)
Alternative name(s):
Leucine zipper- and sterile alpha motif kinase ZAK
MLK-like mitogen-activated protein triple kinase
Mixed lineage kinase-related kinase
Short name:
MLK-related kinase
Short name:
MRK
Sterile alpha motif- and leucine zipper-containing kinase AZK
Gene namesi
Name:Zak
Synonyms:Mltk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:2443258. Zak.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication
Note: Appears to shuttle between nucleus and cytoplasm.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451K → M: Loss of kinase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 802802Mitogen-activated protein kinase kinase kinase MLTPRO_0000086339Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei3 – 31PhosphoserineBy similarity
Modified residuei155 – 1551PhosphoserineBy similarity
Modified residuei161 – 1611Phosphothreonine; by autocatalysisBy similarity
Modified residuei165 – 1651Phosphoserine; by autocatalysisBy similarity
Modified residuei264 – 2641PhosphoserineBy similarity
Modified residuei275 – 2751PhosphoserineBy similarity
Modified residuei302 – 3021PhosphoserineBy similarity
Modified residuei326 – 3261PhosphoserineBy similarity
Modified residuei328 – 3281PhosphothreonineBy similarity
Modified residuei557 – 5571PhosphoserineBy similarity
Modified residuei565 – 5651PhosphoserineBy similarity
Modified residuei568 – 5681PhosphoserineBy similarity
Modified residuei584 – 5841PhosphoserineBy similarity
Modified residuei586 – 5861PhosphothreonineBy similarity
Modified residuei591 – 5911PhosphoserineBy similarity
Modified residuei593 – 5931PhosphoserineBy similarity
Modified residuei599 – 5991PhosphoserineBy similarity
Modified residuei628 – 6281PhosphothreonineBy similarity
Modified residuei634 – 6341PhosphoserineBy similarity
Modified residuei636 – 6361PhosphoserineBy similarity
Modified residuei637 – 6371PhosphoserineBy similarity
Modified residuei638 – 6381PhosphoserineBy similarity
Modified residuei640 – 6401PhosphothreonineBy similarity
Modified residuei649 – 6491PhosphoserineBy similarity
Modified residuei661 – 6611PhosphoserineBy similarity
Modified residuei667 – 6671PhosphoserineBy similarity
Modified residuei668 – 6681PhosphoserineBy similarity
Modified residuei687 – 6871PhosphoserineBy similarity
Modified residuei690 – 6901PhosphoserineBy similarity
Modified residuei691 – 6911PhosphoserineBy similarity
Modified residuei727 – 7271PhosphoserineBy similarity
Modified residuei733 – 7331PhosphoserineBy similarity
Modified residuei756 – 7561PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9ESL4.
PaxDbiQ9ESL4.
PRIDEiQ9ESL4.

PTM databases

PhosphoSiteiQ9ESL4.

Expressioni

Gene expression databases

BgeeiQ9ESL4.
CleanExiMM_B230120H23RIK.
ExpressionAtlasiQ9ESL4. baseline and differential.
GenevestigatoriQ9ESL4.

Interactioni

Subunit structurei

Homodimer. Interacts with PKN1 and ZNF33A (By similarity).By similarity

Protein-protein interaction databases

IntActiQ9ESL4. 1 interaction.
MINTiMINT-4129310.
STRINGi10090.ENSMUSP00000088334.

Structurei

3D structure databases

ProteinModelPortaliQ9ESL4.
SMRiQ9ESL4. Positions 9-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 277262Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini339 – 41072SAMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni287 – 30822Leucine-zipperAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118807.
HOGENOMiHOG000231813.
HOVERGENiHBG080445.
InParanoidiQ9ESL4.
KOiK04424.
OMAiLLFYENC.
OrthoDBiEOG7D85VN.
PhylomeDBiQ9ESL4.
TreeFamiTF106505.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q9ESL4-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha

