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Protein

Nck-associated protein 1

Gene

NCKAP1

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

Functioni

Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1.

GO - Molecular functioni

  • protein complex binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: ProtInc
  • central nervous system development Source: ProtInc
  • Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  • innate immune response Source: Reactome
  • positive regulation of Arp2/3 complex-mediated actin nucleation Source: UniProtKB
  • positive regulation of lamellipodium assembly Source: UniProtKB
  • Rac protein signal transduction Source: UniProtKB
  • small GTPase mediated signal transduction Source: Reactome
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiR-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.

Names & Taxonomyi

Protein namesi
Recommended name:
Nck-associated protein 1
Short name:
NAP 1
Alternative name(s):
Membrane-associated protein HEM-2
p125Nap1
Gene namesi
Name:NCKAP1
Synonyms:HEM2, KIAA0587, NAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:7666. NCKAP1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei995 – 101521HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • lamellipodium membrane Source: UniProtKB-SubCell
  • SCAR complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31468.

Polymorphism and mutation databases

DMDMi12643947.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 11281127Nck-associated protein 1PRO_0000216172Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9Y2A7.
MaxQBiQ9Y2A7.
PaxDbiQ9Y2A7.
PRIDEiQ9Y2A7.

PTM databases

iPTMnetiQ9Y2A7.
PhosphoSiteiQ9Y2A7.
SwissPalmiQ9Y2A7.

Expressioni

Tissue specificityi

Expressed in all tissues examined except peripheral blood leukocytes, with highest expression in brain, heart, and skeletal muscle.

Gene expression databases

BgeeiQ9Y2A7.
CleanExiHS_NCKAP1.
GenevisibleiQ9Y2A7. HS.

Organism-specific databases

HPAiHPA020449.

Interactioni

Subunit structurei

Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterdimer containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by WAVE1, ABI2 and BRK1. Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2. CYFIP2 binds to activated RAC1 which causes the complex to dissociate, releasing activated WASF1. The complex can also be activated by NCK1. Associates preferentially with the first SH3 domain of NCK. Interacts with NYAP1, NYAP2 and MYO16 (By similarity). Interacts with human cytomegalovirus protein UL135.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1Q8IZP03EBI-389845,EBI-375446
CYFIP1Q7L5763EBI-389845,EBI-1048143

GO - Molecular functioni

  • protein complex binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116003. 48 interactions.
DIPiDIP-31119N.
IntActiQ9Y2A7. 20 interactions.
MINTiMINT-244824.
STRINGi9606.ENSP00000354251.

