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Q7KZI7

- MARK2_HUMAN

UniProt

Q7KZI7 - MARK2_HUMAN

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Protein

Serine/threonine-protein kinase MARK2

Gene

MARK2

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

Functioni

Serine/threonine-protein kinase involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4, MAPT/TAU, and RAB11FIP2. Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells.10 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication
ATP + [tau protein] = ADP + [tau protein] phosphate.

Cofactori

Magnesium.By similarity

Enzyme regulationi

Inhibited by PAK7/PAK5; inhibition is independent of the kinase activity of PAK7/PAK5 By similarity. Activated by phosphorylation on Thr-208. Inhibited by phosphorylation at Ser-212 and Thr-596. Inhibited by hymenialdisine. Specifically inhibited by the H.pylori CagA peptide FPLKRHDKVDDLSK that mimics host substrates and binds to the kinase substrate-binding site.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821ATPBy similarityPROSITE-ProRule annotation
Active sitei175 – 1751Proton acceptorBy similarityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi59 – 679ATPBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. lipid binding Source: UniProtKB-KW
  3. magnesium ion binding Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB
  5. protein kinase activator activity Source: ParkinsonsUK-UCL
  6. protein serine/threonine kinase activity Source: UniProtKB
  7. tau-protein kinase activity Source: UniProtKB

GO - Biological processi

  1. activation of protein kinase activity Source: ParkinsonsUK-UCL
  2. establishment of cell polarity Source: UniProtKB
  3. establishment or maintenance of epithelial cell apical/basal polarity Source: UniProtKB
  4. intracellular signal transduction Source: UniProtKB
  5. mitochondrion degradation Source: ParkinsonsUK-UCL
  6. mitochondrion localization Source: ParkinsonsUK-UCL
  7. neuron migration Source: UniProtKB
  8. peptidyl-threonine phosphorylation Source: ParkinsonsUK-UCL
  9. positive regulation of neuron projection development Source: UniProtKB
  10. protein autophosphorylation Source: UniProtKB
  11. protein phosphorylation Source: UniProtKB
  12. regulation of axonogenesis Source: UniProtKB
  13. regulation of cytoskeleton organization Source: UniProtKB
  14. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Differentiation, Wnt signaling pathway

Keywords - Ligandi

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

Enzyme and pathway databases

SignaLinkiQ7KZI7.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase MARK2 (EC:2.7.11.1, EC:2.7.11.26)
Alternative name(s):
ELKL motif kinase 1
Short name:
EMK-1
MAP/microtubule affinity-regulating kinase 2
PAR1 homolog
PAR1 homolog b
Short name:
Par-1b
Short name:
Par1b
Gene namesi
Name:MARK2Imported
Synonyms:EMK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:3332. MARK2.

Subcellular locationi

Cell membrane; Peripheral membrane protein. Cytoplasm. Lateral cell membrane. Cytoplasmcytoskeleton
Note: Phosphorylation at Thr-596 by PRKCZ/aPKC and subsequent interaction with 14-3-3 protein YWHAZ promotes relocation from the cell membrane to the cytoplasm.

GO - Cellular componenti

  1. actin filament Source: UniProtKB
  2. basal cortex Source: Ensembl
  3. lateral plasma membrane Source: UniProtKB
  4. membrane Source: UniProtKB
  5. microtubule bundle Source: UniProtKB
  6. mitochondrion Source: ParkinsonsUK-UCL
  7. nucleus Source: Ensembl
  8. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi208 – 2081T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. 1 Publication
Mutagenesisi596 – 5961T → A: Loss of membrane dissociation and binding to YWHAZ. 2 Publications

