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Q07912

- ACK1_HUMAN

UniProt

Q07912 - ACK1_HUMAN

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Protein
Activated CDC42 kinase 1
Gene
TNK2, ACK1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Non-receptor tyrosine-protein and serine/threonine-protein kinase that is implicated in cell spreading and migration, cell survival, cell growth and proliferation. Transduces extracellular signals to cytosolic and nuclear effectors. Phosphorylates AKT1, AR, MCF2, WASL and WWOX. Implicated in trafficking and clathrin-mediated endocytosis through binding to epidermal growth factor receptor (EGFR) and clathrin. Binds to both poly- and mono-ubiquitin and regulates ligand-induced degradation of EGFR, thereby contributing to the accumulation of EGFR at the limiting membrane of early endosomes. Downstream effector of CDC42 which mediates CDC42-dependent cell migration via phosphorylation of BCAR1. May be involved both in adult synaptic function and plasticity and in brain development. Activates AKT1 by phosphorylating it on 'Tyr-176'. Phosphorylates AR on 'Tyr-267' and 'Tyr-363' thereby promoting its recruitment to androgen-responsive enhancers (AREs). Phosphorylates WWOX on 'Tyr-287'. Phosphorylates MCF2, thereby enhancing its activity as a guanine nucleotide exchange factor (GEF) toward Rho family proteins. Contributes to the control of AXL receptor levels. Confers metastatic properties on cancer cells and promotes tumor growth by negatively regulating tumor suppressor such as WWOX and positively regulating pro-survival factors such as AKT1 and AR.11 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 Publication
ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Magnesium.

Enzyme regulationi

Inhibited by AIM-100 (4-amino-5,6-biaryl-furo[2,3-d]pyrimidine), which suppresses activating phosphorylation at Tyr-284. Repressed by dasatinib.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei158 – 1581ATP
Active sitei252 – 2521Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi132 – 1409ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. GTPase inhibitor activity Source: ProtInc
  3. WW domain binding Source: BHF-UCL
  4. epidermal growth factor receptor binding Source: BHF-UCL
  5. metal ion binding Source: UniProtKB-KW
  6. non-membrane spanning protein tyrosine kinase activity Source: ProtInc
  7. protein binding Source: UniProtKB
  8. protein serine/threonine kinase activity Source: UniProtKB-KW
  9. protein serine/threonine/tyrosine kinase activity Source: UniProtKB
  10. protein tyrosine kinase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cell surface receptor signaling pathway Source: UniProtKB
  2. endocytosis Source: UniProtKB-KW
  3. negative regulation of catalytic activity Source: GOC
  4. peptidyl-tyrosine phosphorylation Source: GOC
  5. phosphorylation Source: UniProtKB
  6. positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  7. regulation of clathrin-mediated endocytosis Source: UniProtKB
  8. small GTPase mediated signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

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

Enzyme and pathway databases

SignaLinkiQ07912.

Names & Taxonomyi

Protein namesi
Recommended name:
Activated CDC42 kinase 1 (EC:2.7.10.2, EC:2.7.11.1)
Short name:
ACK-1
Alternative name(s):
Tyrosine kinase non-receptor protein 2
Gene namesi
Name:TNK2
Synonyms:ACK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:19297. TNK2.

Subcellular locationi

Cell membrane. Nucleus. Endosome. Cell junctionadherens junction By similarity. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicleclathrin-coated vesicle. Membraneclathrin-coated pit
Note: The Tyr-284 phosphorylated form is found both in the membrane and nucleus. Colocalizes with EGFR on endosomes. Nuclear translocation is CDC42-dependent.6 Publications

GO - Cellular componenti

  1. Grb2-EGFR complex Source: BHF-UCL
  2. adherens junction Source: UniProtKB-SubCell
  3. axon Source: Ensembl
  4. clathrin-coated vesicle Source: UniProtKB
  5. coated pit Source: UniProtKB
  6. cytoplasm Source: UniProtKB
  7. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  8. dendrite Source: Ensembl
  9. endosome Source: UniProtKB
  10. growth cone Source: Ensembl
  11. neuronal cell body Source: Ensembl
  12. nucleus Source: UniProtKB
  13. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Coated pit, Cytoplasmic vesicle, Endosome, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi158 – 1581K → R: Loss of autophosphorylation. 1 Publication
Mutagenesisi487 – 4871L → F: Constantly active kinase. 1 Publication