Structurei

Secondary structure

1
1128
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103Combined sources
Helixi13 – 3927Combined sources
Turni41 – 433Combined sources
Helixi46 – 483Combined sources
Turni51 – 533Combined sources
Helixi54 – 6310Combined sources
Helixi77 – 815Combined sources
Helixi83 – 11735Combined sources
Turni123 – 1253Combined sources
Helixi127 – 14822Combined sources
Helixi153 – 16513Combined sources
Beta strandi168 – 1703Combined sources
Helixi175 – 18410Combined sources
Helixi188 – 1958Combined sources
Turni196 – 1994Combined sources
Helixi200 – 2089Combined sources
Helixi209 – 2124Combined sources
Helixi214 – 2174Combined sources
Helixi221 – 2266Combined sources
Turni227 – 2304Combined sources
Beta strandi232 – 2354Combined sources
Helixi236 – 2383Combined sources
Beta strandi239 – 2413Combined sources
Helixi248 – 2525Combined sources
Helixi255 – 26814Combined sources
Helixi271 – 2755Combined sources
Helixi277 – 28711Combined sources
Beta strandi291 – 2966Combined sources
Beta strandi299 – 3024Combined sources
Helixi303 – 3119Combined sources
Helixi315 – 3173Combined sources
Helixi320 – 35940Combined sources
Helixi361 – 3644Combined sources
Turni365 – 3673Combined sources
Helixi368 – 39124Combined sources
Turni397 – 4004Combined sources
Helixi405 – 42117Combined sources
Helixi423 – 43614Combined sources
Helixi438 – 4469Combined sources
Helixi454 – 46815Combined sources
Helixi472 – 4765Combined sources
Helixi484 – 49815Combined sources
Helixi506 – 5083Combined sources
Helixi510 – 52718Combined sources
Helixi529 – 5379Combined sources
Helixi540 – 5445Combined sources
Helixi546 – 55813Combined sources
Helixi560 – 5634Combined sources
Helixi564 – 5674Combined sources
Helixi568 – 5725Combined sources
Helixi573 – 5797Combined sources
Helixi585 – 5873Combined sources
Helixi588 – 62639Combined sources
Helixi630 – 6334Combined sources
Helixi634 – 6407Combined sources
Helixi662 – 6643Combined sources
Helixi674 – 68916Combined sources
Beta strandi695 – 6973Combined sources
Beta strandi700 – 7023Combined sources
Helixi704 – 72320Combined sources
Turni728 – 7314Combined sources
Helixi736 – 75217Combined sources
Helixi753 – 7553Combined sources
Helixi761 – 77111Combined sources
Beta strandi774 – 7763Combined sources
Helixi784 – 79411Combined sources
Helixi796 – 8016Combined sources
Beta strandi804 – 8085Combined sources
Turni809 – 8124Combined sources
Beta strandi813 – 8164Combined sources
Beta strandi818 – 8203Combined sources
Helixi828 – 8314Combined sources
Helixi833 – 87139Combined sources
Helixi874 – 8829Combined sources
Helixi887 – 8948Combined sources
Helixi900 – 93132Combined sources
Helixi933 – 94412Combined sources
Helixi955 – 96410Combined sources
Helixi973 – 9797Combined sources
Helixi989 – 100618Combined sources
Helixi1007 – 10126Combined sources
Helixi1014 – 10163Combined sources
Turni1020 – 10234Combined sources
Helixi1029 – 10313Combined sources
Helixi1032 – 104615Combined sources
Helixi1051 – 106818Combined sources
Helixi1069 – 10713Combined sources
Turni1075 – 10806Combined sources
Helixi1081 – 109414Combined sources
Helixi1100 – 11067Combined sources
Helixi1109 – 112012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P8CX-ray2.29B1-1128[»]
4N78X-ray2.43B1-1128[»]
ProteinModelPortaliQ9Y2A7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y2A7.

Family & Domainsi

Sequence similaritiesi

Belongs to the HEM-1/HEM-2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1917. Eukaryota.
ENOG410XPQI. LUCA.
GeneTreeiENSGT00390000016619.
HOGENOMiHOG000231880.
HOVERGENiHBG006344.
InParanoidiQ9Y2A7.
KOiK05750.
OMAiALIRNAY.
OrthoDBiEOG7TJ3H0.
PhylomeDBiQ9Y2A7.
TreeFamiTF313683.

Family and domain databases

InterProiIPR019137. Nck-associated_protein-1.
[Graphical view]
PfamiPF09735. Nckap1. 1 hit.
[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. AlignAdd to basket

