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P16333

- NCK1_HUMAN

UniProt

P16333 - NCK1_HUMAN

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Protein

Cytoplasmic protein NCK1

Gene

NCK1

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

Functioni

Adapter protein which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in the DNA damage response, not in the detection of the damage by ATM/ATR, but for efficient activation of downstream effectors, such as that of CHEK2. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. Modulates the activation of EIF2AK2/PKR by dsRNA. May play a role in cell adhesion and migration through interaction with ephrin receptors.6 Publications

GO - Molecular functioni

  1. cytoskeletal adaptor activity Source: UniProtKB
  2. protein kinase inhibitor activity Source: UniProtKB
  3. receptor binding Source: UniProtKB
  4. receptor signaling complex scaffold activity Source: UniProtKB
  5. receptor tyrosine kinase binding Source: UniProtKB

GO - Biological processi

  1. actin filament organization Source: Ensembl
  2. axon guidance Source: Reactome
  3. cell migration Source: Ensembl
  4. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  5. innate immune response Source: Reactome
  6. lamellipodium assembly Source: Ensembl
  7. negative regulation of cell death Source: UniProtKB
  8. negative regulation of protein kinase activity Source: GOC
  9. positive regulation of actin filament polymerization Source: UniProtKB
  10. positive regulation of T cell proliferation Source: UniProtKB
  11. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  12. regulation of translation Source: UniProtKB-KW
  13. response to other organism Source: Ensembl
  14. signal complex assembly Source: UniProtKB
  15. T cell activation Source: UniProtKB
  16. T cell receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Translation regulation

Enzyme and pathway databases

ReactomeiREACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_12623. Generation of second messenger molecules.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_17025. Downstream signal transduction.
REACT_19226. Activation of Rac.
REACT_22351. DCC mediated attractive signaling.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_23832. Nephrin interactions.
SignaLinkiP16333.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic protein NCK1
Alternative name(s):
NCK adaptor protein 1
Short name:
Nck-1
SH2/SH3 adaptor protein NCK-alpha
Gene namesi
Name:NCK1
Synonyms:NCK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:7664. NCK1.

Subcellular locationi

Cytoplasm. Endoplasmic reticulum. Nucleus
Note: Mostly cytoplasmic, but shuttles between the cytoplasm and the nucleus. Import into the nucleus requires the interaction with SOCS7. Predominantly nuclear following genotoxic stresses, such as UV irradiation, hydroxyurea or mitomycin C treatments.

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. endoplasmic reticulum Source: UniProtKB-KW
  5. nucleus Source: UniProtKB-KW
  6. plasma membrane Source: Reactome
  7. vesicle membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381W → K: Small decrease in RASA1-binding. Almost complete loss of RASA1-binding; when associated with K-143 and K-229. 1 Publication
Mutagenesisi143 – 1431W → K: No effect on RASA1-binding. Almost complete loss of RASA1-binding; when associated with K-38 and K-229. 1 Publication
Mutagenesisi229 – 2291W → K: Small decrease in RASA1-binding. Almost complete loss of RASA1-binding; when associated with K-38 and K-229. 1 Publication
Mutagenesisi308 – 3081R → K: No effect on RASA1-binding. 1 Publication

Organism-specific databases

PharmGKBiPA31466.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 377376Cytoplasmic protein NCK1PRO_0000096766Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei85 – 851Phosphoserine2 Publications
Modified residuei91 – 911Phosphoserine1 Publication
Modified residuei96 – 961Phosphoserine1 Publication
Modified residuei105 – 1051Phosphotyrosine3 Publications

Post-translational modificationi

Phosphorylated on Ser and Tyr residues. Phosphorylated in response to activation of EGFR and FcERI. Phosphorylated by activated PDGFRB.9 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP16333.
PaxDbiP16333.
PeptideAtlasiP16333.
PRIDEiP16333.

