wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein uS2c (30S ribosomal protein S2, chloroplastic) (P56797)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Small ribosomal subunit protein uS11c
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Small ribosomal subunit protein uS14c
- At1g64880
- Small ribosomal subunit protein uS9c
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL28c
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein eS28z/eS28y
- Small ribosomal subunit protein eS1y
Sequence:
MTKRYWNIDLEEMMRAGVHFGHGTRKWNPRMAPYISAKRKGIHIINLTRTARFLSEACDLVFDAASRGKQFLIVGTKNKAADLVSRAAIRARCHYVNKKWLGGMLTNWSTTEKRLHKFRDLRTEQKTEGFNRLPKRDAAVLKRQLSRLETYLGGIKYMTGLPDIVIILDQQEEYTALRECITLGIPTISLIDTNCNPDLADISIPANDDAIASIRFILNKLVFAICEGRSSYIQNS
Protein: RNA-binding protein 45 (Developmentally-regulated RNA-binding protein 1) (RNA-binding motif protein 45) (Q8CFD1)
Organism: Rattus norvegicus (Rat)
Function: RNA-binding protein with binding specificity for poly(C). May play an important role in neural development.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. May shuttle between cytoplasm and nucleus. {ECO:0000250}.
Interaction partners:
- GDH/6PGL endoplasmic bifunctional protein
- Transaldolase
- Glucose-6-phosphate 1-dehydrogenase
- ribulose-phosphate 3-epimerase
- Ribose-5-phosphate isomerase
- Probable ATP-dependent RNA helicase DDX23
- transketolase
- transketolase
- Transketolase
- 6-phosphogluconolactonase
Sequence:
MDDAGSSGGSGGFRPGVDSLDEPPNSRIFLVISKYTSESVLREHFSPFGDIQDIWVVRDKHTKESKGIAFVKFARSSQACRAMEEMHGQCLGPNDTKPIKVFIAQSRSSGSHRDVEDEELTRIFVMIPKSYTEEDLREKFKVYGDIEYCSVIKNKVTGESKGLGYVRYLKPSQAAQAIENCDRSFRALLAEPKNKVLESPEQDYYSSVRQETLGHEPRGNLFPFVGEQQSEFSTFDKNDSRGQEAISKRLSVASRVPFTEEQLFSIFDIVPGLEYCEVHRDPYLNYGHGVVQYFNVASAVYAQYKLHGFQYPPGNRIAVSFLDDGSNSADLIRKMATQMVAAQLASTVWSNPSHQQFLQFGGSAGSQVPQIQTDVVLPSCRKKAPPETPVKERLFIVFNPHPLPLDVLEDIFCRFGNLIEVYLVSGKNVGYVKYADRMSANDAITTLHGKILNGVRLKVMLADSPREVSKKRQRTY
Protein: Bifunctional protein PaaZ [Includes: 2-oxepin-2(3H)-ylideneacetyl-CoA hydrolase (EC 3.3.2.12) (Oxepin-CoA hydrolase); 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (EC 1.2.1.91)] (P77455)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolytic ring cleavage of 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA) via the open-chain aldehyde intermediate to yield 3-oxo-5,6-dehydrosuberyl-CoA. The enzyme consists of a C-terminal (R)-specific enoyl-CoA hydratase domain (formerly MaoC) that cleaves the ring and produces the highly reactive 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde and an N-terminal NADP-dependent aldehyde dehydrogenase domain that oxidizes the aldehyde to 3-oxo-5,6-dehydrosuberyl-CoA. Can also use crotonyl-CoA as substrate.