Isoform 1 (identifier: Q9Y2A7-1) [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
MSRSVLQPSQ QKLAEKLTIL NDRGVGMLTR LYNIKKACGD PKAKPSYLID
60 70 80 90 100
KNLESAVKFI VRKFPAVETR NNNQQLAQLQ KEKSEILKNL ALYYFTFVDV
110 120 130 140 150
MEFKDHVCEL LNTIDVCQVF FDITVNFDLT KNYLDLIITY TTLMILLSRI
160 170 180 190 200
EERKAIIGLY NYAHEMTHGA SDREYPRLGQ MIVDYENPLK KMMEEFVPHS
210 220 230 240 250
KSLSDALISL QMVYPRRNLS ADQWRNAQLL SLISAPSTML NPAQSDTMPC
260 270 280 290 300
EYLSLDAMEK WIIFGFILCH GILNTDATAL NLWKLALQSS SCLSLFRDEV
310 320 330 340 350
FHIHKAAEDL FVNIRGYNKR INDIRECKEA AVSHAGSMHR ERRKFLRSAL
360 370 380 390 400
KELATVLSDQ PGLLGPKALF VFMALSFARD EIIWLLRHAD NMPKKSADDF
410 420 430 440 450
IDKHIAELIF YMEELRAHVR KYGPVMQRYY VQYLSGFDAV VLNELVQNLS
460 470 480 490 500
VCPEDESIIM SSFVNTMTSL SVKQVEDGEV FDFRGMRLDW FRLQAYTSVS
510 520 530 540 550
KASLGLADHR ELGKMMNTII FHTKMVDSLV EMLVETSDLS IFCFYSRAFE
560 570 580 590 600
KMFQQCLELP SQSRYSIAFP LLCTHFMSCT HELCPEERHH IGDRSLSLCN
610 620 630 640 650
MFLDEMAKQA RNLITDICTE QCTLSDQLLP KHCAKTISQA VNKKSKKQTG
660 670 680 690 700
KKGEPEREKP GVESMRKNRL VVTNLDKLHT ALSELCFSIN YVPNMVVWEH
710 720 730 740 750
TFTPREYLTS HLEIRFTKSI VGMTMYNQAT QEIAKPSELL TSVRAYMTVL
760 770 780 790 800
QSIENYVQID ITRVFNNVLL QQTQHLDSHG EPTITSLYTN WYLETLLRQV
810 820 830 840 850
SNGHIAYFPA MKAFVNLPTE NELTFNAEEY SDISEMRSLS ELLGPYGMKF
860 870 880 890 900
LSESLMWHIS SQVAELKKLV VENVDVLTQM RTSFDKPDQM AALFKRLSSV
910 920 930 940 950
DSVLKRMTII GVILSFRSLA QEALRDVLSY HIPFLVSSIE DFKDHIPRET
960 970 980 990 1000
DMKVAMNVYE LSSAAGLPCE IDPALVVALS SQKSENISPE EEYKIACLLM
1010 1020 1030 1040 1050
VFVAVSLPTL ASNVMSQYSP AIEGHCNNIH CLAKAINQIA AALFTIHKGS
1060 1070 1080 1090 1100
IEDRLKEFLA LASSSLLKIG QETDKTTTRN RESVYLLLDM IVQESPFLTM
1110 1120
DLLESCFPYV LLRNAYHAVY KQSVTSSA
Length:1,128
Mass (Da):128,790
Last modified:November 1, 1999 - v1
Checksum:i12D32BAC7080CB5A
GO
Isoform 2 (identifier: Q9Y2A7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     36-36: K → KQGQVWK

Show »
Length:1,134
Mass (Da):129,517
Checksum:i71019B9B0BCA760D
GO

Sequence cautioni

The sequence BAA25513.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei36 – 361K → KQGQVWK in isoform 2. 1 PublicationVSP_036558

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014509 mRNA. Translation: BAA77295.1.
AB011159 mRNA. Translation: BAA25513.2. Different initiation.
AK292914 mRNA. Translation: BAF85603.1.
BT007033 mRNA. Translation: AAP35681.1.
AC108514 Genomic DNA. Translation: AAX93118.1.
AC064871 Genomic DNA. Translation: AAY24196.1.
BC015025 mRNA. Translation: AAH15025.1.
CCDSiCCDS2287.1. [Q9Y2A7-1]
CCDS2288.1. [Q9Y2A7-2]
RefSeqiNP_038464.1. NM_013436.4. [Q9Y2A7-1]
NP_995314.1. NM_205842.2. [Q9Y2A7-2]
UniGeneiHs.603732.
Hs.708541.