Organism-specific databases

PharmGKBiPA35047.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 788788Serine/threonine-protein kinase MARK2PRO_0000086301Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401Phosphoserine1 Publication
Modified residuei58 – 581Phosphothreonine; by autocatalysisBy similarity
Modified residuei91 – 911Phosphoserine; by CaMK1By similarity
Modified residuei92 – 921Phosphoserine; by CaMK1By similarity
Modified residuei93 – 931Phosphoserine; by CaMK1By similarity
Modified residuei208 – 2081Phosphothreonine; by LKB1 and TAOK12 Publications
Modified residuei212 – 2121Phosphoserine; by GSK3-betaBy similarity
Modified residuei274 – 2741Phosphoserine; by autocatalysisBy similarity
Modified residuei275 – 2751Phosphothreonine; by autocatalysisBy similarity
Modified residuei294 – 2941Phosphothreonine; by CaMK1By similarity
Modified residuei409 – 4091Phosphoserine2 Publications
Modified residuei456 – 4561Phosphoserine5 Publications
Modified residuei486 – 4861Phosphoserine5 Publications
Modified residuei493 – 4931Phosphoserine1 Publication
Modified residuei569 – 5691Phosphoserine1 Publication
Modified residuei596 – 5961Phosphothreonine; by PKC/PRKCZ2 Publications
Modified residuei619 – 6191Phosphoserine1 Publication
Modified residuei722 – 7221Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylated. Phosphorylated at Thr-208 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-208 by TAOK1 activates the kinase activity, leading to phosphorylation and detachment of MAPT/TAU from microtubules. Phosphorylation at Ser-212 by GSK3-beta (GSK3B) inhibits the kinase activity. Phosphorylation by CaMK1 promotes activity and is required to promote neurite outgrowth. Phosphorylation at Thr-596 by PRKCZ/aPKC in polarized epithelial cells inhibits the kinase activity and promotes binding to 14-3-3 protein YWHAZ, leading to relocation from cell membrane to cytoplasm.11 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ7KZI7.
PaxDbiQ7KZI7.
PRIDEiQ7KZI7.

PTM databases

PhosphoSiteiQ7KZI7.

Expressioni

Tissue specificityi

High levels of expression in heart, brain, skeletal muscle and pancreas, lower levels observed in lung, liver and kidney.1 Publication

Gene expression databases

BgeeiQ7KZI7.
CleanExiHS_MARK2.
ExpressionAtlasiQ7KZI7. baseline and differential.
GenevestigatoriQ7KZI7.

Organism-specific databases

HPAiHPA038790.

Interactioni

Subunit structurei

Homodimer. Interacts with PAK7/PAK5; leading to inhibit the protein kinase activity By similarity. Interacts with MTCL1 isoform 1; the interaction is direct and increases MARK2 microtubule-binding ability. Interacts (when phosphorylated at Thr-596) with YWHAZ. In case of infection, interacts with H.pylori CagA, leading to inhibit kinase activity and junctional and polarity defects.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PARD6GQ9BYG42EBI-516560,EBI-295417
YWHABP319463EBI-516560,EBI-359815
YWHAGP619812EBI-516560,EBI-359832
YWHAHQ049178EBI-516560,EBI-306940
YWHAZP631046EBI-516560,EBI-347088

Protein-protein interaction databases

BioGridi108326. 60 interactions.
DIPiDIP-31321N.
IntActiQ7KZI7. 34 interactions.
MINTiMINT-1149196.
STRINGi9606.ENSP00000389184.

Structurei

Secondary structure

1
788
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi53 – 608
Beta strandi66 – 727
Turni73 – 753
Beta strandi78 – 869
Helixi91 – 10616
Beta strandi115 – 1206
Beta strandi122 – 1298
Helixi137 – 1448
Helixi149 – 16820
Helixi178 – 1803
Beta strandi181 – 1833
Beta strandi189 – 1913
Helixi213 – 2153
Helixi218 – 2214
Helixi228 – 24518
Helixi255 – 26410
Helixi275 – 28410
Helixi289 – 2913
Helixi295 – 2995
Helixi302 – 3054
Helixi326 – 3349
Helixi339 – 3479
Helixi353 – 3619