Interaction partners:
- 1,2-epoxyphenylacetyl-CoA isomerase
- 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase
- 1,2-phenylacetyl-CoA epoxidase, subunit A
- 1,2-phenylacetyl-CoA epoxidase, subunit C
- Putative 1,2-phenylacetyl-CoA epoxidase, subunit D
- 1,2-phenylacetyl-CoA epoxidase, subunit B
- Acyl-coenzyme A thioesterase PaaI
- Phenylacetate-coenzyme A ligase
- 2,3-dehydroadipyl-CoA hydratase
- 1,2-phenylacetyl-CoA epoxidase, subunit E
Sequence:
MQQLASFLSGTWQSGRGRSRLIHHAISGEALWEVTSEGLDMAAARQFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYALSAQTGATRADSWVDIEGGIGTLFTYASLGSRELPDDTLWPEDELIPLSKEGGFAARHLLTSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLVPEGAISLICGSAGDLLDHLDSQDVVTFTGSAATGQMLRVQPNIVAKSIPFTMEADSLNCCVLGEDVTPDQPEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNILLAAGCEIRLGGQADLSAAGAFFPPTLLYCPQPDETPAVHATEAFGPVATLMPAQNQRHALQLACAGGGSLAGTLVTADPQIARQFIADAARTHGRIQILNEESAKESTGHGSPLPQLVHGGPGRAGGGEELGGLRAVKHYMQRTAVQGSPTMLAAISKQWVRGAKVEEDRIHPFRKYFEELQPGDSLLTPRRTMTEADIVNFACLSGDHFYAHMDKIAAAESIFGERVVHGYFVLSAAAGLFVDAGVGPVIANYGLESLRFIEPVKPGDTIQVRLTCKRKTLKKQRSAEEKPTGVVEWAVEVFNQHQTPVALYSILTLVARQHGDFVD
Protein: Cancer/testis antigen 2 (CT2) (Autoimmunogenic cancer/testis antigen NY-ESO-2) (Cancer/testis antigen 6.2) (CT6.2) (L antigen family member 1) (LAGE-1) (O75638)
Organism: Homo sapiens (Human)
Interaction partners:
- Melanoma-associated antigen 4
- Melanoma-associated antigen 3
- Melanoma-associated antigen 6
- Cancer/testis antigen 1
- Melanoma-associated antigen 1
- Melanoma-associated antigen 2
- Melanoma-associated antigen 10
- Melanoma-associated antigen C1
Sequence:
MQAEGRGTGGSTGDADGPGGPGIPDGPGGNAGGPGEAGATGGRGPRGAGAARASGPRGGAPRGPHGGAASAQDGRCPCGARRPDSRLLELHITMPFSSPMEAELVRRILSRDAAPLPRPGAVLKDFTVSGNLLFMSVRDQDREGAGRMRVVGWGLGSASPEGQKARDLRTPKHKVSEQRPGTPGPPPPEGAQGDGCRGVAFNVMFSAPHI
Protein: DNA replication protein DnaC (O67056)
Organism: Aquifex aeolicus (strain VF5)
Interaction partners:
- Replicative DNA helicase
- Chromosomal replication initiator protein DnaA
- DNA primase
- Beta sliding clamp
- Protein RecA
- Bifunctional chorismate mutase/prephenate dehydratase
Sequence:
MQDTATCSICQGTGFVKTEDNKVRLCECRFKKRDVNRELNIPKRYWNANLDTYHPKNVSQNRALLTIRVFVHNFNPEEGKGLTFVGSPGVGKTHLAVATLKAIYEKKGIRGYFFDTKDLIFRLKHLMDEGKDTKFLKTVLNSPVLVLDDLGSERLSDWQRELISYIITYRYNNLKSTIITTNYSLQREEESSVRISADLASRLGENVVSKIYEMNELLVIKGSDLRKSKKLSTPS
Protein: (thale cress) hypothetical protein (A0A384LLE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEGNCSQGRFDSQVSSMRDLRPNAINQNQKQHHPNSRQDSGFNNTMDTRHNNVDRGKKSMSEDDELCLLSSDGQNKSKENSPWQRVKWMDKMVKLMITALSYIGEDSGSDKKFAVLQKKGKWRSVSKVMDERGYHVSPQQCEDKFNDLNKRYKKLNEMLGRGTSCEVVENPSLLDKIDYLNEKEKDEVRRIMSSKHLFYEEMCSYHNGNRLHLPHDPAVQRSLHLITLGSRDDHDNDEHGKHQNEDLDDDDDYEEDHDGALSDRPLKRLRQSQSHEDVGHPNKGYDVPCLPRSQADVNRGISLDSRKAAGLQRQQIESKSLELEGRKLQIQAEMMELERQQFKWEVFSKRREQKLAKMRMENERMKLENERMSLELKRIELGAKL
Protein: Laccase-S (ThLacc-S) (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase S) (Diphenol oxidase S) (Urishiol oxidase S) (C0HLV6)
Organism: Trametes hirsuta (White-rot fungus) (Coriolus hirsutus)
Function: Lignin degradation and detoxification of lignin-derived products (By similarity). Has activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS).