Genome annotation databases

EnsembliENST00000360982; ENSP00000354251; ENSG00000061676. [Q9Y2A7-2]
ENST00000361354; ENSP00000355348; ENSG00000061676. [Q9Y2A7-1]
GeneIDi10787.
KEGGihsa:10787.
UCSCiuc002upb.5. human. [Q9Y2A7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014509 mRNA. Translation: BAA77295.1.
AB011159 mRNA. Translation: BAA25513.2. Different initiation.
AK292914 mRNA. Translation: BAF85603.1.
BT007033 mRNA. Translation: AAP35681.1.
AC108514 Genomic DNA. Translation: AAX93118.1.
AC064871 Genomic DNA. Translation: AAY24196.1.
BC015025 mRNA. Translation: AAH15025.1.
CCDSiCCDS2287.1. [Q9Y2A7-1]
CCDS2288.1. [Q9Y2A7-2]
RefSeqiNP_038464.1. NM_013436.4. [Q9Y2A7-1]
NP_995314.1. NM_205842.2. [Q9Y2A7-2]
UniGeneiHs.603732.
Hs.708541.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P8CX-ray2.29B1-1128[»]
4N78X-ray2.43B1-1128[»]
ProteinModelPortaliQ9Y2A7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116003. 48 interactions.
DIPiDIP-31119N.
IntActiQ9Y2A7. 20 interactions.
MINTiMINT-244824.
STRINGi9606.ENSP00000354251.

PTM databases

iPTMnetiQ9Y2A7.
PhosphoSiteiQ9Y2A7.
SwissPalmiQ9Y2A7.

Polymorphism and mutation databases

DMDMi12643947.

Proteomic databases

EPDiQ9Y2A7.
MaxQBiQ9Y2A7.
PaxDbiQ9Y2A7.
PRIDEiQ9Y2A7.

Protocols and materials databases

DNASUi10787.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360982; ENSP00000354251; ENSG00000061676. [Q9Y2A7-2]
ENST00000361354; ENSP00000355348; ENSG00000061676. [Q9Y2A7-1]
GeneIDi10787.
KEGGihsa:10787.
UCSCiuc002upb.5. human. [Q9Y2A7-1]

Organism-specific databases

CTDi10787.
GeneCardsiNCKAP1.
HGNCiHGNC:7666. NCKAP1.
HPAiHPA020449.
MIMi604891. gene.
neXtProtiNX_Q9Y2A7.
PharmGKBiPA31468.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1917. Eukaryota.
ENOG410XPQI. LUCA.
GeneTreeiENSGT00390000016619.
HOGENOMiHOG000231880.
HOVERGENiHBG006344.
InParanoidiQ9Y2A7.
KOiK05750.
OMAiALIRNAY.
OrthoDBiEOG7TJ3H0.
PhylomeDBiQ9Y2A7.
TreeFamiTF313683.

Enzyme and pathway databases

ReactomeiR-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.

Miscellaneous databases

ChiTaRSiNCKAP1. human.
EvolutionaryTraceiQ9Y2A7.
GeneWikiiNCKAP1.
GenomeRNAii10787.
NextBioi40972.
PROiQ9Y2A7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2A7.
CleanExiHS_NCKAP1.
GenevisibleiQ9Y2A7. HS.

Family and domain databases

InterProiIPR019137. Nck-associated_protein-1.
[Graphical view]
PfamiPF09735. Nckap1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a novel apoptosis-related gene, human Nap1 (NCKAP1), and its possible relation to Alzheimer disease."
    Suzuki T., Nishiyama K., Yamamoto A., Inazawa J., Iwaki T., Yamada T., Kanazawa I., Sakaki Y.
    Genomics 63:246-254(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Trachea.
  4. "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 1).
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Uterus.
  7. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL135.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF WAVE1 COMPLEX, SUBUNIT.

Entry informationi

Entry nameiNCKP1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2A7
Secondary accession number(s): O60329
, Q53QN5, Q53S94, Q53Y35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1999
Last modified: May 11, 2016
This is version 141 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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