PTM databases

PhosphoSiteiP16333.

Miscellaneous databases

PMAP-CutDBP16333.

Expressioni

Gene expression databases

BgeeiP16333.
CleanExiHS_NCK1.
ExpressionAtlasiP16333. baseline and differential.
GenevestigatoriP16333.

Organism-specific databases

HPAiCAB005063.

Interactioni

Subunit structurei

Interacts (via SH2 domain and SH3 domain 2) with EGFR. Interacts with PAK1 and SOS1. Interacts (via SH3 domains) with PKN2. Associates with BLNK, PLCG1, VAV1 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with SOCS7. This interaction is required for nuclear import. Part of a complex containing PPP1R15B, PP1 and NCK1. Interacts with RALGPS1. Interacts with CAV2 (tyrosine phosphorylated form). Interacts with ADAM15. Interacts with FASLG. Directly interacts with RASA1. Interacts with isoform 4 of MINK1. Interacts with FLT1 (tyrosine phosphorylated). Interacts with KDR (tyrosine phosphorylated). Interacts (via SH2 domain) with EPHB1; activates the JUN cascade to regulate cell adhesion. Interacts with EPHA2. Interacts (via SH2 domain) with PDGFRB (tyrosine phosphorylated). Interacts with the inactive form of EIF2AK2/PKR.19 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABCG5Q9H2222EBI-389883,EBI-1761423
ABL1P005192EBI-389883,EBI-375543
ABL2P426844EBI-389883,EBI-1102694
AGERQ151092EBI-389883,EBI-1646426
AIREO439182EBI-389883,EBI-1753081
ARHGEF11O150853EBI-389883,EBI-311099
ASAP1Q9ULH16EBI-389883,EBI-346622
ASB16Q96NS52EBI-389883,EBI-1751918
BAZ2AQ9UIF92EBI-389883,EBI-934890
BRD4O608852EBI-389883,EBI-723869
BRPF3Q9ULD43EBI-389883,EBI-1753470
C6P136712EBI-389883,EBI-1753221
CASTP208102EBI-389883,EBI-1268770
CBLBQ131914EBI-389883,EBI-744027
CD247P209632EBI-389883,EBI-1165705
CD3EP077666EBI-389883,EBI-1211297
CDC27P302603EBI-389883,EBI-994813
CELSR3Q9NYQ72EBI-389883,EBI-308417
CHAF1AQ131112EBI-389883,EBI-1020839
CKAP5Q140083EBI-389883,EBI-310585
CNTNAP1P783572EBI-389883,EBI-1751903
CYP4F2P783292EBI-389883,EBI-1752413
DAB2P980822EBI-389883,EBI-1171238
DAG1Q141182EBI-389883,EBI-1755945
DLGAP1O144904EBI-389883,EBI-1753207
DLGAP2Q9P1A64EBI-389883,EBI-1753397
DLGAP3O958862EBI-389883,EBI-1752541
DLGAP4Q9Y2H05EBI-389883,EBI-722139
DLX4Q929883EBI-389883,EBI-1752755
DNM1Q051932EBI-389883,EBI-713135
DOCK3Q8IZD93EBI-389883,EBI-1752361
DUSP15Q9H1R22EBI-389883,EBI-1752795
ECT2Q9H8V33EBI-389883,EBI-1054039
EGFRP005333EBI-389883,EBI-297353
ELK3P419703EBI-389883,EBI-1758534
EPS15P425662EBI-389883,EBI-396684
F2RL2O002542EBI-389883,EBI-1751853
FAM110AQ9BQ892EBI-389883,EBI-1752811