Organism-specific databases

Orphaneti391316. Infantile-onset mesial temporal lobe epilepsy with severe cognitive regression.
PharmGKBiPA134909759.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10381038Activated CDC42 kinase 1
PRO_0000088058Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei284 – 2841Phosphotyrosine; by SRC and autocatalysis8 Publications
Modified residuei518 – 5181Phosphotyrosine1 Publication
Modified residuei724 – 7241Phosphoserine1 Publication
Modified residuei827 – 8271Phosphotyrosine1 Publication
Modified residuei859 – 8591Phosphotyrosine1 Publication
Modified residuei872 – 8721Phosphotyrosine1 Publication
Modified residuei881 – 8811Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylation regulates kinase activity. Phosphorylation on Tyr-518 is required for interaction with SRC and is observed during association with clathrin-coated pits.
Polyubiquitinated by NEDD4 and NEDD4L. Degradation can be induced by EGF and is lysosome-dependent By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ07912.
PaxDbiQ07912.
PRIDEiQ07912.

PTM databases

PhosphoSiteiQ07912.

Expressioni

Tissue specificityi

The Tyr-284 phosphorylated form shows a significant increase in expression in breast cancers during the progressive stages i.e. normal to hyperplasia (ADH), ductal carcinoma in situ (DCIS), invasive ductal carcinoma (IDC) and lymph node metastatic (LNMM) stages. It also shows a significant increase in expression in prostate cancers during the progressive stages.3 Publications

Gene expression databases

ArrayExpressiQ07912.
BgeeiQ07912.
CleanExiHS_TNK2.
GenevestigatoriQ07912.

Organism-specific databases

HPAiCAB009948.
HPA041954.

Interactioni

Subunit structurei

Interacts with NEDD4 (via WW3 domain). NEDD4L and EGF promote association with NEDD4 By similarity. Homodimer. Interacts with AR, CDC42, WWASL and WWOX. Interacts with CSPG4 (activated). Interacts with MERTK (activated); stimulates autophosphorylation. May interact (phosphorylated) with HSP90AB1; maintains kinase activity. Interacts with NPHP1. Interacts with SNX9 (via SH3 domain). Interacts with SRC (via SH2 and SH3 domain). Interacts with EGFR, and this interaction is dependent on EGF stimulation and kinase activity of EGFR. Interacts (via kinase domain) with AKT1. Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with BCAR1/p130cas via SH3 domains. Forms complexes with GRB2 and numerous receptor tyrosine kinases (RTK) including LTK, AXL or PDGFRL, in which GRB2 promotes RTK recruitment by TNK2.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAR1P569455EBI-603457,EBI-702093
CDC42P60953-22EBI-603457,EBI-287394

Protein-protein interaction databases

BioGridi115485. 50 interactions.
DIPiDIP-33858N.
IntActiQ07912. 19 interactions.
MINTiMINT-1382124.
STRINGi9606.ENSP00000371341.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi118 – 1203
Helixi123 – 1253
Beta strandi126 – 1338
Beta strandi140 – 1467
Beta strandi148 – 1503
Beta strandi152 – 1598
Turni163 – 1653
Helixi171 – 18111
Beta strandi192 – 1965
Beta strandi198 – 2003
Beta strandi202 – 2065
Helixi213 – 2197
Helixi221 – 2233
Helixi226 – 24520
Helixi255 – 2573
Beta strandi258 – 2625
Beta strandi265 – 2684
Helixi273 – 2764
Beta strandi283 – 2853
Helixi288 – 2903
Helixi294 – 2963
Helixi299 – 3046
Beta strandi306 – 3083
Helixi309 – 32416
Turni325 – 3273
Turni330 – 3334
Helixi336 – 3449
Helixi358 – 36710
Helixi372 – 3743
Helixi378 – 38710
Beta strandi392 – 3943
Beta strandi402 – 4043
Beta strandi412 – 4176
Beta strandi419 – 4213
Beta strandi423 – 43210
Beta strandi435 – 4395
Helixi440 – 4434
Beta strandi449 – 4513
Turni484 – 4863

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CF4NMR-B448-489[»]
1U46X-ray2.00A/B109-395[»]
1U4DX-ray2.10A/B109-395[»]
1U54X-ray2.80A/B109-395[»]
3EQPX-ray2.30A/B117-392[»]
3EQRX-ray2.00A/B117-392[»]
4EWHX-ray2.50A/B117-391[»]
4HZRX-ray1.31A/B115-389[»]
4HZSX-ray3.23A/B/C/D115-453[»]
4ID7X-ray3.00A117-389[»]
ProteinModelPortaliQ07912.
SMRiQ07912. Positions 81-489.

