wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase ssp1 (EC 2.7.11.1) (P50526)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in actin localization and thus in polarized cell growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- SNF1-like protein kinase ssp2
- Protein sak1
- Serine/threonine-protein kinase atg1
- M-phase inducer phosphatase
Sequence:
MGSVNNEEKTLIEPQRLLRKNTWHPEVDDSEVPPSVFPEYPVHKAIQKTSDSFRKRNYSAGDYVIAPLGGEREGSSLTHSWTFQPGKHNQRLYSDNFQEAQRQWKRLQEWGEVKETKKIRKRFDRFSGRKYINHYEIIKELGRGMHGKVKLGRDTVTRELLAIKIIPKTERRPKLGRANASSQKEKVRREIAILKKCVHPNVVRLREVIDDPSSTKVYLVLEYMSGGEVPWTDCDSPVLSISEARQYFRDVVLGLEYLHYQGIIHRDIKPANLLLNSSNCVKISDFGVSYIANAGLNEDNDVELAKTVGTPAFFAPELCWTDLDRPRPKISEAIDVWALGVTLFCLLFGRCPFNASMEYELFDKIVNERLNIPSTPDIGEEGRDLLKRLLCKDPEQRITLVEVKLHPWTLDGLKDPEKWLQNTDPSTVSRVEVSTDEVASAISLVGRLRRKLGKLFRFRRPKARVFDSSSSVPSDSSICRPESSGNSSIGLSASELSDSFNRLAVNESQKDRERKQVHPVEMGRNSSEKKPRCDFGWDYEAFPNDNQDADDACSYNTGDSIPQVSKSINGHFETYSRTSMDTDDVASFESPNAKHEESGMPVVTFRNYENYDANPSNFHPVVPGFVSSPNLHLAGGSDTPIYCIEHSFTPTN
Protein: Forkhead box protein O6 (Q70KY4)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12857750}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:12857750}. Note=When phosphorylated, translocated from nucleus to cytoplasm. High nuclear localization after stimulation with growth factors.
Interaction partners:
- RAC-alpha serine/threonine-protein kinase
- RAC-beta serine/threonine-protein kinase
- Serine/threonine-protein kinase Sgk1
- RAC-gamma serine/threonine-protein kinase
- Serine/threonine-protein kinase 4
- Ubiquitin carboxyl-terminal hydrolase 7
- Cyclin-dependent kinase 2
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Stress-activated protein kinase JNK
- Mitogen-activated protein kinase 9
Sequence:
MAAKLRAHQVDVDPDFAPQSRPRSCTWPLPQPDLAGDEDGALGAGVAEGSEDCGPERRATAPAMAPAPPLGAEVGPLRKAKSSRRNAWGNLSYADLITKAIESAPDKRLTLSQIYDWMVRYVPYFKDKGDSNSSAGWKNSIRHNLSLHTRFIRVQNEGTGKSSWWMLNPEGGKTGKTPRRRAVSMDNGAKFLRIKGKASKKKQLHLPERSPDDSPPGAPVPGPLSASAKWAASPASHASDDYEAWADFRGSRRPLLGEAAELEDDEALEALAPSSPLMYPSPASALSPALGARCPGELPRLAELGGPLGLHGGGVAGLPDALLDGAQDAYGPRARAGTPSYFGSCKASAYGGGGGFGPPALGSLRRLPMQTIQENKQASFVQAAAPFRPGALPALLPPPPPAPRPGPLLGAPGELALAGAAAAYPGKGAAPYAPPAPSRSALAHPISLMTLPGEAGAAGLAPPAHAAAFGGPPGGLLLDALPGPYAAAAAGPLGAGPDRFPADLDLDMFSGSLECDVESIILNDFMDSDEMDFNFDSALPPPPPGLAGAPPPNQSWVPG
Protein: Protein Iojap-related, mitochondrial (Q9CAF9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be a ribosome silencing factor involved in organelle biogenesis and required for germination.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21908688}.