FCGR2BP319942EBI-389883,EBI-724784
FCGR2CP319952EBI-389883,EBI-1396036
FLNBO753693EBI-389883,EBI-352089
FOXH1O755932EBI-389883,EBI-1759806
FYBO151173EBI-389883,EBI-1753267
GAB1Q134803EBI-389883,EBI-517684
GABBR1Q9UBS53EBI-389883,EBI-724156
GAD1Q992592EBI-389883,EBI-743184
GHRP109123EBI-389883,EBI-286316
GLTSCR1Q9NZM43EBI-389883,EBI-1754943
GNSP155862EBI-389883,EBI-1752200
GSTZ1O437082EBI-389883,EBI-748043
HIST1H1EP104122EBI-389883,EBI-358163
HNRNPRO433902EBI-389883,EBI-713419
ID4P479283EBI-389883,EBI-1754719
ISG20L2Q9H9L32EBI-389883,EBI-751335
JAK2O606742EBI-389883,EBI-518647
KDRP359683EBI-389883,EBI-1005487
KITP107213EBI-389883,EBI-1379503
KMT2BQ9UMN62EBI-389883,EBI-765774
LCP2Q1309414EBI-389883,EBI-346946
LRRC3Q9BY712EBI-389883,EBI-1761329
MAP4P278162EBI-389883,EBI-715255
MAP4K1Q929184EBI-389883,EBI-881
MAP4K5Q9Y4K42EBI-389883,EBI-1279
MEPEQ9NQ763EBI-389883,EBI-1753293
METP085812EBI-389883,EBI-1039152
MYLKQ157462EBI-389883,EBI-968482
NELFBQ8WX926EBI-389883,EBI-347721
NKX2-1P436992EBI-389883,EBI-1391923
NPHS1O605003EBI-389883,EBI-996920
PAK2Q131772EBI-389883,EBI-1045887
PDIA2Q130873EBI-389883,EBI-1752525
PHACTR2O751672EBI-389883,EBI-1754409
PIK3C2BO007503EBI-389883,EBI-641107
PNMA2Q9UL422EBI-389883,EBI-302355
PRXQ9BXM02EBI-389883,EBI-1753064
PTPN4P290743EBI-389883,EBI-710431
RAG1P159182EBI-389883,EBI-1755109
RAPGEF1Q139052EBI-389883,EBI-976876
RASA1P209366EBI-389883,EBI-1026476
RIMS2Q9UQ262EBI-389883,EBI-1756749
RIN3Q8TB242EBI-389883,EBI-1570523
RPL13P263732EBI-389883,EBI-356849
RPP38P783452EBI-389883,EBI-366493
RRASP103013EBI-389883,EBI-968703
SCARF2Q96GP62EBI-389883,EBI-1752088
SEMA7AO753262EBI-389883,EBI-1753538
SEPN1Q9NZV52EBI-389883,EBI-1751965
SHANK2Q9UPX86EBI-389883,EBI-1570571
SHANK3Q9BYB04EBI-389883,EBI-1752330
SHROOM2Q137962EBI-389883,EBI-1644065
SLC23A1Q9UHI72EBI-389883,EBI-1759386
SLC24A1O607213EBI-389883,EBI-1753504
SNX12Q9UMY43EBI-389883,EBI-1752602
SNX17Q150363EBI-389883,EBI-1752620
SNX8Q9Y5X22EBI-389883,EBI-1752557
SOS1Q078895EBI-389883,EBI-297487
SOS2Q078903EBI-389883,EBI-298181
SP1P080472EBI-389883,EBI-298336
SPENQ96T583EBI-389883,EBI-765739
SUV39H2Q9H5I12EBI-389883,EBI-723127
SYNJ2O150563EBI-389883,EBI-310513
TGOLN2O434933EBI-389883,EBI-1752146
TMPOP421672EBI-389883,EBI-455283
TPSAB1Q156612EBI-389883,EBI-1761369
TPX2Q9ULW04EBI-389883,EBI-1037322
TRAIPQ9BWF23EBI-389883,EBI-1756205
TRIM39Q9HCM92EBI-389883,EBI-739510
TULP1O002942EBI-389883,EBI-1756778
VPS13AQ96RL73EBI-389883,EBI-1752583
WIPF1O435162EBI-389883,EBI-346356

