wanglab/gogpt-training-data huggingface dataset:
Protein: Homoserine dehydrogenase (HDH) (EC 1.1.1.3) (F4K6Y8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Aspartokinase 1, chloroplastic
- Aspartokinase 3, chloroplastic
- Aspartokinase 2, chloroplastic
- Homoserine kinase
- aspartate-semialdehyde dehydrogenase
- Phosphoserine phosphatase, chloroplastic
- Homoserine kinase, putative / HSK
- Probable cystathionine gamma-synthase 2
- Cystathionine gamma-synthase 1, chloroplastic
- 4-hydroxy-tetrahydrodipicolinate synthase 2, chloroplastic
Sequence:
MKKIPVLLMGCGGVGRHLLQHIVSCRSLHAKMGVHIRVIGVCDSKSLVAPMDVLKEELNDELLSEVCLIKSTGSALSKLGALEKGGYRVVHDSELSTETEEIAKLLGKSTGLAVVDCSASMETIEILMKAVDLGCCIVLANKKPVTSTLEHYDKLALHPRFIRHESTVGAGLPVIASLNRIISSGDPVHRIVGSLSGTLGYVMSELEDGKPLSQVVQAAKKLGYTEPDPRDDLGGMDVARKGLILARLLGKRIIMDSIKIESLYPEEMGPGLMSVDDFLHNGIVKLDQNIEERVKKASSKGCVLRYVCVIEGSSVQVGIREVSKDSPLGRLRGSDNIVEIYSRCYKEQPLVIQGAGAGNDTTAAGVLADIIDLQDLFH
Protein: Leishmanolysin-like peptidase (EC 3.4.24.-) (F1Q5N1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Dynein regulatory complex protein 9
- Guanine nucleotide exchange C9orf72 homolog
Sequence:
MMASGWRQPRSVIGAALFFNTTIIIFISTGAQTHTCDHKVPLHTEVIHKVFLKPDRLTKRSTDQQLNIKIEYDSSLDGLDEAKSSLVKDKLLPQAIDYLQKAFRVRRQSGPILLSRQCATNQYLRKRDDPHRYCQGPCANVTKCGPVVVPEHHLQQCRVCSESGKSCGPVGPPDGEGVARADFVLYVSAMTTERCGQENIVAYAAYCQLESELDRPIAGYANLCPNMISTQPQEFEGMLSTVKHEIIHALGFSAGLFAFYHDDGGKPLTPRSASGLPAYNESLGLYQWSDKVIKRATRLWDIRGGQMVRHTVHLLATPRVVEEARRHFNCPILEGMELENQGGAGTELNHWEKRLLENEAMTGSHTQNRVFSRITLAIMEDTGWYRANYSMAENLQWGRGLGCDFVMKSCKFWIDQHRHKRPTLSPYCDSVRSAPLQLTCRQDQLAVAVCNLQKFSNALPAEYQYFDHIPGVPKEDLSAYGGAVEIADYCPFSQEFSWHVGGEYQRSSYCRIQENQPATWRNYGAEQYGPGSVCLYQKSAFVMEQCTKRMTYPDWGSGCYKVSCTAQGLLVWVQNETFLCVRTGQVISVSIRMNEWVYNGQLICPACSDFCSNCPLPHLIPPLNTTKSAPIDPCSRSSFLVVNLWQLLLTLTPLLIGFLLCGWD
Protein: Fibroblast growth factor 1 (FGF-1) (Acidic fibroblast growth factor) (aFGF) (Heparin-binding growth factor 1) (HBGF-1) (P61148)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequential autophosphorylation on tyrosine residues which act as docking sites for interacting proteins, leading to the activation of several signaling cascades. Binds to integrin ITGAV:ITGB3. Its binding to integrin, subsequent ternary complex formation with integrin and FGFR1, and the recruitment of PTPN11 to the complex are essential for FGF1 signaling. Induces the phosphorylation and activation of FGFR1, FRS2, MAPK3/ERK1, MAPK1/ERK2 and AKT1. Can induce angiogenesis.
Subcellular location: Secreted. Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Note=Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu(2+) ions and S100A13. Secreted in a complex with SYT1. Binding of exogenous FGF1 to FGFR facilitates endocytosis followed by translocation of FGF1 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as LRRC59 (By similarity). {ECO:0000250}.