Miscellaneous databases

EvolutionaryTraceiQ07912.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini126 – 385260Protein kinase
Add
BLAST
Domaini386 – 44863SH3
Add
BLAST
Domaini454 – 46613CRIB
Add
BLAST
Domaini958 – 99639UBA
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 110110SAM-like domain
Add
BLAST
Regioni623 – 65230Required for interaction with SRC
Add
BLAST
Regioni632 – 6354Required for interaction with NEDD4 By similarity
Regioni733 – 876144EBD domain By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi577 – 958382Pro-rich
Add
BLAST

Domaini

The EBD (EGFR-binding domain) domain is necessary for interaction with EGFR By similarity.1 Publication
The SAM-like domain is necessary for NEDD4-mediated ubiquitination. Promotes membrane localization and dimerization to allow for autophosphorylation.1 Publication
The UBA domain binds both poly- and mono-ubiquitin.1 Publication

Sequence similaritiesi

Contains 1 CRIB domain.
Contains 1 SH3 domain.
Contains 1 UBA domain.

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000168225.
HOVERGENiHBG100429.
KOiK08886.
OMAiVRPMPQA.
OrthoDBiEOG71G9T3.
PhylomeDBiQ07912.
TreeFamiTF316643.

Family and domain databases

Gene3Di4.10.680.10. 1 hit.
InterProiIPR015116. Cdc42_binding_dom_like.
IPR021619. Inhibitor_Mig-6.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF09027. GTPase_binding. 1 hit.
PF11555. Inhibitor_Mig-6. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q07912-1) [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

MQPEEGTGWL LELLSEVQLQ QYFLRLRDDL NVTRLSHFEY VKNEDLEKIG     50
MGRPGQRRLW EAVKRRKALC KRKSWMSKVF SGKRLEAEFP PHHSQSTFRK 100
TSPAPGGPAG EGPLQSLTCL IGEKDLRLLE KLGDGSFGVV RRGEWDAPSG 150
KTVSVAVKCL KPDVLSQPEA MDDFIREVNA MHSLDHRNLI RLYGVVLTPP 200
MKMVTELAPL GSLLDRLRKH QGHFLLGTLS RYAVQVAEGM GYLESKRFIH 250
RDLAARNLLL ATRDLVKIGD FGLMRALPQN DDHYVMQEHR KVPFAWCAPE 300
SLKTRTFSHA SDTWMFGVTL WEMFTYGQEP WIGLNGSQIL HKIDKEGERL 350
PRPEDCPQDI YNVMVQCWAH KPEDRPTFVA LRDFLLEAQP TDMRALQDFE 400
EPDKLHIQMN DVITVIEGRA ENYWWRGQNT RTLCVGPFPR NVVTSVAGLS 450
AQDISQPLQN SFIHTGHGDS DPRHCWGFPD RIDELYLGNP MDPPDLLSVE 500
LSTSRPPQHL GGVKKPTYDP VSEDQDPLSS DFKRLGLRKP GLPRGLWLAK 550
PSARVPGTKA SRGSGAEVTL IDFGEEPVVP ALRPCAPSLA QLAMDACSLL 600
DETPPQSPTR ALPRPLHPTP VVDWDARPLP PPPAYDDVAQ DEDDFEICSI 650
NSTLVGAGVP AGPSQGQTNY AFVPEQARPP PPLEDNLFLP PQGGGKPPSS 700
AQTAEIFQAL QQECMRQLQA PAGSPAPSPS PGGDDKPQVP PRVPIPPRPT 750
RPHVQLSPAP PGEEETSQWP GPASPPRVPP REPLSPQGSR TPSPLVPPGS 800
SPLPPRLSSS PGKTMPTTQS FASDPKYATP QVIQAPGPRA GPCILPIVRD 850
GKKVSSTHYY LLPERPSYLE RYQRFLREAQ SPEEPTPLPV PLLLPPPSTP 900
APAAPTATVR PMPQAALDPK ANFSTNNSNP GARPPPPRAT ARLPQRGCPG 950
DGPEAGRPAD KIQMAMVHGV TTEECQAALQ CHGWSVQRAA QYLKVEQLFG 1000
LGLRPRGECH KVLEMFDWNL EQAGCHLLGS WGPAHHKR 1038
Length:1,038
Mass (Da):114,569
Last modified:May 5, 2009 - v3
Checksum:i74A1980665BC3E6B
GO
Isoform 2 (identifier: Q07912-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     485-528: LYLGNPMDPP...DPVSEDQDPL → CPFSAFSPGH...HPVSSRTKGL
     529-1038: Missing.