Protein-protein interaction databases

BioGridi110770. 71 interactions.
DIPiDIP-639N.
IntActiP16333. 195 interactions.
MINTiMINT-92747.
STRINGi9606.ENSP00000288986.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Beta strandi28 – 336Combined sources
Beta strandi35 – 428Combined sources
Beta strandi48 – 514Combined sources
Turni53 – 553Combined sources
Beta strandi56 – 583Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi109 – 1157Combined sources
Beta strandi131 – 1388Combined sources
Beta strandi142 – 1487Combined sources
Beta strandi151 – 1566Combined sources
Helixi157 – 1593Combined sources
Beta strandi160 – 1623Combined sources
Beta strandi168 – 1703Combined sources
Helixi289 – 29911Combined sources
Beta strandi304 – 3096Combined sources
Beta strandi311 – 3133Combined sources
Beta strandi316 – 3216Combined sources
Beta strandi324 – 3263Combined sources
Beta strandi328 – 3358Combined sources
Beta strandi338 – 3414Combined sources
Beta strandi344 – 3485Combined sources
Helixi349 – 35810Combined sources
Beta strandi361 – 3633Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CI8X-ray1.80A281-377[»]
2CI9X-ray1.50A/B281-377[»]
2CUBNMR-A99-173[»]
2JS0NMR-A107-165[»]
2JS2NMR-A1-61[»]
2JW4NMR-A1-63[»]
ProteinModelPortaliP16333.
SMRiP16333. Positions 1-61, 99-174, 193-250, 279-377.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16333.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 6160SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini115 – 16551SH3 2PROSITE-ProRule annotationAdd
BLAST
Domaini190 – 25263SH3 3PROSITE-ProRule annotationAdd
BLAST
Domaini282 – 37695SH2PROSITE-ProRule annotationAdd
BLAST

Domaini

Only the first and third SH3 domains seem to be involved in RASA1-binding; the second SH3 domain and the SH2 domains do not seeem to be involved.

Sequence similaritiesi

Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 3 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG261435.
GeneTreeiENSGT00550000074482.
HOGENOMiHOG000290684.
HOVERGENiHBG000719.
InParanoidiP16333.
KOiK07365.
OMAiTIMQNNP.
OrthoDBiEOG7SV0VJ.
PhylomeDBiP16333.
TreeFamiTF351631.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR017304. NCK.
IPR028526. NCK1.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR22820:SF11. PTHR22820:SF11. 1 hit.
PfamiPF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
PF14604. SH3_9. 1 hit.
[Graphical view]
PIRSFiPIRSF037874. Cytoplasmic_NCK. 1 hit.
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 3 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 3 hits.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
PS50002. SH3. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P16333-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEEVVVVAK FDYVAQQEQE LDIKKNERLW LLDDSKSWWR VRNSMNKTGF
60 70 80 90 100
VPSNYVERKN SARKASIVKN LKDTLGIGKV KRKPSVPDSA SPADDSFVDP
110 120 130 140 150
GERLYDLNMP AYVKFNYMAE REDELSLIKG TKVIVMEKCS DGWWRGSYNG
160 170 180 190 200
QVGWFPSNYV TEEGDSPLGD HVGSLSEKLA AVVNNLNTGQ VLHVVQALYP
210 220 230 240 250
FSSSNDEELN FEKGDVMDVI EKPENDPEWW KCRKINGMVG LVPKNYVTVM
260 270 280 290 300
QNNPLTSGLE PSPPQCDYIR PSLTGKFAGN PWYYGKVTRH QAEMALNERG
310 320 330 340 350
HEGDFLIRDS ESSPNDFSVS LKAQGKNKHF KVQLKETVYC IGQRKFSTME
360 370
ELVEHYKKAP IFTSEQGEKL YLVKHLS
Length:377
Mass (Da):42,864
Last modified:August 1, 1990 - v1
Checksum:i554E9B1A936AEF30
GO
Isoform 2 (identifier: P16333-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: MAEEVVVVAK...IVKNLKDTLG → MDWLNVFKDFFS

Note: No experimental confirmation available.