Interaction partners:
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 3
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 4
- Protein S100-A13
- Fibroblast growth factor-binding protein 1
- Fibroblast growth factor 2
- Synaptotagmin-1
- Epidermal growth factor receptor
- Vascular endothelial growth factor receptor 1
Sequence:
MAEGEITTFAALTERFNLPLGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESAGEVYIKGTETGQYLAMDTEGLLYGSQTPNEECLFLERLEENHYNTYTSKKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD
Protein: GATOR2 complex protein Wdr59 (Q9VKK2)
Organism: Drosophila melanogaster (Fruit fly)
Function: A component of the GATOR subcomplex GATOR2 which functions as an activator of the amino acid-sensing branch of the TORC1 signaling pathway. The two GATOR subcomplexes, GATOR1 and GATOR2, regulate the TORC1 pathway in order to mediate metabolic homeostasis, female gametogenesis and the response to amino acid limitation and complete starvation. GATOR2 activates the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex, controlling the switch to cell proliferation and growth under nutrient replete conditions and during female oocyte development.
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:Q6PJI9}.
Interaction partners:
- GATOR2 complex protein Mio
- Protein SEC13 homolog
- Nucleoporin seh1
- GATOR complex protein Iml1
- GATOR complex protein NPRL2
- GATOR2 complex protein Wdr24
- GATOR complex protein NPRL3
- FI04419p
- GH04846p
- GH16429p
Sequence:
MPPTETLRPGERGTAGGPGAGAPEQTYIVRQSNKYYEHRDSQATAMSVDYSGQWVLLAGRGHLALQRLGQDDGSLRRHERQSKYEVSVAEFAICPSRKEYCAIATSQHIDIVRWGTAEPHYEMSLRGHTRTVTDIDWHGKDPNLLVSCSIDTFSHIWDLREPRKPALSLNAVCMSGATQVGFNRVSGNLLAAAHDGDLRIWDIRKGSCPTHYITAHLNRVHGINWSHKRETCLATASQDGTVKYFDVCNPRRAEKIITTMSPVWRARYTPIGNGLVSIVVPHLGRGENSLLLWSNSKQTDPICSFVGHTDVILDFAWRPNRESSNEIELVTWSRDRTLRVWKIDDNMLKLCEPSAEEIESRFEPDLSELRVPTPPEFLHPRSILVAASLPISTGDGACNTLPMARSPSFGGGYYRREEPHIARSLTDQPTCSLHHEFSLLNTNMPHVEVDTLDAIKRYACFKICAGGHTVILQVTFTTSYPSPSAPPDFQLCQGTTLSSEVSGVLLKVLRCNALQRVKKSRTCLEQCLRALVAAMKKKVAAVGGADRSQLLLQSPRLEGALSSTLHDACIPYPRTSGVHFNAIGMLTTFAQPVNNKRLTLRQHTALTPRTFSSINGSGLLGNVMATAQREANASFYLQERMISGKPGKQRAIRQMNGSPVVHVYDTSSLLHISRRMAREFSLDKCNIAETCRKNGEICRQHGRLDLVPVWLLAELIATPQIPHETLNDLLFYKDPFKKSLLESLIMHYAISGDIQTAVLLACLFDKCPTGGGAIMEKTVRLPPQLNSQISPYHTVLPLDVKSSSSSNTWQQLKQLRSNSWSDSLDLEIKQIQSDAYACSLIRRTKMPLFDQFKRAYAEILFGWQLLSKRALILKHTQNTPPPVQGVEFVTECRKCAKPKRTPKCEPCKRPVLFCVLCRLPVKGAANACLACGHGGHIDHMMQWFEKHNVCATCGCKCLERTSELLALLS
Protein: Pentatricopeptide repeat-containing protein 1, mitochondrial (Q8C2E4)
Organism: Mus musculus (Mouse)
Function: Mitochondrial protein implicated in negative regulation of leucine tRNA levels, as well as negative regulation of mitochondria-encoded proteins and COX activity. Affects also the 3'-processing of mitochondrial tRNAs.