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:528
Mass (Da):60,062
Checksum:i6CE378AE9D186C20
GO
Isoform 3 (identifier: Q07912-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLEARPPRTQGSDAAGAAAGRGLRALLLSLTAAAGIWGSMGERSAYQRLAGGEEGPQRLGGGRM
     514-514: K → KREPPPRPPQPAFFTQ
     965-994: Missing.

Note: No experimental confirmation available.

Show »
Length:1,086
Mass (Da):119,349
Checksum:i6FC37F9EFDF69D5E
GO

Sequence cautioni

The sequence AAH08884.1 differs from that shown. Reason: Unlikely isoform. Aberrant splice sites.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341R → L in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_032792
Natural varianti71 – 711K → R.1 Publication
Corresponds to variant rs56036945 [ dbSNP | Ensembl ].
VAR_032793
Natural varianti99 – 991R → Q in an ovarian mucinous carcinoma sample; somatic mutation; undergoes autoactivation and causes phosphorylation on Tyr-284 leading to activation of AKT1. 1 Publication
VAR_032794
Natural varianti99 – 991R → W.1 Publication
Corresponds to variant rs3747673 [ dbSNP | Ensembl ].
VAR_032795
Natural varianti152 – 1521T → M.1 Publication
Corresponds to variant rs56161912 [ dbSNP | Ensembl ].
VAR_032796
Natural varianti346 – 3461E → K in an ovarian endometrioid cancer sample; somatic mutation. 2 Publications
VAR_032797
Natural varianti409 – 4091M → I in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_032798
Natural varianti507 – 5071P → S.1 Publication
Corresponds to variant rs35759128 [ dbSNP | Ensembl ].
VAR_032799
Natural varianti725 – 7251P → L.2 Publications
Corresponds to variant rs56260729 [ dbSNP | Ensembl ].
VAR_032800
Natural varianti748 – 7481R → Q.1 Publication
Corresponds to variant rs57872314 [ dbSNP | Ensembl ].
VAR_032801
Natural varianti802 – 8021P → L.
Corresponds to variant rs3749333 [ dbSNP | Ensembl ].
VAR_057115
Natural varianti1038 – 10381R → H.1 Publication
Corresponds to variant rs13433937 [ dbSNP | Ensembl ].
VAR_032802

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MLEARPPRTQGSDAAGAAAG RGLRALLLSLTAAAGIWGSM GERSAYQRLAGGEEGPQRLG GGRM in isoform 3.
VSP_037284
Alternative sequencei485 – 52844LYLGN…DQDPL → CPFSAFSPGHPPAETCGQVL WTGRREACASDPRLHPVSSR TKGL in isoform 2.
VSP_008655Add
BLAST
Alternative sequencei514 – 5141K → KREPPPRPPQPAFFTQ in isoform 3.
VSP_037285
Alternative sequencei529 – 1038510Missing in isoform 2.
VSP_008656Add
BLAST
Alternative sequencei965 – 99430Missing in isoform 3.
VSP_037286Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381G → V in AAH08884. 1 Publication
Sequence conflicti304 – 35249TRTFS…ERLPR → PPWRDISASSSTQFPHAVPC FPTSLLAKLLLRHSVPASSR EIKLVSILC in AAH08884. 1 Publication
Add
BLAST
Sequence conflicti353 – 1038686Missing in AAH08884. 1 Publication
Add
BLAST
Sequence conflicti586 – 5861A → P in AAA53570. 1 Publication
Sequence conflicti722 – 7221Missing in AAA53570. 1 Publication
Sequence conflicti838 – 8403PRA → AG in AAA53570. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L13738 mRNA. Translation: AAA53570.2.
AK131539 mRNA. Translation: BAD18675.1.
AC124944 Genomic DNA. No translation available.
BC008884 mRNA. Translation: AAH08884.1. Sequence problems.
BC028164 mRNA. Translation: AAH28164.1.
CCDSiCCDS33927.1. [Q07912-3]
CCDS33928.1. [Q07912-1]
PIRiS33596.
RefSeqiNP_001010938.1. NM_001010938.1. [Q07912-3]
NP_005772.3. NM_005781.4. [Q07912-1]
UniGeneiHs.518513.