Interaction partners:
- Short integuments 2, mitochondrial
- At4g38020 family protein)
- Large ribosomal subunit protein uL24c
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL43
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- Protein Iojap
- 50S ribosomal protein L33
- Class I peptide chain release factor
- Large ribosomal subunit protein bL28c
Sequence:
MLTTLRSRCSSLLLNQSWKLAPNRIFASSPSFSSSAGISNVSEILTLPEVEKILADVKADNVTVIPTHNHCFWADFTVIATGRSDWHLRNIAQALVYRAKQKQKGAKHVMLPSVQGYNSKWIVIDYGKFVVHALDEKARGYFNLESLWSAESSGTDTSDQDLQNVFVKVRPKNNSKRKPAKVSS
Protein: GDSL esterase/lipase 2 (EC 3.1.1.-) (Extracellular lipase 2) (Q9SYF0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the resistance to the necrotropic bacteria Erwinia carotovora, probably via negative regulation of auxin signaling. Possesses lipase and antimicrobial activities, inhibiting germination of fungal spores (e.g. Alternaria brassicicola).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Protein WVD2-like 1
- Phospholipase A1 PLIP1, chloroplastic
- Triacylglycerol lipase 1
- Phospholipase SGR2
Sequence:
MENSRSTLIIFFAYTTIILIGSINCRDNNNNNLVTNQSALFVFGDSVFDAGNNNYIDTLPSFRSNYWPYGQTTFKFPTGRVSDGRTIPDFIAEYAWLPLIPAYLQPSNGKNQFPYGVSFASAGAGALVGTFPGMVINLKSQLNNFKKVEKLLRSTLGEAQGKMVISRAVYLFHIGVNDYQYPFSTNSSIFQSSPQEIYVDFVVGNTTAVIKEVYKIGGRKFGFLNMGAYDCAPASLIIDQTKIGTCFKPVTELINLHNEKLESGLRRLERELSGFKYALHDYHTSLSVRMNNPSKYGFKEGKMACCGTGPLRGINTCGGRMGVSQSYELCEKVTDYLFFDHFHLTEKAHQQIAELIWSGPTNVTKPYNLQALFELN
Protein: LD08195p (Uncoordinated 76, isoform A) (Uncoordinated 76, isoform B) (Uncoordinated 76, isoform C) (Q9W525)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Kinesin heavy chain
- Protein unc-119 homolog
- GEO08385p1
- PTB domain-containing adapter protein ced-6
- Autophagy-related 1, isoform B
- Synaptotagmin 1
- Kinesin light chain
Sequence:
MRDLGTKMAELKFEAPLAKFEETDEWGGCDFISSQNAINDTLNLNLKDSSAGGKPDATKLRLLEDAVRDAHVSKNGGGVVGGGAGSISPNCNTLQGGSLIEIGLSDVGLVPGEGAGVGLDGLEKRSLAVGDHVDNFTETFGGSLEDLVNTFDEKITKCFGNYEENVEELAPVQVRSQEEIMNECQMWWTITGNFGNILPIDWSKSYTRQMHMPTLNLGQNHTKQQQQNRNQQQQLHNQSHQAYPHTNGLGSGSGSGLDAQTPGDEFNDLTSEDEAVANDLDMHALILNGLNGDMDDQPIKTVEEVIKEIDDIMDEAESPLDEPETCDSEVIEKAREVLGAPLYAEKLQYLTTTQLNELYMEMEVLIQELSETLINELALRDELEFEKELKNSFISLLLAVQNKRRQYHVEKKRGKFQGPEPKYLTTVIPYHLENGTPNNQSLQVLIKILKAINEDSPTVPALLTDYILKVLCPT
Protein: Chitin deacetylase (EC 3.5.1.41) (AnCDA) (Q5AQQ0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine polymers in chitin to form chitosan and acetate.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Uncharacterized protein
Sequence:
MFATLALVFTALASNALTTPLPLVRRVPTGQVITQCTTPNTIALTFDDGPSEYTPQLLDLLSRYSARATFFVLGDAAAQNPGLLQRMRDEGHQVGAHTYDHVSLPSLGYDGIASQMTRLEEVIRPALGVAPAYMRPPYLETNELVLQVMRDLDYRVISASVDTKDYENQDADAIINTSFQLFLDQLDAGGNIVLAHDIHYWTVASLAERMLQEVNARGLIATTVGDCLGDGEIAWYH
Protein: COP9 signalosome complex subunit 7a (SGN7a) (Signalosome subunit 7a) (Dermal papilla-derived protein 10) (JAB1-containing signalosome subunit 7a) (Q9UBW8)
Organism: Homo sapiens (Human)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9535219}. Nucleus {ECO:0000269|PubMed:9535219}.