Subcellular location: Mitochondrion {ECO:0000250}. Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- FAST kinase domain-containing protein 2
- FAST kinase domain-containing protein 3
- Neugrin
- Mitochondrial mRNA pseudouridine synthase Rpusd3
- Pseudouridylate synthase RPUSD4, mitochondrial
- Pentatricopeptide repeat-containing protein 2
- Mitochondrial ribonuclease P catalytic subunit
- Probable ATP-dependent RNA helicase DDX28
- Small ribosomal subunit protein mS39
- Transcription termination factor 3, mitochondrial
Sequence:
MDLLRLSRLFSGPRPIGLSVLQHLDLVGSTRWTGGREGPARLRAAFCGSSSPLPLGSGNQKEMSSLCSDSSKLSTVAPQEEAEEESFGSLSGKFSSRRIFHKSTAQLYNLQLKEQGGEEEELEPRPWRGRRNTQYWYFFQCKRLIKEGKLAEALDLFERQMLKEERLQPLECNYTVLIGGCGRVGYLKKAFRLFNDMKKRDLEPSDATYTALFNVCAESPWKDSALQSALKLRQQLQARNFQLNLKTYHALLKVAAKCADLRLCLDVFKEIIQRGHAVTEETFCFLLVGCIQDKKTGFRQAMQVWRQMLSLGIKPSRHGYNLLLEAARDCGLGDPEVASRLLLTSQEETILLPPPKGRHMAGRKVQAKTVHGVSLRHVEALERQLFLEPSQKLEGPPALPEARVTSRTQPEVETTAEPGHTVALTPLASKPTHLELEVSLLSLGTLSPAVVSFGTVATPADRLALMGGLEGFLGKMTEHGLQPDIKTLTLLAEVVEPGSTAESSLLSVLDRHRVEADVTFFNTLIRKKSKLGDLEGAKALLPILAKKGIVPNLRTFCNLAIGCHRPRDGMQLLADMKKSQVSPNIHIYSTLINAALKKLDYTYLISILKDMRQNSVPVNEVVVRQLEFAAEYPPTFDRYKGKNTYLEKIDGFRAYYKQWLKAMPAEEAPHPWQEFQNKPVGDQDTTDKAGGLRDG
Protein: 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily protein (F4J670)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNNLDEIKIESKTCLNDQEQEVKIDNMHMSDQDKNKIEIKNKSGLGEKWPEPIVRVQSLAESNLTSLPDRYIKPPSQRPQTTIIDHQPEVADINIPIIDLDSLFSGNEDDKKRISEACREWGFFQVINHGVKPELMDAARETWKSFFNLPVEAKEVYSNSPRTYEGYGSRLGVEKGAILDWNDYYYLHFLPLALKDFNKWPSLPSNIREMNDEYGKELVKLGGRLMTILSSNLGLRAEQLQEAFGGEDVGACLRVNYYPKCPQPELALGLSPHSDPGGMTILLPDDQVVGLQVRHGDTWITVNPLRHAFIVNIGDQIQILSNSKYKSVEHRVIVNSEKERVSLAFFYNPKSDIPIQPMQQLVTSTMPPLYPPMTFDQYRLFIRTQGYRSYGSLKNYLEIPKDW
Protein: Uncharacterized protein YJR098C (P47139)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm. Mitochondrion.