Genome annotation databases

EnsembliENST00000316664; ENSP00000323216; ENSG00000061938. [Q07912-2]
ENST00000333602; ENSP00000329425; ENSG00000061938. [Q07912-1]
ENST00000381916; ENSP00000371341; ENSG00000061938. [Q07912-3]
ENST00000392400; ENSP00000376201; ENSG00000061938. [Q07912-1]
ENST00000439230; ENSP00000395588; ENSG00000061938. [Q07912-2]
GeneIDi10188.
KEGGihsa:10188.
UCSCiuc003fvt.1. human. [Q07912-3]
uc003fvu.1. human. [Q07912-1]

Polymorphism databases

DMDMi229462980.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

CGP resequencing studies

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L13738 mRNA. Translation: AAA53570.2 .
AK131539 mRNA. Translation: BAD18675.1 .
AC124944 Genomic DNA. No translation available.
BC008884 mRNA. Translation: AAH08884.1 . Sequence problems.
BC028164 mRNA. Translation: AAH28164.1 .
CCDSi CCDS33927.1. [Q07912-3 ]
CCDS33928.1. [Q07912-1 ]
PIRi S33596.
RefSeqi NP_001010938.1. NM_001010938.1. [Q07912-3 ]
NP_005772.3. NM_005781.4. [Q07912-1 ]
UniGenei Hs.518513.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CF4 NMR - B 448-489 [» ]
1U46 X-ray 2.00 A/B 109-395 [» ]
1U4D X-ray 2.10 A/B 109-395 [» ]
1U54 X-ray 2.80 A/B 109-395 [» ]
3EQP X-ray 2.30 A/B 117-392 [» ]
3EQR X-ray 2.00 A/B 117-392 [» ]
4EWH X-ray 2.50 A/B 117-391 [» ]
4HZR X-ray 1.31 A/B 115-389 [» ]
4HZS X-ray 3.23 A/B/C/D 115-453 [» ]
4ID7 X-ray 3.00 A 117-389 [» ]
ProteinModelPortali Q07912.
SMRi Q07912. Positions 81-489.
ModBasei Search...

Protein-protein interaction databases

BioGridi 115485. 50 interactions.
DIPi DIP-33858N.
IntActi Q07912. 19 interactions.
MINTi MINT-1382124.
STRINGi 9606.ENSP00000371341.

Chemistry

BindingDBi Q07912.
ChEMBLi CHEMBL4599.
DrugBanki DB00171. Adenosine triphosphate.
GuidetoPHARMACOLOGYi 2246.

PTM databases

PhosphoSitei Q07912.

Polymorphism databases

DMDMi 229462980.

Proteomic databases

MaxQBi Q07912.
PaxDbi Q07912.
PRIDEi Q07912.

Protocols and materials databases

DNASUi 10188.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000316664 ; ENSP00000323216 ; ENSG00000061938 . [Q07912-2 ]
ENST00000333602 ; ENSP00000329425 ; ENSG00000061938 . [Q07912-1 ]
ENST00000381916 ; ENSP00000371341 ; ENSG00000061938 . [Q07912-3 ]
ENST00000392400 ; ENSP00000376201 ; ENSG00000061938 . [Q07912-1 ]
ENST00000439230 ; ENSP00000395588 ; ENSG00000061938 . [Q07912-2 ]
GeneIDi 10188.
KEGGi hsa:10188.
UCSCi uc003fvt.1. human. [Q07912-3 ]
uc003fvu.1. human. [Q07912-1 ]

Organism-specific databases

CTDi 10188.
GeneCardsi GC03M195590.
H-InvDB HIX0003961.
HGNCi HGNC:19297. TNK2.
HPAi CAB009948.
HPA041954.
MIMi 606994. gene.
neXtProti NX_Q07912.
Orphaneti 391316. Infantile-onset mesial temporal lobe epilepsy with severe cognitive regression.
PharmGKBi PA134909759.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000168225.
HOVERGENi HBG100429.
KOi K08886.
OMAi VRPMPQA.
OrthoDBi EOG71G9T3.
PhylomeDBi Q07912.
TreeFami TF316643.

Enzyme and pathway databases

SignaLinki Q07912.