Interaction partners:
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 7b
- COP9 signalosome complex subunit 9
- Cullin-4A
Sequence:
MSAEVKVTGQNQEQFLLLAKSAKGAALATLIHQVLEAPGVYVFGELLDMPNVRELAESDFASTFRLLTVFAYGTYADYLAEARNLPPLTEAQKNKLRHLSVVTLAAKVKCIPYAVLLEALALRNVRQLEDLVIEAVYADVLRGSLDQRNQRLEVDYSIGRDIQRQDLSAIARTLQEWCVGCEVVLSGIEEQVSRANQHKEQQLGLKQQIESEVANLKKTIKVTTAAAAAATSQDPEQHLTELREPAPGTNQRQPSKKASKGKGLRGSAKIWSKSN
Protein: Cell adhesion molecule DSCAML1 (Down syndrome cell adhesion molecule-like protein 1 homolog) (Q4VA61)
Organism: Mus musculus (Mouse)
Function: Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Promotes both isoneuronal self-avoidance for creating an orderly neurite arborization in retinal rod bipolar cells and heteroneuronal self-avoidance to maintain mosaic spacing between AII amacrine cells. Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8TD84}; Single-pass type I membrane protein {ECO:0000305}. Synapse {ECO:0000250|UniProtKB:E1C8P7}.
Interaction partners:
- Cell adhesion molecule DSCAM
Sequence:
MWLVTFLLLLDSLHKARPEDVGTSLYFVNDSLQHVTFSSSVGVVVPCPAAGSPSAALRWYLATGDDIYDVPHIRHVHANGTLQLFPFSPSAFNSFIHDNDYFCTAENAAGKIRSPNIRIKAVFREPYTVRVEDQRSMRGNVAVFKCLIPSSVQEYVSVVSWEKDTVSITPENRFFITSHGGLYISDVQKEDALSTYRCITQHKYSGETRQSNGARLSVTDPAESIPTILDGFHSQEVWTGHSVELPCAASGYPIPAIRWLKDGRPLPADSRWAKRITGLTISDLRTEDSGTYICEVTNTFGSAEANGILTVIDPLHVTLTPKKLKTGIGSTVILSCALTGSPEFTIRWYRNTELVLPGEAISIRGLSNETLLISSAQKSHSGAYQCFATRKAQTAQDFAIIVLEDGTPRIVSSFSEKVVNPGEQFSLMCAAKGAPPPTVTWALDDEPVVRDGSHRTNQYTMSDGTTISHMNVTGPQIRDGGVYRCTARNSVGSAEYQARINVRGPPSIRAMRNITAVAGRDTLINCRVIGYPYYSIKWYKDALLLPDNHRQVVFENGTLKLTDVQKGMDEGEYLCSVLIQPQLSISQSVHVAVKVPPLIQPFEFPPASIGQLLYIPCVVSSGDMPIRITWRKDGQVIISGSGVTIESKEFMSSLQISSVSLKHNGNYTCIASNAAATVSRERQLIVRVPPRFVVQPNNQDGIYGKAGVLNCSVDGYPPPKVMWKHAKGSGNPQQYHPVPLTGRIQILPNSSLLIRHVLEEDIGYYLCQASNGVGTDISKAMFLTVKIPAMITSHPNTTIAIKGHPKELNCTARGERPIIIRWEKGDTVIDPDRVMRYAIATKDNGDEVVSTLKLKPADRGDSVFFSCHAINSYGEDRGLIQLTVQEPPDPPELEIREVKARSMNLRWTQRFDGNSIITGFDIEYKNKSDSWDFKQSTRNISPTINQANIVDLHPASVYSIRMYSFNKIGRSEPSKELTISTEEAAPDGPPMDVTLQPVTSQSIQVTWKAPKKELQNGVIRGYQIGYRENSPGSNGQYSIVEMKATGDSEVYTLDNLKKFAQYGVVVQAFNRAGTGPSSSEINATTLEDVPSQPPENVRALSITSDVAVISWSEPPRSTLNGVLKGYRVIFWSLYVDGEWGEMQNVTTTRERVELRGMEKFTNYSVQVLAYTQAGDGVRSSVLYIQTKEDVPGPPAGIKAVPSSASSVVVSWLPPTKPNGVIRKYTIFCSSPGSGQPAPSEYETSPEQLFYRIAHLNRGQQYLLWVAAVTSAGRGNSSEKVTIEPAGKAPAKIISFGGTVTTPWMKDVRLPCNSVGDPAPAVKWTKDSEDSAIPVSLDGHRLIHTNGTLLLRAVKAEDSGYYTCTATNTGGFDTIIVNLLVQVPPDQPRLTVSKTSASSITLTWIPGDNGGSSIRGFVLQYSVDNSEEWKDVFISSSERSFKLDSLKCGTWYKVKLAAKNSVGSGRISEIIEAKTHGREPSFSKDQHLFTHINSTHARLNLQGWNNGGCPITAIVLEYRPKGTWAWQGVRANSSTEVFLTELREATWYELRMRACNSAGCGNETAQFATLDYDGSTIPPIKSAQGEGDDVKKLFTIGCPVILATLGVALLFVVRKKRKEKRLKRLRDAKSLAEMLISKNNRSFDTPVKGPPQGPRLHIDIPRVQLLIEDKEGIKQLGDDKATIPVTDAEFSQAVNPQSFCTGVSLHHPALIQSTGPLIDMSDIRPGTNPVSRKNVKSAHSTRNRYSSQWTLTKCQASTPARTLTSDWRTVGSQHGVTVTESDSYSASLSQDTDKGRNSMVSTESASSTYEELARAYEHAKLEEQLQHAKFEITECFISDSSSDQMTTGTNENADSMTSMSTPSEPGICRFTASPPKPQDADRGKNVAVPIPHRANKSDYCNLPLYTKSEAFFRKADGREPCPVVPPREASMRNLTRAYHTQARHLTLDPASKPLGLPHPGATAATATATLPQRTLAMPAPPAGTAPPAPGPTPSEPSAAPSAAPPAPSTEPPRAGGPHTKMGGSRDSLLEMSTPGVGRSQKQGAGAYSKSYTLV
Protein: tRNA (guanine(10)-N(2))-methyltransferase (EC 2.1.1.214) (tRNA guanosine-2'-O-methyltransferase TRM11) (tRNA methylase 11) (O94636)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Multifunctional methyltransferase subunit trm112
- tRNA
- tRNA
- tRNA
- tRNA
- 18S rRNA
- eRF1 methyltransferase catalytic subunit mtq2
- tRNA
- tRNA
- NAD-dependent histone deacetylase sir2
Sequence:
MSVYLLHLASTHAHFHLPELETLAKIENVEFWLIPKSEYLNVAFKSDKSRNQALFSHAIKEFQDSISPNDATTQNPFMLAVVNSNEDARRWIRRSIFCKGIYEIYCIGDSFTRLHEKMKELNPAPWDSFKHNSSYKFTFETFGTRRTMKEQLSIISDFEYMQLQGPVSMHNPQHVFTVLENRRNNVEGPKVYFGHWCGSGSRDAIDTFDLKQRSYIGITSFDAELSLVTAQMAMAAPGKLIYDPFVGTGSFLYTCSFFGAHTLGSDIDGRQMRGKNGRSIKSNFRQYKLSPFFLDTFTGDVTNCPLRKNLLLDAIVCDPPYGVRAGAKKIAKCSQRPPKESSSTGNHYPKLEQYQISDMVYDIICFASDRLVDGGRLVLWLPTITEEYGIDDIPSHPYLSLIYNSIQPFTHWSRRLLTFQRLPRAHDSKSLNLLPKINNKTPSHHNFREKYFSSAGRASASTKFSPVLE
Protein: Os09g0455300 protein (cDNA clone:001-012-F09, full insert sequence) (cDNA clone:J023048E05, full insert sequence) (Q67TR8)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDFDLFNSYPESQLDLMSTMLQLEQLTALSDQSLFMAAPTSPPVSPMGTPSPQFSPPPQMSVTTTTAGGGYQDQYNSMPATYGAGAGVHQLDFAMSSPGSDSGAPQGSSSSSSSEAMREMIFHIAALQPVEIDPEAVRPPKRRNVRISKDPQSVAARLRRERISERIRILQRLVPGGTKMDTASMLDEAIHYVKFLKSQVQSLERAAAATGAAAHRAAAFGAAYPAALPMQHHAPW
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (A0A0A0MS38)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERMRMAEGGVTSEDYRTFLQQPSGNMDDSGFFSIQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEADQLLQMIRVQQMHRPKLIGEELAQLKEQRVHKTDLERVLEANDGSGMLDEDEEDLQRALALSRQEIDMEDEEADLRRAIQLSMQGSSRNISQDMTQTSGTNLTSEELRKRREAYFEKQQQKQQQQQQQQQQGDLSGQSSHPCERPATSSGALGSDLGDAMSEEDMLQAAVTMSLETVRNDLKTEGKK