Interaction partners:
Sequence:
MMATPATDLISDNDKYNKQCLSDSSDSGSDVSFFSVNESEGELDTMEKVDTLIGGARVISNKVEKDSDSEQRGRKKETTGPNNYHNLEEKQASAISLDADDEDLDEIISYSHDGNYDSSHKTFSFSLPFGNTNFRSSSPLAIIKTVLPKTPDEFIKKNLRKNEIKQKLKKSTSISSLEEIELFKYERGIDNSRLRAVKESLEMDALKNSIKQITADPFDKTHDGYYRSRLESIWNELEGDVVIMGGYRGSVLRDATTHKRIWIPLKAGLNMTKVDLLIGPNDEDELKTQKEIVPDGMLTHIGPVDISKRLIKRLDANPNLNVQQFGYDWRLSLDISAKHLTTKLEEIYNKQKNKKGIYIIAHSMGGLVAHKVLQDCTHLIRGIIYVGSPSQCPNILGPIRFGDDVMWNKTIFTKETNFFMRSSFYFLPLDGRCFVDKITLERYDFDFFDTDVWKTLGLSPLVNEKREESAHEKSKLLPRKTKSALSLKATLNATTKFVLNAPVVRNVAGNNKQVPRDVPFDEVFHTSYEDSCEYLARTLKRTKNYLDSLDYDPNKEYPPLAMVYGNKVPTVRGAKVNGIQDIKDGNYEDFYYGPGDGVVHHKWLLPEQRGFPVVCKIASSSGHVSLMTDLKSMAKAFISIVDSEKEGRRSRTRTSS
Protein: Sorcin (22 kDa protein) (CP-22) (V19) (P05044)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Calcium-binding protein that modulates excitation-contraction coupling in the heart. Contributes to calcium homeostasis in the sarcoplasmic reticulum in the heart. Modulates the activity of RYR2 calcium channels.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15754088}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:15754088}; Peripheral membrane protein {ECO:0000269|PubMed:15754088}; Cytoplasmic side {ECO:0000269|PubMed:15754088}. Note=Relocates to the sarcoplasmic reticulum membrane in response to elevated calcium levels and phosphorylation.
Interaction partners:
Sequence:
MAYPGHPGAGGGYYPGGYGGAPGGPSFPGQTQDPLYGYFASVAGQDGQIDADELQRCLTQSGIAGGYKPFNLETCRLMVSMLDRDMSGTMGFNEFKELWAVLNGWRQHFISFDSDRSGTVDPQELQKALTTMGFRLNPQTVNSIAKRYSTSGKITFDDYIACCVKLRALTDSFRRRDSAQQGMVNFSYDDFIQCVMTV
Protein: Transcription initiation factor TFIID subunit 6 (Transcription initiation factor TFIID 70 kDa subunit) (TAF(II)70) (TAFII-70) (TAFII70) (Transcription initiation factor TFIID 80 kDa subunit) (TAF(II)80) (TAFII-80) (TAFII80) (p80) (Q62311)
Organism: Mus musculus (Mouse)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C. TAF6 homodimer connects TFIID modules, forming a rigid core.
Subcellular location: Nucleus.
Interaction partners:
- Transcription initiation factor TFIID subunit 9
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 10
- TATA-box binding protein associated factor 4
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 8
Sequence:
MAEEKKLKLSNTVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALKLKNVEPLYGFHAQEFIPFRFASGGGRELYFYEEKEVDLSDIINTPLPRVPLDVCLKAHWLSIEGCQPAIPENPPPAPKEQQKAEATEPLKSAKPGQEEDGPLKGKGQGAAAADGKGKEKKAPPLLEGAPFRLKPRSIHELSVEQQLYYKEITEACVGSCEAKRAEALQSIATDPGLYQMLPRFSTFISEGVRVNVVQNNLALLIYLMRMVKALMDNPTLYLEKYVHELIPAVMTCIVSRQLCLRPDVDNHWALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTRYGSIAGLAELGHDVIKTLILPRLQQEGERIRSVLDGPVLSNIDRIGADHVQSLLLKHCAPVLAKLRPPPDNQDAYRGEFGSLGPLLCSHVVKARAQAALQAQQVNRTTLTITQPRPTLTLSQAPQPGPRTPGLLKVPGSIALPVQTLVSARAAAPPQPSPPPTKFIVMSSSSSASSTQQVLSLSTSAPGSGSTTTSPVTTTVPSVQPIVKLVSTATTAPPSTAPAGSGSVQKYIVVSLPPTGEGKGGPPSHPSPVPPSSSSPSPLGGSTLCGGKQEAGDSPPPAPGTPKANGSQPTGPGSPQPAL
Protein: Ran-binding protein 9 (RanBP9) (B-cell antigen receptor Ig beta-associated protein 1) (IBAP-1) (Ran-binding protein M) (RanBPM) (P69566)
Organism: Mus musculus (Mouse)
Function: May act as scaffolding protein, and as adapter protein to couple membrane receptors to intracellular signaling pathways. Acts as a mediator of cell spreading and actin cytoskeleton rearrangement. Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18710924}. Cell membrane {ECO:0000305|PubMed:18710924}; Peripheral membrane protein {ECO:0000305|PubMed:18710924}; Cytoplasmic side {ECO:0000305|PubMed:18710924}. Nucleus {ECO:0000269|PubMed:18710924}. Note=Predominantly cytoplasmic (PubMed:18710924). A phosphorylated form is associated with the plasma membrane (By similarity). Perinuclear in spermatids (PubMed:14648869). {ECO:0000250|UniProtKB:Q96S59, ECO:0000269|PubMed:14648869, ECO:0000269|PubMed:18710924}.