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IECX-ray2.20A/B/C/D49-363[»]
ProteinModelPortaliQ7KZI7.
SMRiQ7KZI7. Positions 19-363, 689-788.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7KZI7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 304252Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini323 – 36240UBAPROSITE-ProRule annotationAdd
BLAST
Domaini739 – 78850KA1PROSITE-ProRule annotationAdd
BLAST

Domaini

The UBA domain does not seem to bind ubiquitin and ubiquitin-like and might play a role in regulating the enzyme conformation and localization. Activation of the kinase activity following phosphorylation at Thr-208 is accompanied by a conformational change that alters the orientation of the UBA domain with respect to the catalytic domain.1 Publication
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
Contains 1 UBA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118892.
HOVERGENiHBG052453.
InParanoidiQ7KZI7.
KOiK08798.
OMAiHERYMLL.
OrthoDBiEOG79CXXX.
PhylomeDBiQ7KZI7.
TreeFamiTF315213.

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.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]
PfamiPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
SM00165. UBA. 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.
PS50030. UBA. 1 hit.
[Graphical view]

Sequences (16)i

Sequence statusi: Complete.

This entry describes 16 isoformsi produced by alternative promoter usage and alternative splicing. Align

Isoform 1Curated (identifier: Q7KZI7-1) [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
MSSARTPLPT LNERDTEQPT LGHLDSKPSS KSNMIRGRNS ATSADEQPHI
60 70 80 90 100
GNYRLLKTIG KGNFAKVKLA RHILTGKEVA VKIIDKTQLN SSSLQKLFRE
110 120 130 140 150
VRIMKVLNHP NIVKLFEVIE TEKTLYLVME YASGGEVFDY LVAHGRMKEK
160 170 180 190 200
EARAKFRQIV SAVQYCHQKF IVHRDLKAEN LLLDADMNIK IADFGFSNEF
210 220 230 240 250
TFGNKLDTFC GSPPYAAPEL FQGKKYDGPE VDVWSLGVIL YTLVSGSLPF
260 270 280 290 300
DGQNLKELRE RVLRGKYRIP FYMSTDCENL LKKFLILNPS KRGTLEQIMK
310 320 330 340 350
DRWMNVGHED DELKPYVEPL PDYKDPRRTE LMVSMGYTRE EIQDSLVGQR
360 370 380 390 400
YNEVMATYLL LGYKSSELEG DTITLKPRPS ADLTNSSAPS PSHKVQRSVS
410 420 430 440 450
ANPKQRRFSD QAAGPAIPTS NSYSKKTQSN NAENKRPEED RESGRKASST
460 470 480 490 500
AKVPASPLPG LERKKTTPTP STNSVLSTST NRSRNSPLLE RASLGQASIQ
510 520 530 540 550
NGKDSLTMPG SRASTASASA AVSAARPRQH QKSMSASVHP NKASGLPPTE
560 570 580 590 600
SNCEVPRPST APQRVPVASP SAHNISSSGG APDRTNFPRG VSSRSTFHAG
610 620 630 640 650
QLRQVRDQQN LPYGVTPASP SGHSQGRRGA SGSIFSKFTS KFVRRNLSFR
660 670 680 690 700
FARRNLNEPE SKDRVETLRP HVVGSGGNDK EKEEFREAKP RSLRFTWSMK
710 720 730 740 750
TTSSMEPNEM MREIRKVLDA NSCQSELHEK YMLLCMHGTP GHEDFVQWEM
760 770 780
EVCKLPRLSL NGVRFKRISG TSMAFKNIAS KIANELKL

Note: Produced by alternative promoter usage. No experimental confirmation available.

Length:788
Mass (Da):87,911
Last modified:April 12, 2005 - v2
Checksum:iF307BF4DDB543A70
GO
Isoform 21 Publication (identifier: Q7KZI7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     505-558: Missing.