Protein: AT14585p (Milkah) (Q9VAZ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LP10995p
- AT22380p
- Testis-enriched HMG-box-containing protein 2, isoform B
- GEO12122p1
- 10 kDa heat shock protein, mitochondrial
- FI13205p
- Histone H2A.v
- GEO13348p1
- Glutamate dehydrogenase
- FI08029p
Sequence:
METVRNRNPPRMKYTAPPKMESDLNFTEKEKKTLTELKQLYLETINLDVALQRDIYNIEKKYEDKHNIIFDKRKKILDEFRKQNHGDVETNQSVPNFWLRVLKASYTEFISKRDEKILECLSDIRSRLYNEPVVKFDIEFHFDPNDYFTNTVLTKTYFLNCLPDPDDPLAYDGAEIYKCEGCVIDWKQTKDQTKTENQEPSFFEFFSPPLLPEDTLDPNYCDVNAMLQNDFEVGFYLKERVIPKAVIFFTGEIADCQSSSGSETESEDTEDESDAEEEDGVDK
Protein: Mitochondrial RNA binding protein (Q57Y20)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYPFIEPRKIGEKYRVEKNMRCLSLLPRGCGPMISVMHVRFITSLSPAGATAAGFQPINSTWTNTLGTATTFASTDQSKREVKAEGGACTTYLAPKSRARKRTVTGTVKILMSMACTSERETKRSTVITTAACAEETKEAAEGTVAVDVTPQPVDPRRLLRVLRAYIRSEALLEKLCRSKIPAVRRHYLVIRARRQRLPVLHRDILLNEVTRVVERREVPLIEVARLLKLRWPAQFTDLSGSRCLSFLKRSLMSWIAELLREGKLAPDGARTVLSQCPRLFHGHISLMSSIVERALLDVNTIQNPEPIIVLMWSVNEAGTHAPNHFWRRVVGRLAQLNRSLRHRFGDTVQLGKCESGHKGDTAVCSAPGDKGKDCGETDIKSNNDNKEGNINDTKRNYTVGHVFSGLTTRQLFRVLRVLRKECWCNDVSTVYDFVDKALKNIALEVDAIGSCEATSQKRPMSRQTITQRVKKSADLTPKELLSLLSIAGELGVDFHASLARTSDFLLAPMVHYLDRGQLLQLSFFVRKTHCDSPTLLQSMANEIVRRGVNYPVSLSVSKAVLRTALQKPVLLSQLTLTPLVDHVISLCKTYGWYMRASQLLGWAEVLYDLSRRHDPSSSVGVNVRSCVERLAAPLRAMLEVGVVPMTVVSRFIELTVILGMRAKPLQYTQSIKLWEERNAAANARITFAKSVLNKENDTLIPMAEFPYNAAELEDSGEVGEVTSRSTAELCRAARQVYDELIYLFEMQMIMRSPITQKEEDRLNDTFSHVGLYNIVVGARAMWRVHLQPSSFPSANASCVEGVVPLSSPHRISSTPPRALPVWVERRVNAIVEGRIRRANISATSTDEDVLRLFGQRRCNAAKVRHFMQLLMEESSLVLVKQQRFVWIFTVELARRFGGEQEQQMAQEMLAKVLY
Protein: SANT_DAMP1_like domain-containing protein (A8XQE0)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Helicase ssl-1
- Enhancer of polycomb-like protein
- Actin-related protein 4
- YEATS domain-containing protein
- HIT-type domain-containing protein
- Uncharacterized protein
- Vacuolar protein sorting-associated protein 72 homolog
- RuvB-like 1
- Mortality factor related protein 1
- Chromatin modification-related protein MEAF6
Sequence:
MIGDVHQILQSTEAPKDATKKPPKPGTSAPRKPEGMKRELFNLMSGKDLTAVMPTDVKKTYKQKFQTGFRSVRKYKWMPFTNESRDDGLMLHHWVRADKVEAMQPYPFSRFNKVIDIPIYTDDEYENYLKIAKWSREETDYLFDTCRMFDLRWPIVYDRFDCKKFNQNRTVEDLKERFYSITYELGILRDPSSSPTAYDAEHERRRKEQLNKQWNRTAEQLQEEEDLTAELRRIELRKKEREKKAHDLQKLINMSEQQPASPSAGGIGGAASAKRKNAFRTKAGSISTTATTFFNPLDISVTALRFSEFKSSGAHFRCQEMKLPTNIGQKKLKNIEVVLEKCKMEMNPVASEPIMKTYNDFRSQIMLAQELKSAMQTAEFELESIRTRMQENGKDFDIEPRFRISQLPEGGIDDDFIGGKGQPATNRRITSYIDASSKDLTAFQIASRKRKTIATTPTITTTTSSSFVSSSNSPSTSAASDPKRIRKI
Protein: Nucleophosmin (NPM) (Nucleolar phosphoprotein B23) (Nucleolar protein NO38) (Numatrin) (P06748)
Organism: Homo sapiens (Human)
Function: Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade. In complex with MYC enhances the transcription of MYC target genes. May act as chaperonin or cotransporter in the nucleolar localization of transcription termination factor TTF1 (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:19208757, ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:25818168, ECO:0000269|PubMed:25956029}. Nucleus, nucleoplasm {ECO:0000269|PubMed:25818168}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Note=Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or treatment with anticancer drugs. Has been found in the cytoplasm in patients with primary acute myelogenous leukemia (AML), but not with secondary AML. Co-localizes with the methylated form of RPS10 in the granular component (GC) region of the nucleolus. Colocalized with nucleolin and APEX1 in nucleoli. Isoform 1 of NEK2 is required for its localization to the centrosome during mitosis. Can shuttle between cytoplasm and nucleus (PubMed:38231884). {ECO:0000269|PubMed:38231884}.
Interaction partners:
- Nucleolin
- Cyclin-dependent kinase inhibitor 2A
- Cellular tumor antigen p53
- ALK tyrosine kinase receptor
- Protein argonaute-2
- Holliday junction recognition protein
- Histone H4
- Large ribosomal subunit protein uL18
- Transcriptional repressor CTCF
- E3 ubiquitin-protein ligase Mdm2
Sequence:
MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEEEEDVKLLSISGKRSAPGGGSKVPQKKVKLAADEDDDDDDEEDDDEDDDDDDFDDEEAEEKAPVKKSIRDTPAKNAQKSNQNGKDSKPSSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL
Protein: Translationally-controlled tumor protein (TCTP) (Lens epithelial protein) (P63029)
Organism: Rattus norvegicus (Rat)
Function: Involved in calcium binding and microtubule stabilization.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P13693}.