Miscellaneous databases

ChiTaRSi TNK2. human.
EvolutionaryTracei Q07912.
GeneWikii TNK2.
GenomeRNAii 10188.
NextBioi 38556.
PROi Q07912.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q07912.
Bgeei Q07912.
CleanExi HS_TNK2.
Genevestigatori Q07912.

Family and domain databases

Gene3Di 4.10.680.10. 1 hit.
InterProi IPR015116. Cdc42_binding_dom_like.
IPR021619. Inhibitor_Mig-6.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view ]
Pfami PF09027. GTPase_binding. 1 hit.
PF11555. Inhibitor_Mig-6. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
PRINTSi PR00109. TYRKINASE.
SMARTi SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A non-receptor tyrosine kinase that inhibits the GTPase activity of p21cdc42."
    Manser E., Leung T., Salihuddin H., Tan L., Lim L.
    Nature 363:364-367(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CDC42.
    Tissue: Hippocampus.
  2. "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 3), VARIANT LEU-725.
    Tissue: Brain.
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain and Uterus.
  5. "Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas."
    Eisenmann K.M., McCarthy J.B., Simpson M.A., Keely P.J., Guan J.-L., Tachibana K., Lim L., Manser E., Furcht L.T., Iida J.
    Nat. Cell Biol. 1:507-513(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSPG4.
  6. "Activation of the guanine nucleotide exchange factor Dbl following ACK1-dependent tyrosine phosphorylation."
    Kato J., Kaziro Y., Satoh T.
    Biochem. Biophys. Res. Commun. 268:141-147(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS MCF2 KINASE.
  7. "The tyrosine kinase ACK1 associates with clathrin-coated vesicles through a binding motif shared by arrestin and other adaptors."
    Teo M., Tan L., Lim L., Manser E.
    J. Biol. Chem. 276:18392-18398(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: SUBCELLULAR LOCATION.
  9. "Activated tyrosine kinase Ack1 promotes prostate tumorigenesis: role of Ack1 in polyubiquitination of tumor suppressor Wwox."
    Mahajan N.P., Whang Y.E., Mohler J.L., Earp H.S.
    Cancer Res. 65:10514-10523(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION, INTERACTION WITH HSP90AB1; MTERK AND WWOX, MUTAGENESIS OF LYS-158 AND LEU-487.
  10. "SNX9 as an adaptor for linking synaptojanin-1 to the Cdc42 effector ACK1."
    Yeow-Fong L., Lim L., Manser E.
    FEBS Lett. 579:5040-5048(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX9, SUBCELLULAR LOCATION.
  11. "Phosphorylation of WASP by the Cdc42-associated kinase ACK1: dual hydroxyamino acid specificity in a tyrosine kinase."
    Yokoyama N., Lougheed J., Miller W.T.
    J. Biol. Chem. 280:42219-42226(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS WAS KINASE, INTERACTION WITH WASL.
  12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: FUNCTION, TISSUE SPECIFICITY.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Ack1 mediates Cdc42-dependent cell migration and signaling to p130Cas."
    Modzelewska K., Newman L.P., Desai R., Keely P.J.
    J. Biol. Chem. 281:37527-37535(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH BCAR1; CDC42 AND CRK.
  16. "Purification and enzyme activity of ACK1."
    Yokoyama N., Miller W.T.
    Methods Enzymol. 406:250-260(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOPHOSPHORYLATION AT TYR-284.
  17. "Activated Cdc42-associated kinase Ack1 promotes prostate cancer progression via androgen receptor tyrosine phosphorylation."
    Mahajan N.P., Liu Y., Majumder S., Warren M.R., Parker C.E., Mohler J.L., Earp H.S., Whang Y.E.
    Proc. Natl. Acad. Sci. U.S.A. 104:8438-8443(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AR.
  18. "Nephrocystin-1 interacts directly with Ack1 and is expressed in human collecting duct."
    Eley L., Moochhala S.H., Simms R., Hildebrandt F., Sayer J.A.
    Biochem. Biophys. Res. Commun. 371:877-882(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NPHP1.
  19. "TNK2 preserves epidermal growth factor receptor expression on the cell surface and enhances migration and invasion of human breast cancer cells."
    Howlin J., Rosenkvist J., Andersson T.
    Breast Cancer Res. 10:R36-R36(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Dysregulation of Ack1 inhibits down-regulation of the EGF receptor."
    Groevdal L.M., Johannessen L.E., Roedland M.S., Madshus I.H., Stang E.