Note: Produced by alternative splicing of isoform 6.1 Publication

Show »
Length:701
Mass (Da):78,851
Checksum:i3D68318CFDCA31EE
GO
Isoform 31 Publication (identifier: Q7KZI7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     644-652: Missing.

Note: Produced by alternative splicing of isoform 6.1 Publication

Show »
Length:746
Mass (Da):83,184
Checksum:i58F2BBE10943C90F
GO
Isoform 41 Publication (identifier: Q7KZI7-4) [UniParc]FASTAAdd to Basket

Also known as: Par-1Balpha1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     505-558: Missing.
     644-652: Missing.

Note: Produced by alternative splicing of isoform 1.1 Publication

Show »
Length:725
Mass (Da):81,280
Checksum:iD676331938A84716
GO
Isoform 5 (identifier: Q7KZI7-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     505-558: Missing.
     654-668: Missing.

Note: Produced by alternative splicing of isoform 1.

Show »
Length:719
Mass (Da):80,647
Checksum:iEC39154CF73E9858
GO
Isoform 6Curated (identifier: Q7KZI7-6) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.

Note: Produced by alternative promoter usage. No experimental confirmation available.

Show »
Length:755
Mass (Da):84,333
Checksum:i493CD8C6DC3A4C06
GO
Isoform 7Curated (identifier: Q7KZI7-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     505-558: Missing.
     644-652: Missing.

Note: Produced by alternative splicing of isoform 6. No experimental confirmation available.Curated

Show »
Length:692
Mass (Da):77,702
Checksum:i4BD9AA1F872638A6
GO
Isoform 8Curated (identifier: Q7KZI7-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     644-652: Missing.

Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.Curated

Show »
Length:779
Mass (Da):86,762
Checksum:i5AF7014EB5639857
GO
Isoform 9Curated (identifier: Q7KZI7-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     505-558: Missing.

Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.Curated

Show »
Length:734
Mass (Da):82,429
Checksum:i60D126D3C8967186
GO
Isoform 10Curated (identifier: Q7KZI7-10) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     505-558: Missing.
     654-668: Missing.

Note: Produced by alternative splicing of isoform 6. No experimental confirmation available.Curated

Show »
Length:686
Mass (Da):77,069
Checksum:i9389E28076FDDAF8
GO
Isoform 11Curated (identifier: Q7KZI7-11) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     654-668: Missing.

Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.

Show »
Length:773
Mass (Da):86,129
Checksum:i0378FF0433C4D901
GO
Isoform 12Curated (identifier: Q7KZI7-12) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     654-668: Missing.

Note: Produced by alternative splicing of isoform 6. No experimental confirmation available.Curated

Show »
Length:740
Mass (Da):82,551
Checksum:i6220FC8C1A308548
GO
Isoform 13 (identifier: Q7KZI7-13) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     412-412: Missing.
     505-558: Missing.
     644-652: Missing.

Note: Produced by alternative splicing of isoform 6. Contains a phosphoserine at position 376.

Show »
Length:691
Mass (Da):77,631
Checksum:i2216B4AE7BCF31BE
GO
Isoform 14 (identifier: Q7KZI7-14) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     412-412: Missing.
     644-652: Missing.

Note: Produced by alternative splicing of isoform 6. Contains a phosphoserine at position 376.

Show »
Length:745
Mass (Da):83,113
Checksum:i54CA1DAF4B6E02CF
GO
Isoform 15 (identifier: Q7KZI7-15) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     412-412: Missing.
     505-558: Missing.
     645-668: Missing.

Note: Produced by alternative splicing of isoform 1. Contains a phosphoserine at position 409.

Show »
Length:709
Mass (Da):79,427
Checksum:iF30B3AB6B60B3621
GO
Isoform 16 (identifier: Q7KZI7-16) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     412-412: Missing.
     505-558: Missing.
     644-652: Missing.