Interaction partners:
- Elongation factor 1-gamma
- Ubiquitin-ribosomal protein eL40 fusion protein
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein uL5
- 40S ribosomal protein S24
- Small ribosomal subunit protein eS8
- Small ribosomal subunit protein eS12
- Large ribosomal subunit protein eL18
- Eukaryotic translation elongation factor 1 beta 2
- Small ribosomal subunit protein uS9
Sequence:
MIIYRDLISHDELFSDIYKIREIADGLCLEVEGKMVSRTEGAIDDSLIGGNASAEGPEGEGTESTVVTGVDIVMNHHLQETSFTKEAYKKYIKDYMKSLKGKLEEQKPERVKPFMTGAAEQIKHILANFNNYQFFIGENMNPDGMVALLDYREDGVTPFMIFFKDGLEMEKC
Protein: Anthranilate synthase alpha subunit 1, chloroplastic (OsASA1) (EC 4.1.3.27) (Q94GF1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS to produce anthranilate.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Anthranilate synthase beta subunit 1, chloroplastic
- anthranilate phosphoribosyltransferase
- Anthranilate synthase beta subunit 2, chloroplastic
- Os02g0131200 protein
- indole-3-glycerol-phosphate synthase
- indole-3-glycerol-phosphate synthase
- indole-3-glycerol-phosphate synthase
- phosphoribosylanthranilate isomerase
- Anthranilate synthase alpha subunit 2, chloroplastic
- Tryptophan synthase
Sequence:
MASLVLSLRIAPSTPPLGLGGGRFRGRRGAVACRAATFQQLDAVAVREEESKFKAGAAEGCNILPLKRCIFSDHLTPVLAYRCLVREDDREAPSFLFESVEQGSEGTNVGRYSVVGAQPAMEIVAKANHVTVMDHKMKSRREQFAPDPMKIPRSIMEQWNPQIVEGLPDAFCGGWVGFFSYDTVRYVETKKLPFSNAPEDDRNLPDIHLGLYNDIVVFDHVEKKTHVIHWVRVDCHESVDEAYEDGKNQLEALLSRLHSVNVPTLTAGSVKLNVGQFGSALQKSSMSREDYKKAVVQAKEHILAGDIFQVVLSQRFERRTFADPFEVYRALRIVNPSPYMAYLQARGCILVASSPEILTRVEKRTIVNRPLAGTIRRGKSKAEDKVLEQLLLSDGKQCAEHIMLVDLGRNDVGKVSKPGSVKVEKLMNVERYSHVMHISSTVTGELRDDLTCWDALRAALPVGTVSGAPKVRAMELIDQMEGKMRGPYSGGFGGVSFRGDMDIALALRTIVFPTGSRFDTMYSYTDKNARQEWVAHLQAGAGIVADSKPDDEHQECLNKAAGLARAIDLAESTFVDE
Protein: RuvB-like 1 (EC 3.6.4.12) (Pontin) (zPontin) (Q8AWW7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Has single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity suggesting a role in nuclear processes such as recombination and transcription (By similarity). Proposed core component of the chromatin remodeling Ino80 complex which exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP-dependent nucleosome sliding (By similarity). May act as a negative regulator of embryonic heart growth.
Subcellular location: Nucleus {ECO:0000250}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q9DE26}.
Interaction partners:
- RuvB-like 2
- Actin-related protein 5
- RNA polymerase II-associated protein 3
- Actin-related protein 6
- PIH1 domain-containing protein 2
- Transformation/transcription domain-associated protein
- INO80 complex subunit C
- PIH1 domain-containing protein 1
- Actin-like 6A
- DNA methyltransferase 1-associated protein 1.