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
MSSLGASFVQ IKFDDLQFFE NCGGGSFGSV YRAKWISQDK EVAVKKLLKI
60 70 80 90 100
EKEAEILSVL SHRNIIQFYG VILEPPNYGI VTEYASLGSL YDYINSNRSE
110 120 130 140 150
EMDMEHIMTW ATDVAKGMHY LHMEAPVKVI HRDLKSRNVV IAADGVLKIC
160 170 180 190 200
DFGASRFHNH TTHMSLVGTF PWMAPEVIQS LPVSETCDTY SYGVVLWEML
210 220 230 240 250
TREVPFKGLE GLQVAWLVVE KNERLTIPSS CPRSFAELLH QCWEADAKKR
260 270 280 290 300
PSFKQIISIL ESMSNDTNLP DQCNSFLHNK AEWRCEIEAT LERLKKLERD
310 320 330 340 350
LSFKEQELKE RERRLKMWEQ KLTEQSNTPL LPSFEIGAWT EDDVYFWVQQ
360 370 380 390 400
LVRKGESSVE MSGYASLFKE NNITGKRLLL LEEEDLKDMG IVSKGHIIHF
410 420 430 440 450
KSAIEKLTHD YLNLFHFPPL IKDSGGEPEE NEEKIVNLEL VFGFHLKPGT
460 470 480 490 500
GPQDCKWKMY MEMDGDEVAI TYIKDVTFNT SLPDAEILKM TKPPFVMEKW
510 520 530 540 550
IVGIAEDQTV ECTVTYENDV RTPKLTKHVH SIQWDRTKPQ DEVKAVQLAI
560 570 580 590 600
QTLFSSSEGN PGSRSDSSAD CQWLDTLRMR QIASHTSLQR SQSNPILGSP
610 620 630 640 650
FFPYFANQDS YAAAVRRTQT PVKYQQITPS INPSRSSSPT QYGLSRNFSS
660 670 680 690 700
LNLSSRDSGF SSLNDSSSER GRYSDRSRNK YYRGSVSLNS SPKGRYGGKS
710 720 730 740 750
QHSTPSRERY SGKFYRLPQS ALNTHQSPDF KRSPNDHDRR VPRTIPGMPL
760 770 780 790 800
HPETASKAGE EESRVSEGGW TKVEYRKKTH RQLSAKTSKE RTRGNYRGRR

NF
Length:802
Mass (Da):91,720
Last modified:March 1, 2001 - v1
Checksum:iD431DF8F312A43CC
GO
Isoform 21 Publication (identifier: Q9ESL4-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     332-454: PSFEIGAWTE...HLKPGTGPQD → LPLSARMSEE...DAENDVDNSE
     455-802: Missing.

Note: Contains a phosphoserine at position 434. Contains a phosphoserine at position 453.By similarity

Show »
Length:454
Mass (Da):51,366
Checksum:i35C2FC0D729D9395
GO
Isoform 3Curated (identifier: Q9ESL4-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     285-289: CEIEA → WVAPA
     290-802: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:289
Mass (Da):32,842
Checksum:i440E5651076A04A4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711P → Q in BAC32371. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei285 – 2895CEIEA → WVAPA in isoform 3. 1 PublicationVSP_051747
Alternative sequencei290 – 802513Missing in isoform 3. 1 PublicationVSP_051748Add
BLAST
Alternative sequencei332 – 454123PSFEI…TGPQD → LPLSARMSEESYFESKTEES NSAEMSCQITAASNGEGHGM NPGLQAMMLMGFGDVFSMNK AGAVLHSGMQINMQAKQNSS KTTCKRRGKKVNMALGFSDF DLSEGDDDDHDGDDAENDVD NSE in isoform 2. 1 PublicationVSP_051745Add
BLAST
Alternative sequencei455 – 802348Missing in isoform 2. 1 PublicationVSP_051746Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049731 mRNA. Translation: BAB16442.1.
AB049732 mRNA. Translation: BAB16443.1.
AK045444 mRNA. Translation: BAC32371.1.
AK132186 mRNA. Translation: BAE21021.1.
BC023718 mRNA. Translation: AAH23718.1.
CCDSiCCDS38143.1. [Q9ESL4-1]
CCDS50605.1. [Q9ESL4-2]
RefSeqiNP_001158263.1. NM_001164791.1. [Q9ESL4-2]
NP_075544.1. NM_023057.5. [Q9ESL4-1]
NP_835185.2. NM_178084.4. [Q9ESL4-3]
XP_006500060.1. XM_006499997.1. [Q9ESL4-1]
UniGeneiMm.304143.
Mm.314618.