Note: Produced by alternative splicing of isoform 1. Contains a phosphoserine at position 409.

Show »
Length:724
Mass (Da):81,209
Checksum:i9D8FB211F5B08149
GO

Sequence cautioni

The sequence AAK82368.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1921A → G in CAA80914. (PubMed:8274451)Curated
Sequence conflicti236 – 2361L → C in CAA80914. (PubMed:8274451)Curated
Sequence conflicti389 – 3902PS → QF in CAA66229. (PubMed:9730619)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333Missing in isoform 2, isoform 3, isoform 6, isoform 7, isoform 10, isoform 12, isoform 13 and isoform 14. 2 PublicationsVSP_051705Add
BLAST
Alternative sequencei412 – 4121Missing in isoform 13, isoform 14, isoform 15 and isoform 16. CuratedVSP_039872
Alternative sequencei505 – 55854Missing in isoform 2, isoform 4, isoform 5, isoform 7, isoform 9, isoform 10, isoform 13, isoform 15 and isoform 16. 4 PublicationsVSP_051706Add
BLAST
Alternative sequencei644 – 6529Missing in isoform 3, isoform 4, isoform 7, isoform 8, isoform 13, isoform 14 and isoform 16. 3 PublicationsVSP_051707
Alternative sequencei645 – 66824Missing in isoform 15. CuratedVSP_041853Add
BLAST
Alternative sequencei654 – 66815Missing in isoform 5, isoform 11, isoform 10 and isoform 12. 3 PublicationsVSP_051708Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X97630 mRNA. Translation: CAA66229.1.
AB188493 mRNA. Translation: BAD37141.1.
BT007342 mRNA. Translation: AAP36006.1.
AP003780 Genomic DNA. No translation available.
BC008771 mRNA. Translation: AAH08771.2.
BC084540 mRNA. Translation: AAH84540.1.
AF387638 mRNA. Translation: AAK82368.1. Different initiation.
Z25427 mRNA. Translation: CAA80914.1.
CCDSiCCDS41665.1. [Q7KZI7-14]
CCDS53649.1. [Q7KZI7-1]
CCDS53650.1. [Q7KZI7-5]
CCDS53651.1. [Q7KZI7-15]
CCDS8051.2. [Q7KZI7-16]
PIRiG01025.
I38217.
RefSeqiNP_001034558.2. NM_001039469.2. [Q7KZI7-1]
NP_001156768.1. NM_001163296.1. [Q7KZI7-5]
NP_001156769.1. NM_001163297.1. [Q7KZI7-15]
NP_004945.4. NM_004954.4. [Q7KZI7-16]
NP_059672.2. NM_017490.3. [Q7KZI7-14]
XP_006718504.1. XM_006718441.1. [Q7KZI7-8]
XP_006718506.1. XM_006718443.1. [Q7KZI7-11]
XP_006718509.1. XM_006718446.1. [Q7KZI7-4]
UniGeneiHs.567261.

Genome annotation databases

EnsembliENST00000350490; ENSP00000294247; ENSG00000072518. [Q7KZI7-15]
ENST00000361128; ENSP00000355091; ENSG00000072518. [Q7KZI7-5]
ENST00000402010; ENSP00000385751; ENSG00000072518. [Q7KZI7-1]
ENST00000408948; ENSP00000386128; ENSG00000072518. [Q7KZI7-13]
ENST00000508192; ENSP00000425765; ENSG00000072518. [Q7KZI7-16]
ENST00000509502; ENSP00000423974; ENSG00000072518. [Q7KZI7-14]
ENST00000513765; ENSP00000421075; ENSG00000072518. [Q7KZI7-6]
GeneIDi2011.
KEGGihsa:2011.
UCSCiuc001nxv.4. human. [Q7KZI7-16]
uc001nxw.3. human. [Q7KZI7-1]
uc001nxx.3. human. [Q7KZI7-5]
uc001nxy.3. human. [Q7KZI7-15]
uc001nxz.4. human. [Q7KZI7-14]