Sequence:
MKIEEVKSTTKTQRIASHSHVKGLGLDEAGNAKQSASGLVGQESAREACGIITELIRSKKMAGRAILLAGPPGTGKTALALAMAQELGNKVPFCPMVGSEVYSSEIKKTEVLMENFRRAIGLRIKETKEVYEGEVTELTPCETENPMGGYGKTISHVIIGLKTAKGTKQLKLDPSIYESLQKERVEVGDVIYIEANSGAVKRQGRCDTFATEFDLEAEEYVPLPKGDVHEKKEIIQDVTLHDLDVANARPQGGQDILSMMGQLMKPKKTEITDKLRGEINKVVNKYIDQGVAELVPGVLFIDEVHMLDIECFTYLHRALESSIAPIVVFASNRGNCLIRGTEDISSPHGIPLDLLDRVMIIRTMLYTPQEMKQIIKIRAQTEGLNISEEALSHLGEIGTKTTLRYAVQLLTPASLLARVQGREVVEKEHVEEINELFYDAKSSAKILQDQHTKFMK
Protein: Mekk1a (Q95YH7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSNRRRVRTIDYLALQQSLRLQKTPAATTNAEEQVAREEENGNGHHSTVTAETPPTPPIPPIPPIRLRREQSVEEDVARVEYRVKQTPSRPVQMTRNRIGALEEDLPPEDELAAHYEAFGTTPPRTRLKIKNRDWERKQKVVNVTASADLPASVGGTPKKTRTARSRVLRRNTMDCALLNEMFVNDESKRTDKRLQSLLRDSEREMKNSLATTAVAAPRGNSFHETAHPLESLDQIMPLNSEAMAPIPLRIASKVVESCNRYRCVSSRPIGYRSSAPPLAFAAQLPAGMLRSDGRATPGLGKRKDFHETFANLIKLGSVDRQDAKLSQEEHTWQTELKDLIWLELQAWQADRTVEQQDKYLFEARQGVSDLLTHIINYKFQPRYRREPSLISLDSGTHSDSNSNASSPLPSKMCQGCMSLYCKDCMDHQKLALREVEGMLTRLEAAEALYPSSQAMGALHPIYKSQSFVGRIKSMCLWYNITKQNKLKLSILGKILARLQDEKFSWPVCTSSYIATDSGSSSASGVENDDSAVNSMDSSKPPSMAGSASRKGVTPCHKVQFMLNDATHVPGETSSSNESTSTEVSQWSSECSHSHMRKGSMHDINIFSVEPLGTCSSNGTGEQSTGLYRKFIENVLKSRGLAKSLAFLHKLHNVALYKAHIALEKPGAEDFDYESDAESIEEDVPRLDPEISREQVVELRTYGYWSEEAQSINLPSYIPTFVFLSGIPLQFMHEFLRMRLETRPVRPNPLSLEQLMKELREGLTLALTHRERYQRHITTALVENEAELGSYISILNHYDATVRKTFELYLEYIDQLVLVAVPEGNQKSVLEKEWMFTKLISPMIKGMHTLASQKFCGIISKLLRSISERLVKRTVELDQQIDGTADTDDNEEVKWQLLTICRETQSLLTVERERSIKVLFFAKTFCRDVETTDFHREHYEHDVANQQHDFICSDVKAAFKLLQQDVLQVRNKLTAIIEGVQKRCCLSNMRDLDEQDKQAVLSRTREILHQGYKFGFEYHKDVIRLFEQKIMDQKDSGAHTVDLALGIIAYAKMWMHFVMERCERGRGMRPRWASQGLEFLILACDPQITQHLDDDEFEALKQQMDRCISHVIGITSEPEKVAKKKASPRTRKTSSPATSRSRTPTRTPMSAGMVLNPNTPPLQSPPYNKLLHPQFSLKEDVSGTSYSPVDSSDYVDTPCQRSANGELRLLVPQTPPTPASPGKSSLESTPLALRQERVRDAVNRLDMDLEDGLRERRLIGQVKSLNSSDKVHIRARSVHFRWHRGIKIGQGRFGKVYTAVNNNTGELMAMKEIAIQPGETRALKNVAEELKILEGIKHKNLVRYYGIEVHREELLIFMELCSEGTLESLVELTGNLPEALTRRFTAQLLSGVSELHKHGIVHRDIKTANIFLVDGSNSLKLGDFGSAVKIQAHTTVPGELQGYVGTQAYMAPEVFTKTNSDGHGRAADIWSVGCVVVEMASGKRPWAQFDSNFQIMFKVGMGEKPQAPESLSQEGHDFIDHCLQHDPKRRLTAVELLEHNFCKYGRDECSSEQLQMQVRGSFRRNVATSSS