Show »
Length:313
Mass (Da):35,511
Checksum:iD10F0F2DEF1D72F7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti180 – 1801A → V.
Corresponds to variant rs13320485 [ dbSNP | Ensembl ].
VAR_051228

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7676MAEEV…KDTLG → MDWLNVFKDFFS in isoform 2. 1 PublicationVSP_043122Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17576 mRNA. Translation: CAA35599.1.
AK301460 mRNA. Translation: BAH13487.1.
AC011597 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79105.1.
CH471052 Genomic DNA. Translation: EAW79108.1.
CH471052 Genomic DNA. Translation: EAW79109.1.
BC006403 mRNA. Translation: AAH06403.1.
CCDSiCCDS3092.1. [P16333-1]
CCDS54644.1. [P16333-2]
PIRiS08636.
RefSeqiNP_001177725.1. NM_001190796.2. [P16333-2]
NP_001278928.1. NM_001291999.1. [P16333-1]
NP_006144.1. NM_006153.5. [P16333-1]
XP_006713713.1. XM_006713650.1. [P16333-1]
XP_006713714.1. XM_006713651.1. [P16333-1]
XP_006713715.1. XM_006713652.1. [P16333-1]
UniGeneiHs.126889.
Hs.477693.

Genome annotation databases

EnsembliENST00000288986; ENSP00000288986; ENSG00000158092. [P16333-1]
ENST00000469404; ENSP00000419631; ENSG00000158092. [P16333-2]
ENST00000481752; ENSP00000417273; ENSG00000158092. [P16333-1]
GeneIDi4690.
KEGGihsa:4690.
UCSCiuc003erh.3. human. [P16333-1]
uc011bme.2. human. [P16333-2]

Polymorphism databases

DMDMi127962.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17576 mRNA. Translation: CAA35599.1 .
AK301460 mRNA. Translation: BAH13487.1 .
AC011597 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79105.1 .
CH471052 Genomic DNA. Translation: EAW79108.1 .
CH471052 Genomic DNA. Translation: EAW79109.1 .
BC006403 mRNA. Translation: AAH06403.1 .
CCDSi CCDS3092.1. [P16333-1 ]
CCDS54644.1. [P16333-2 ]
PIRi S08636.
RefSeqi NP_001177725.1. NM_001190796.2. [P16333-2 ]
NP_001278928.1. NM_001291999.1. [P16333-1 ]
NP_006144.1. NM_006153.5. [P16333-1 ]
XP_006713713.1. XM_006713650.1. [P16333-1 ]
XP_006713714.1. XM_006713651.1. [P16333-1 ]
XP_006713715.1. XM_006713652.1. [P16333-1 ]
UniGenei Hs.126889.
Hs.477693.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CI8 X-ray 1.80 A 281-377 [» ]
2CI9 X-ray 1.50 A/B 281-377 [» ]
2CUB NMR - A 99-173 [» ]
2JS0 NMR - A 107-165 [» ]
2JS2 NMR - A 1-61 [» ]
2JW4 NMR - A 1-63 [» ]
ProteinModelPortali P16333.
SMRi P16333. Positions 1-61, 99-174, 193-250, 279-377.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110770. 71 interactions.
DIPi DIP-639N.
IntActi P16333. 195 interactions.
MINTi MINT-92747.
STRINGi 9606.ENSP00000288986.

Chemistry

BindingDBi P16333.
ChEMBLi CHEMBL4846.

PTM databases

PhosphoSitei P16333.

Polymorphism databases

DMDMi 127962.