Polymorphism databases

DMDMi62510922.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X97630 mRNA. Translation: CAA66229.1 .
AB188493 mRNA. Translation: BAD37141.1 .
BT007342 mRNA. Translation: AAP36006.1 .
AP003780 Genomic DNA. No translation available.
BC008771 mRNA. Translation: AAH08771.2 .
BC084540 mRNA. Translation: AAH84540.1 .
AF387638 mRNA. Translation: AAK82368.1 . Different initiation.
Z25427 mRNA. Translation: CAA80914.1 .
CCDSi CCDS41665.1. [Q7KZI7-14 ]
CCDS53649.1. [Q7KZI7-1 ]
CCDS53650.1. [Q7KZI7-5 ]
CCDS53651.1. [Q7KZI7-15 ]
CCDS8051.2. [Q7KZI7-16 ]
PIRi G01025.
I38217.
RefSeqi NP_001034558.2. NM_001039469.2. [Q7KZI7-1 ]
NP_001156768.1. NM_001163296.1. [Q7KZI7-5 ]
NP_001156769.1. NM_001163297.1. [Q7KZI7-15 ]
NP_004945.4. NM_004954.4. [Q7KZI7-16 ]
NP_059672.2. NM_017490.3. [Q7KZI7-14 ]
XP_006718504.1. XM_006718441.1. [Q7KZI7-8 ]
XP_006718506.1. XM_006718443.1. [Q7KZI7-11 ]
XP_006718509.1. XM_006718446.1. [Q7KZI7-4 ]
UniGenei Hs.567261.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IEC X-ray 2.20 A/B/C/D 49-363 [» ]
ProteinModelPortali Q7KZI7.
SMRi Q7KZI7. Positions 19-363, 689-788.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108326. 60 interactions.
DIPi DIP-31321N.
IntActi Q7KZI7. 34 interactions.
MINTi MINT-1149196.
STRINGi 9606.ENSP00000389184.

Chemistry

BindingDBi Q7KZI7.
ChEMBLi CHEMBL3831.
GuidetoPHARMACOLOGYi 2098.

PTM databases

PhosphoSitei Q7KZI7.

Polymorphism databases

DMDMi 62510922.

Proteomic databases

MaxQBi Q7KZI7.
PaxDbi Q7KZI7.
PRIDEi Q7KZI7.

Protocols and materials databases

DNASUi 2011.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000350490 ; ENSP00000294247 ; ENSG00000072518 . [Q7KZI7-15 ]
ENST00000361128 ; ENSP00000355091 ; ENSG00000072518 . [Q7KZI7-5 ]
ENST00000402010 ; ENSP00000385751 ; ENSG00000072518 . [Q7KZI7-1 ]
ENST00000408948 ; ENSP00000386128 ; ENSG00000072518 . [Q7KZI7-13 ]
ENST00000508192 ; ENSP00000425765 ; ENSG00000072518 . [Q7KZI7-16 ]
ENST00000509502 ; ENSP00000423974 ; ENSG00000072518 . [Q7KZI7-14 ]
ENST00000513765 ; ENSP00000421075 ; ENSG00000072518 . [Q7KZI7-6 ]
GeneIDi 2011.
KEGGi hsa:2011.
UCSCi uc001nxv.4. human. [Q7KZI7-16 ]
uc001nxw.3. human. [Q7KZI7-1 ]
uc001nxx.3. human. [Q7KZI7-5 ]
uc001nxy.3. human. [Q7KZI7-15 ]
uc001nxz.4. human. [Q7KZI7-14 ]

Organism-specific databases

CTDi 2011.
GeneCardsi GC11P063606.
HGNCi HGNC:3332. MARK2.
HPAi HPA038790.
MIMi 600526. gene.
neXtProti NX_Q7KZI7.
PharmGKBi PA35047.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118892.
HOVERGENi HBG052453.
InParanoidi Q7KZI7.
KOi K08798.
OMAi HERYMLL.
OrthoDBi EOG79CXXX.
PhylomeDBi Q7KZI7.
TreeFami TF315213.