Genome annotation databases

EnsembliENSMUST00000090824; ENSMUSP00000088334; ENSMUSG00000004085. [Q9ESL4-1]
ENSMUST00000135469; ENSMUSP00000118983; ENSMUSG00000004085. [Q9ESL4-2]
GeneIDi65964.
KEGGimmu:65964.
UCSCiuc008kbs.2. mouse. [Q9ESL4-3]
uc008kbv.2. mouse. [Q9ESL4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049731 mRNA. Translation: BAB16442.1.
AB049732 mRNA. Translation: BAB16443.1.
AK045444 mRNA. Translation: BAC32371.1.
AK132186 mRNA. Translation: BAE21021.1.
BC023718 mRNA. Translation: AAH23718.1.
CCDSiCCDS38143.1. [Q9ESL4-1]
CCDS50605.1. [Q9ESL4-2]
RefSeqiNP_001158263.1. NM_001164791.1. [Q9ESL4-2]
NP_075544.1. NM_023057.5. [Q9ESL4-1]
NP_835185.2. NM_178084.4. [Q9ESL4-3]
XP_006500060.1. XM_006499997.1. [Q9ESL4-1]
UniGeneiMm.304143.
Mm.314618.

3D structure databases

ProteinModelPortaliQ9ESL4.
SMRiQ9ESL4. Positions 9-325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9ESL4. 1 interaction.
MINTiMINT-4129310.
STRINGi10090.ENSMUSP00000088334.

PTM databases

PhosphoSiteiQ9ESL4.

Proteomic databases

MaxQBiQ9ESL4.
PaxDbiQ9ESL4.
PRIDEiQ9ESL4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000090824; ENSMUSP00000088334; ENSMUSG00000004085. [Q9ESL4-1]
ENSMUST00000135469; ENSMUSP00000118983; ENSMUSG00000004085. [Q9ESL4-2]
GeneIDi65964.
KEGGimmu:65964.
UCSCiuc008kbs.2. mouse. [Q9ESL4-3]
uc008kbv.2. mouse. [Q9ESL4-1]

Organism-specific databases

CTDi51776.
MGIiMGI:2443258. Zak.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118807.
HOGENOMiHOG000231813.
HOVERGENiHBG080445.
InParanoidiQ9ESL4.
KOiK04424.
OMAiLLFYENC.
OrthoDBiEOG7D85VN.
PhylomeDBiQ9ESL4.
TreeFamiTF106505.

Miscellaneous databases

NextBioi320398.
PROiQ9ESL4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ESL4.
CleanExiMM_B230120H23RIK.
ExpressionAtlasiQ9ESL4. baseline and differential.
GenevestigatoriQ9ESL4.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a novel MAP kinase kinase kinase, MLTK."
    Gotoh I., Adachi M., Nishida E.
    J. Biol. Chem. 276:4276-4286(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, HOMODIMERIZATION, MUTAGENESIS OF LYS-45.
    Tissue: Heart1 Publication.
  2. "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] (ISOFORMS 1 AND 3).
    Strain: C57BL/6J.
    Tissue: Head.
  3. "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).
    Strain: FVB/NImported.
    Tissue: Mammary glandImported.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 225-233, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  5. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMLTK_MOUSE
AccessioniPrimary (citable) accession number: Q9ESL4
Secondary accession number(s): Q3V1X8, Q8BR73, Q9ESL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: March 1, 2001
Last modified: February 4, 2015
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. 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.