Interaction partners:
- Ran-binding protein 10
- WD repeat-containing protein 26
- Muskelin
- Neural cell adhesion molecule L1
- Glucose-induced degradation protein 8 homolog
- Armadillo repeat-containing protein 8
- E3 ubiquitin-protein ligase RMND5A
- Glucose-induced degradation protein 4 homolog
- ATP-dependent RNA helicase DDX4
- E3 ubiquitin-protein transferase MAEA
Sequence:
MSGQPPPPPPQQQPPPPPPPASAAAPATAPPGLAVGPGPAAGVPVPGLAAGSSAAAPFPHGDSALNEQEKELQRRLKRLYPAVDEQETPLPRSWSPKDKFSYIGLSQNNLRVHYKGHGKTPKDAASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLPPNLYPTVGLQTPGEVVDANFGQHPFVFDIEDYMREWRTKIQAQIDRFPIGDREGEWQTMIQKMVSSYLVHHGYCATAEAFARSTDQTVLEELASIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSEVRCLGGRSPKSQDSYPVSPRPFSSPSMSPSHGMSIHSLAPGKSSTAHFSGFESCSNGVISNKAHQSYCHSKHQLSSLTVPELNSLNVSRSQQVNNFTSNDVDMETDHYSNGVGETSSNGFLNGSSKHDHEMEDCDTEMEVDCSQLRRQLCGGSQAAIERMIHFGRELQAMSEQLRRECGKNTANKKMLKDAFSLLAYSDPWNSPVGNQLDPIQREPVCSALNSAILETHNLPKQPPLALAMGQATQCLGLMARSGVGSCAFATVEDYLH
Protein: Cysteine-rich secretory protein LCCL domain containing 2 (A0A0G2JUW3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSCLLNNMVPVGLALLVCGVQAFFLPNTMSLERLLSKYQHTEPHSRVRRAIPMSDRQEILMLHNKLRGQVYPPASNMEYMTWDEELERSAAAWAQRCLWEHGPASLLVSIGQNLAVHWGRYRSPGFHVQSWYDEVKDYTYPYPHECNPWCPERCSGAMCTHYTQMVWATTNKIGCAVHTCRSMSVWGDIWENAVYLVCNYSPKGNWIGEAPYKHGRPCSECPSSYGGGCRNNLCYRAEEHYHQKPEVDEMNEVESPPAPEETHVWVQPRVVKPSKTKKTPVVNFMTQVVHCDTKMKDSCKGSTCNRYQCPAGCLNNKAKVFGSLFYESSSSICRAAIHYGVIDDRGGLVDVTRNGMVPFFVKSQKNGLESLSKYKPSSSFTVSKVKETAVDCHTTVAQLCPFEKPATHCPRVRCPSRCGEEPSYWAPVYGTNIYADTSSICKAAVHAGVIVDEVGGYADVMPVDKKKSYVGSLRNGVQSESPSTPQNGNAFRIFPVRQ
Protein: Zinc-regulated GTPase metalloprotein activator 1A (EC 3.6.5.-) (Cobalamin synthase W domain-containing protein 1) (COBW domain-containing protein 1) (NPC-A-6 COBW domain-containing protein 1) (NPC-A-6) (Q9BRT8)
Organism: Homo sapiens (Human)
Function: Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them. Catalyzes zinc insertion into the active site of methionine aminopeptidase METAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation. Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of METAP1. After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1A to the zinc binding site in the peptidase domain of METAP1 in a process requiring GTP hydrolysis. GTP/GDP exchange is required for release of active METAP1.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8VEH6}.