Enzyme and pathway databases

SignaLinki Q7KZI7.

Miscellaneous databases

ChiTaRSi MARK2. human.
EvolutionaryTracei Q7KZI7.
GeneWikii MARK2.
GenomeRNAii 2011.
NextBioi 8141.
PROi Q7KZI7.
SOURCEi Search...

Gene expression databases

Bgeei Q7KZI7.
CleanExi HS_MARK2.
ExpressionAtlasi Q7KZI7. baseline and differential.
Genevestigatori Q7KZI7.

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.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view ]
Pfami PF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
SM00165. UBA. 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.
PS50030. UBA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human serine/threonine protein kinase EMK1: genome structure and cDNA cloning of isoforms produced by alternative splicing."
    Espinosa L., Navarro E.
    Cytogenet. Cell Genet. 81:278-282(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY.
    Tissue: ColonImported.
  2. Sugiyama A., Inoue H., Oka M.
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    Tissue: KidneyImported.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-755 (ISOFORM 1).
    Tissue: KidneyImported and PlacentaImported.
  6. "PAR-1 is a Dishevelled-associated kinase and a positive regulator of Wnt signalling."
    Sun T.-Q., Lu B., Feng J.-J., Reinhard C., Jan Y.N., Fantl W.J., Williams L.T.
    Nat. Cell Biol. 3:628-636(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-788 (ISOFORM 4), FUNCTION.
  7. "Identification of 21 novel human protein kinases, including 3 members of a family related to the cell cycle regulator nimA of Aspergillus nidulans."
    Schultz S.J., Nigg E.A.
    Cell Growth Differ. 4:821-830(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 190-237.
  8. "Protein kinase MARK/PAR-1 is required for neurite outgrowth and establishment of neuronal polarity."
    Biernat J., Wu Y.Z., Timm T., Zheng-Fischhofer Q., Mandelkow E., Meijer L., Mandelkow E.M.
    Mol. Biol. Cell 13:4013-4028(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  9. "Splicing alterations in human renal allografts: detection of a new splice variant of protein kinase Par1/Emk1 whose expression is associated with an increase of inflammation in protocol biopsies of transplanted patients."
    Hueso M., Beltran V., Moreso F., Ciriero E., Fulladosa X., Grinyo J.M., Seron D., Navarro E.
    Biochim. Biophys. Acta 1689:58-65(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ALTERNATIVE PROMOTER USAGE.
  10. "LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1."
    Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A., Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G., Alessi D.R.
    EMBO J. 23:833-843(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-208, MUTAGENESIS OF THR-208.
  11. "Par-1 promotes a hepatic mode of apical protein trafficking in MDCK cells."
    Cohen D., Rodriguez-Boulan E., Musch A.
    Proc. Natl. Acad. Sci. U.S.A. 101:13792-13797(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Atypical PKC phosphorylates PAR-1 kinases to regulate localization and activity."
    Hurov J.B., Watkins J.L., Piwnica-Worms H.
    Curr. Biol. 14:736-741(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-596, MUTAGENESIS OF THR-596, SUBCELLULAR LOCATION.
  13. "aPKC acts upstream of PAR-1b in both the establishment and maintenance of mammalian epithelial polarity."
    Suzuki A., Hirata M., Kamimura K., Maniwa R., Yamanaka T., Mizuno K., Kishikawa M., Hirose H., Amano Y., Izumi N., Miwa Y., Ohno S.
    Curr. Biol. 14:1425-1435(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-596, MUTAGENESIS OF THR-596, INTERACTION WITH YWHAZ.
  14. "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-486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "MARK2/EMK1/Par-1Balpha phosphorylation of Rab11-family interacting protein 2 is necessary for the timely establishment of polarity in Madin-Darby canine kidney cells."
    Ducharme N.A., Hales C.M., Lapierre L.A., Ham A.J., Oztan A., Apodaca G., Goldenring J.R.