Proteomic databases

MaxQBi P16333.
PaxDbi P16333.
PeptideAtlasi P16333.
PRIDEi P16333.

Protocols and materials databases

DNASUi 4690.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000288986 ; ENSP00000288986 ; ENSG00000158092 . [P16333-1 ]
ENST00000469404 ; ENSP00000419631 ; ENSG00000158092 . [P16333-2 ]
ENST00000481752 ; ENSP00000417273 ; ENSG00000158092 . [P16333-1 ]
GeneIDi 4690.
KEGGi hsa:4690.
UCSCi uc003erh.3. human. [P16333-1 ]
uc011bme.2. human. [P16333-2 ]

Organism-specific databases

CTDi 4690.
GeneCardsi GC03P136581.
HGNCi HGNC:7664. NCK1.
HPAi CAB005063.
MIMi 600508. gene.
neXtProti NX_P16333.
PharmGKBi PA31466.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG261435.
GeneTreei ENSGT00550000074482.
HOGENOMi HOG000290684.
HOVERGENi HBG000719.
InParanoidi P16333.
KOi K07365.
OMAi TIMQNNP.
OrthoDBi EOG7SV0VJ.
PhylomeDBi P16333.
TreeFami TF351631.

Enzyme and pathway databases

Reactomei REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_12623. Generation of second messenger molecules.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_17025. Downstream signal transduction.
REACT_19226. Activation of Rac.
REACT_22351. DCC mediated attractive signaling.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_23832. Nephrin interactions.
SignaLinki P16333.

Miscellaneous databases

ChiTaRSi NCK1. human.
EvolutionaryTracei P16333.
GeneWikii NCK1.
GenomeRNAii 4690.
NextBioi 18086.
PMAP-CutDB P16333.
PROi P16333.
SOURCEi Search...