Interaction partners:
- Zinc-regulated GTPase metalloprotein activator 1B
- Methionine aminopeptidase 1
Sequence:
MLPAVGSADEEEDPAEEDCPELVPIETTQSEEEEKSGLGAKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSALEKSLAVSQGGELYEEWLELRNGCLCCSVKDSGLRAIENLMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEEKPDGLINEATRQVALADAILINKTDLVPEEDVKKLRTTIRSINGLGQILETQRSRVDLSNVLDLHAFDSLSGISLQKKLQHVPGTQPHLDQSIVTITFEVPGNAKEEHLNMFIQNLLWEKNVRNKDNHCMEVIRLKGLVSIKDKSQQVIVQGVHELYDLEETPVSWKDDTERTNRLVLLGRNLDKDILKQLFIATVTETEKQWTTRFQEDQVCT
Protein: Immunoglobulin kappa variable 1-17 (Ig kappa chain V-I region Gal) (Ig kappa chain V-I region WEA) (P01599)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MDMRVPAQLLGLLLLWFPGARCDIQMTQSPSSLSASVGDRVTITCRASQGIRNDLGWYQQKPGKAPKRLIYAASSLQSGVPSRFSGSGSGTEFTLTISSLQPEDFATYYCLQHNSYP
Protein: MEOX2 protein (Q6FHY5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MEHPLFGCLRSPHATAQGLHPFSQSSLALHGRSDHMSYPELSTSSSSCIIAGYPNEEGMFASQHHRGHHHHHHHHHHHHHQQQHQALQTNWHLPQMSSPPSAARHSLCLQPDSGGPPELGSSPPVLCSNSSSLGSSTPTGAACAPGDYGRQALSPAEAEKRSGGKRKSDSSDSQEGNYKSEVNSKPRKERTAFTKEQIRELEAEFAHHNYLTRLRRYEIAVNLDLTERQVKVWFQNRRMKWKRVKGGQQGAAAREKELVNVKKGTLLPSELSGIGAATLQQTGDSIANEDSHDSDHSSEHAHL
Protein: Peroxidase 72 (Atperox P72) (EC 1.11.1.7) (ATP6a) (PRXR8) (Q9FJZ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
Interaction partners:
- SKP1-like protein 1A
- UDP-glycosyltransferase 72E2
Sequence:
MAKSLNILIAALSLIAFSPFCLCSKAYGSGGYLFPQFYDQSCPKAQEIVQSIVAKAFEHDPRMPASLLRLHFHDCFVKGCDASILLDSSGTIISEKRSNPNRNSARGFELIEEIKHALEQECPETVSCADILALAARDSTVITGGPSWEVPLGRRDARGASLSGSNNDIPAPNNTFQTILTKFKRQGLDLVDLVSLSGSHTIGNSRCTSFRQRLYNQSGNGKPDMTLSQYYATLLRQRCPRSGGDQTLFFLDFATPFKFDNHYFKNLIMYKGLLSSDEILFTKNKQSKELVELYAENQEAFFEQFAKSMVKMGNISPLTGAKGEIRRICRRVNHAY
Protein: Interleukin 7 receptor alpha (A8WH87)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MQNILYCFPNDEPIEEVIFATLCKMKEKSKCTNATLGPKYFSFENLENIVKYELQVHLRDGIIEKEIDLTKMVKIPAPELKSATFLKETDEIFIWFEHRHDYVRQCQFQVEIRGEHEPISLLVDYKNISMSRDRLGGDGVYSTRVRAKPINYFAGDWSEWSSDANFTIKTKNHAPIQTPQVVTGILTIILVLIISLIALRWRTQIKKYITPNIPHPKATLAQMQRAKEGLPFTFSPEIFSDAFIHRVDYVDEKPSAPELQDELRYSSSSASVSEMDMNADERLPREQSHLKIRLLDESDLEKEMENSVSQGLKSPQLECKEEAYVTMSSLFKTQ
Protein: Cartilage matrix protein (Matrilin-1) (P21941)
Organism: Homo sapiens (Human)
Function: Cartilage matrix protein is a major component of the extracellular matrix of non-articular cartilage. It binds to collagen.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Aggrecan core protein
- Matrilin-4
- Collagen alpha-1