    Exp. Cell Res. 314:1292-1300(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  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-881, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "Down-regulation of active ACK1 is mediated by association with the E3 ubiquitin ligase Nedd4-2."
    Chan W., Tian R., Lee Y.-F., Sit S.T., Lim L., Manser E.
    J. Biol. Chem. 284:8185-8194(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEDD4, UBIQUITINATION.
  24. "Cytoplasmic ACK1 interaction with multiple receptor tyrosine kinases is mediated by Grb2: an analysis of ACK1 effects on Axl signaling."
    Pao-Chun L., Chan P.M., Chan W., Manser E.
    J. Biol. Chem. 284:34954-34963(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AXL; LTK; PDGFRL AND GRB2.
  25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-284 AND SER-724, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Regulation of Ack1 localization and activity by the amino-terminal SAM domain."
    Prieto-Echaguee V., Gucwa A., Brown D.A., Miller W.T.
    BMC Biochem. 11:42-42(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-284, DOMAIN SAM-LIKE.
  27. "Dasatinib inhibits site-specific tyrosine phosphorylation of androgen receptor by Ack1 and Src kinases."
    Liu Y., Karaca M., Zhang Z., Gioeli D., Earp H.S., Whang Y.E.
    Oncogene 29:3208-3216(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AR KINASE, ENZYME REGULATION.
  28. Cited for: FUNCTION, INTERACTION WITH AKT1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT LYS-346, PHOSPHORYLATION AT TYR-284, TISSUE SPECIFICITY.
  29. "Effect of Ack1 tyrosine kinase inhibitor on ligand-independent androgen receptor activity."
    Mahajan K., Challa S., Coppola D., Lawrence H., Luo Y., Gevariya H., Zhu W., Chen Y.A., Lawrence N.J., Mahajan N.P.
    Prostate 70:1274-1285(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-284, TISSUE SPECIFICITY, ENZYME REGULATION.
  30. "The Cdc42-associated kinase ACK1 is not auto-inhibited but requires Src for activation."
    Chan W., Sit S.T., Manser E.
    Biochem. J. 435:355-364(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-284, INTERACTION WITH SRC.
  31. "Constitutive activated Cdc42-associated kinase (Ack) phosphorylation at arrested endocytic clathrin-coated pits of cells that lack dynamin."
    Shen H., Ferguson S.M., Dephoure N., Park R., Yang Y., Volpicelli-Daley L., Gygi S., Schlessinger J., De Camilli P.
    Mol. Biol. Cell 22:493-502(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-284; TYR-518; TYR-827; TYR-859 AND TYR-872.
  32. "Shepherding AKT and androgen receptor by Ack1 tyrosine kinase."
    Mahajan K., Mahajan N.P.
    J. Cell. Physiol. 224:327-333(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON TUMOR GROWTH.
  33. "Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK."
    Mott H.R., Owen D., Nietlispach D., Lowe P.N., Manser E., Lim L., Laue E.D.
    Nature 399:384-388(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 448-489.
  34. "Crystal structures of the phosphorylated and unphosphorylated kinase domains of the Cdc42-associated tyrosine kinase ACK1."
    Lougheed J.C., Chen R.-H., Mak P., Stout T.J.
    J. Biol. Chem. 279:44039-44045(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 107-395, PHOSPHORYLATION AT TYR-284.
  35. "Identification and optimization of N3,N6-diaryl-1H-pyrazolo[3,4-d]pyrimidine-3,6-diamines as a novel class of ACK1 inhibitors."
    Kopecky D.J., Hao X., Chen Y., Fu J., Jiao X., Jaen J.C., Cardozo M.G., Liu J., Wang Z., Walker N.P., Wesche H., Li S., Farrelly E., Xiao S.H., Kayser F.
    Bioorg. Med. Chem. Lett. 18:6352-6356(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 117-392 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY.
  36. "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 LEU-34; ARG-71; GLN-99; TRP-99; MET-152; LYS-346; ILE-409; SER-507; LEU-725; GLN-748 AND HIS-1038.

Entry informationi

Entry nameiACK1_HUMAN
AccessioniPrimary (citable) accession number: Q07912
Secondary accession number(s): Q6ZMQ0, Q8N6U7, Q96H59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 152 of the entry and version 3 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 3
    Human chromosome 3: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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