Gene expression databases

Bgeei P16333.
CleanExi HS_NCK1.
ExpressionAtlasi P16333. baseline and differential.
Genevestigatori P16333.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR017304. NCK.
IPR028526. NCK1.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR22820:SF11. PTHR22820:SF11. 1 hit.
Pfami PF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
PF14604. SH3_9. 1 hit.
[Graphical view ]
PIRSFi PIRSF037874. Cytoplasmic_NCK. 1 hit.
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 3 hits.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 3 hits.
SSF55550. SSF55550. 1 hit.
PROSITEi PS50001. SH2. 1 hit.
PS50002. SH3. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the src homology units SH2 and SH3."
    Lehmann J.M., Riethmueller G., Johnson J.P.
    Nucleic Acids Res. 18:1048-1048(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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 2).
    Tissue: Synovium.
  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. 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 1).
    Tissue: Uterus.
  6. "Phosphorylation of Nck in response to a variety of receptors, phorbol myristate acetate, and cyclic AMP."
    Park D., Rhee S.G.
    Mol. Cell. Biol. 12:5816-5823(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, PARTIAL PROTEIN SEQUENCE.
  7. "The SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatment."
    Meisenhelder J., Hunter T.
    Mol. Cell. Biol. 12:5843-5856(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  8. "Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor."
    Nishimura R., Li W., Kashishian A., Mondino A., Zhou M., Cooper J., Schlessinger J.
    Mol. Cell. Biol. 13:6889-6896(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDGFRB, PHOSPHORYLATION.
  9. "A novel ligand for an SH3 domain of the adaptor protein Nck bears an SH2 domain and nuclear signaling motifs."
    Matuoka K., Miki H., Takahashi K., Takenawa T.
    Biochem. Biophys. Res. Commun. 239:488-492(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SOCS7.
  10. "Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2."
    Igarashi K., Isohara T., Kato T., Shigeta K., Yamano T., Uno I.
    Biochem. Biophys. Res. Commun. 246:95-99(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT1.
  11. "BLNK: a central linker protein in B cell activation."
    Fu C., Turck C.W., Kurosaki T., Chan A.C.
    Immunity 9:93-103(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BLNK; GRB2; PLCG1 AND VAV.
  12. "Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase."
    Stein E., Huynh-Do U., Lane A.A., Cerretti D.P., Daniel T.O.
    J. Biol. Chem. 273:1303-1308(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL ADHESION, INTERACTION WITH EPHB1.
    Tissue: Kidney.
  13. "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck."
    Braverman L.E., Quilliam L.A.
    J. Biol. Chem. 274:5542-5549(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EGFR; PAK1; PKN2 AND SOS1, PHOSPHORYLATION.
  14. "Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral."
    Rebhun J.F., Chen H., Quilliam L.A.
    J. Biol. Chem. 275:13406-13410(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RALGPS1.
  15. "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1."
    Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., Lisanti M.P.
    J. Biol. Chem. 277:34556-34567(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAV2.
  16. "Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27)."
    Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W., Campos-Gonzalez R., Lisanti M.P.
    Biochemistry 43:13694-13706(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAV2.
  17. "Identification and functional characterization of a novel human misshapen/Nck interacting kinase-related kinase, hMINK beta."
    Hu Y., Leo C., Yu S., Huang B.C., Wang H., Shen M., Luo Y., Daniel-Issakani S., Payan D.G., Xu X.
    J. Biol. Chem. 279:54387-54397(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MINK1.
  18. "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.
  19. "Nck in a complex containing the catalytic subunit of protein phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling and cell survival to endoplasmic reticulum stress."
    Latreille M., Larose L.
    J. Biol. Chem. 281:26633-26644(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN COMPLEX WITH PP1 AND PPP1R15B, FUNCTION, SUBCELLULAR LOCATION.
  20. "Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF."
    Lamalice L., Houle F., Huot J.
    J. Biol. Chem. 281:34009-34020(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KDR.
  21. "Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7."
    Kremer B.E., Adang L.A., Macara I.G.
    Cell 130:837-850(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SOCS7.
  22. "Nck-1 interacts with PKR and modulates its activation by dsRNA."
    Cardin E., Larose L.
    Biochem. Biophys. Res. Commun. 377:231-235(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EIF2AK2, PHOSPHORYLATION.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  24. "Distinct functions of natural ADAM-15 cytoplasmic domain variants in human mammary carcinoma."
    Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M., Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C., Edwards D.R.
    Mol. Cancer Res. 6:383-394(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADAM15.
  25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-91 AND SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
    Voss M., Lettau M., Janssen O.
    BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FASLG.
  27. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND TYR-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  28. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Adaptor protein Nck1 interacts with p120 Ras GTPase-activating protein and regulates its activity."
    Ger M., Zitkus Z., Valius M.
    Cell. Signal. 23:1651-1658(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RASA1, MUTAGENESIS OF TRP-38; TRP-143; TRP-229 AND ARG-308.
  31. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  32. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "Receptor protein tyrosine phosphatase-receptor tyrosine kinase substrate screen identifies EphA2 as a target for LAR in cell migration."
    Lee H., Bennett A.M.
    Mol. Cell. Biol. 33:1430-1441(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH EPHA2.
  34. "Solution structure of the SH3 domain of the human cytoplasmic protein NCK1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 99-174.
  35. "Specificity determinants of a novel Nck interaction with the juxtamembrane domain of the epidermal growth factor receptor."
    Hake M.J., Choowongkomon K., Kostenko O., Carlin C.R., Sonnichsen F.D.
    Biochemistry 47:3096-3108(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-61 AND 107-165, INTERACTION WITH EGFR.

Entry informationi

Entry nameiNCK1_HUMAN
AccessioniPrimary (citable) accession number: P16333
Secondary accession number(s): B7Z751, D3DNE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 26, 2014
This is version 166 of the entry and version 1 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, Direct protein sequencing, 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. SIMILARITY comments
    Index of protein domains and families

External Data

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