- Cartilage oligomeric matrix protein
- Collagen alpha-1
Sequence:
MRVLSGTSLMLCSLLLLLQALCSPGLAPQSRGHLCRTRPTDLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGMVNYASTVKQEFSLRAHVSKAALLQAVRRIQPLSTGTMTGLAIQFAITKAFGDAEGGRSRSPDISKVVIVVTDGRPQDSVQDVSARARASGVELFAIGVGSVDKATLRQIASEPQDEHVDYVESYSVIEKLSRKFQEAFCVVSDLCATGDHDCEQVCISSPGSYTCACHEGFTLNSDGKTCNVCSGGGGSSATDLVFLIDGSKSVRPENFELVKKFISQIVDTLDVSDKLAQVGLVQYSSSVRQEFPLGRFHTKKDIKAAVRNMSYMEKGTMTGAALKYLIDNSFTVSSGARPGAQKVGIVFTDGRSQDYINDAAKKAKDLGFKMFAVGVGNAVEDELREIASEPVAEHYFYTADFKTINQIGKKLQKKICVEEDPCACESLVKFQAKVEGLLQALTRKLEAVSKRLAILENTVV
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (A0A2R8Y5K3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDESRHCSTGSGSASFAHTAPPPAGVNPDLEEPPLKEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGSSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEELRTCQITASLFPSNCNGSAHHWEMEDLAAQVFVDQD
Protein: Chaperone protein YcdY (P75915)
Organism: Escherichia coli (strain K12)
Function: Acts as a chaperone that increases YcdX activity, maybe by facilitating the correct insertion of the zinc ions into the catalytic site of YcdX. Involved in the swarming motility process.
Interaction partners:
- Probable phosphatase YcdX
- Inner membrane protein YcdZ
- Glyoxylate/hydroxypyruvate reductase A
- Probable nitrate reductase molybdenum cofactor assembly chaperone NarW
- Chaperone protein TorD
- Hydrogenase-2 operon protein HybE
- Protein YhjJ
- Penicillin-binding protein activator LpoA
- Probable phospholipid transport protein YdbH
- Uncharacterized protein YhfK
Sequence:
MNEFSILCRVLGSLYYRQPQDPLLVPLFTLIREGKLAANWPLEQDELLTRLQKSCDMTQVSADYNALFIGDECAVPPYRSAWVEGATEAEVRAFLSERGMPLADTPADHIGTLLLAASWLEDQSTEDESEALETLFSEYLLPWCGAFLGKVEAHATTPFWRTMAPLTRDAISAMWDELEEDSEE
Protein: Truncated Kidins220 isoform m4 (A0A076N402)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
VRAAREQINIGGLAYPPLPLHEAPPRPPSGYSQPASVCSSSASFNGPFPGGVVSPQPHSSYYSGLSGPQHPFYNRPFFAPYLYTPRYYPGGSQHLISRSSVKTSLPRDQNNGLASVPATGTSLLLSSMTVDIVCEKLRQIEGLDQGMLPQYCTTIKKANINGRVLAQCNIDELKKEMAMNFGDWHLFRSMVLEMRSVENQVVPEDPRFLNENSSAPVAHGESARRTSHSELPHTELSSQTPYTLNFSFEELNTLGLDEGAPRHSNLSWQSQTRRTPSLSSLNSQDSSIEISKLTDKVQAEYRDAYREYIAQMSQLEGGTGSSTISGRSSPHSTYYIGQSSSGGSIHSNLEQERGKENELKQEEGRKSFLMKRGDVLDYSSSGVSTNEASPLDPITEEDEKSDQSGSKLLPGKKSSERPSLFQTDLKLKGSGLRYQKLPSDEDESGTEESDNTPLLKDDKDKKAEGKAERVAKSPEHSVEPIRTFIKAKEYLSDALLDKKDSSDSGVRSNESSPNHSLHNEAADDSQLEKANLIELEDEGHSGKRGMPHSLSGLQDPVIARMSICSEDKKSPSECSLIASSPEESWPSCQKAYNLNRTPSTVTLNNNTAPTNRANQNFDEIEGVRETSQVILRPGPSPNPTAVQNENLKSMAHKRSQRSSYTRLSKDASELHAASSDSTGFGEERESIL