    Mol. Biol. Cell 17:3625-3637(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RAB11FIP2.
  16. "New role for hPar-1 kinases EMK and C-TAK1 in regulating localization and activity of class IIa histone deacetylases."
    Dequiedt F., Martin M., Von Blume J., Vertommen D., Lecomte E., Mari N., Heinen M.F., Bachmann M., Twizere J.C., Huang M.C., Rider M.H., Piwnica-Worms H., Seufferlein T., Kettmann R.
    Mol. Cell. Biol. 26:7086-7102(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC7.
  17. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Helicobacter pylori CagA targets PAR1/MARK kinase to disrupt epithelial cell polarity."
    Saadat I., Higashi H., Obuse C., Umeda M., Murata-Kamiya N., Saito Y., Lu H., Ohnishi N., Azuma T., Suzuki A., Ohno S., Hatakeyama M.
    Nature 447:330-333(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH H.PYLORI CAGA.
  19. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456 AND SER-486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  21. "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 SER-409; SER-456; SER-486 AND SER-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "Glucose controls CREB activity in islet cells via regulated phosphorylation of TORC2."
    Jansson D., Ng A.C., Fu A., Depatie C., Al Azzabi M., Screaton R.A.
    Proc. Natl. Acad. Sci. U.S.A. 105:10161-10166(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CRTC2.
  23. "The ubiquitin-associated domain of AMPK-related kinases regulates conformation and LKB1-mediated phosphorylation and activation."
    Jaleel M., Villa F., Deak M., Toth R., Prescott A.R., Van Aalten D.M., Alessi D.R.
    Biochem. J. 394:545-555(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN UBA.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376 (ISOFORMS 13 AND 14), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 (ISOFORMS 15 AND 16), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "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].
  26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-208; SER-409; SER-456; SER-486 AND SER-722, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376 (ISOFORMS 13 AND 14), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Par1b/MARK2 phosphorylates kinesin-like motor protein GAKIN/KIF13B to regulate axon formation."
    Yoshimura Y., Terabayashi T., Miki H.
    Mol. Cell. Biol. 30:2206-2219(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF KIF13B.
  28. "The tau of MARK: a polarized view of the cytoskeleton."
    Matenia D., Mandelkow E.M.
    Trends Biochem. Sci. 34:332-342(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  29. "Structure and function of polarity-inducing kinase family MARK/Par-1 within the branch of AMPK/Snf1-related kinases."
    Marx A., Nugoor C., Panneerselvam S., Mandelkow E.
    FASEB J. 24:1637-1648(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  30. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-486 AND SER-619, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "The novel PAR-1-binding protein MTCL1 has crucial roles in organizing microtubules in polarizing epithelial cells."
    Sato Y., Akitsu M., Amano Y., Yamashita K., Ide M., Shimada K., Yamashita A., Hirano H., Arakawa N., Maki T., Hayashi I., Ohno S., Suzuki A.
    J. Cell Sci. 126:4671-4683(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MTCL1, SUBCELLULAR LOCATION.
  34. "Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates."
    Nesic D., Miller M.C., Quinkert Z.T., Stein M., Chait B.T., Stebbins C.E.
    Nat. Struct. Mol. Biol. 17:130-132(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 49-363 IN COMPLEX WITH H.PYLORI CAGA PEPTIDE INHIBITOR.

Entry informationi

Entry nameiMARK2_HUMAN
AccessioniPrimary (citable) accession number: Q7KZI7
Secondary accession number(s): Q15449
, Q15524, Q5XGA3, Q68A18, Q96HB3, Q96RG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: October 29, 2014
This is version 120 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3