Subcellular location: Secreted {ECO:0000269|PubMed:34093489}.
Interaction partners:
Sequence:
FQLNVIANMNNHTMLKQTSIHWHCHFQKGTNWADGHAFVNACPIASGHSFLYDFTAPDQHGTFWYHSHLSTQYCDGLRGHFVVYDPADPHHDLYDVDDEHTIITLADWYHVAAKLGHHFQLGADSTLINGSGRFAGDPTAHLTVIYVTQGKRYRFHLVSLSCDPNHVFSIDSNHMTVIEADAVSHEHCTVDSIQIYAGQRYSFHLTVDQDVDNYWIRAHPSFGTYSFHDGINSAIARY
Protein: Leucine rich adaptor protein 1 (Leucine repeat adapter protein 35A) (Q96LR2)
Organism: Homo sapiens (Human)
Function: Acts as an activator of the canonical NF-kappa-B pathway and drive the production of pro-inflammatory cytokines. Promotes the antigen (Ag)-presenting and priming function of dendritic cells via the canonical NF-kappa-B pathway. In concert with MYO18A and CDC42BPA/CDC42BPB, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Activates CDC42BPA/CDC42BPB and targets it to actomyosin through its interaction with MYO18A, leading to MYL9/MLC2 phosphorylation and MYH9/MYH10-dependent actomyosin assembly in the lamella (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21048106}.
Interaction partners:
- Serine/threonine-protein kinase MRCK alpha
- Unconventional myosin-XVIIIa
Sequence:
MEGTVESQTPDLRDVEGKVGRKTPEGLLRGLRGECELGTSGALLLPGASSTGHDLGDKIMALKMELAYLRAIDVKILQQLVTLNEGIEAVRWLLEERGTLTSHCSSLTSSQYSLTGGSPGRSRRGSWDSLPDTSTTDRLDSVSIGSFLDTVAPSELDEQGPPGAPRSEMDWAKVIAGGERARTEVDVAATRLGSLRAVWKPPGERLQGGPPESPEDESAKLGFEAHWFWEQCQDDVTFL
Protein: Serpin family C member 1 (A0A096MIW4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEVFKFDTISEKTSDQIHFFFAKLNCRLYRKANKSSNLVSANRLFGDKSLTFNESYQDVSEIVYGAKLQPLDFKENPEQSRVTINNWVANKTEGRIKDVIPQGAIDELTALVLVNTIYFKGIM
Protein: Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase (EC 2.4.1.267) (Asparagine-linked glycosylation protein 6) (Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase) (Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase) (Q12001)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Adds the first glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Man(9)GlcNAc(2)-PP-Dol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:8877369}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dol-P-Man:Man
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl-phosphate beta-glucosyltransferase
- Dol-P-Man:Man
- Alpha-1,2-mannosyltransferase ALG9
- Dol-P-Glc:Glc
- Mannosyl-oligosaccharide glucosidase
- Glucosidase 2 subunit alpha
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
Sequence:
MAIGKRLLVNKPAEESFYASPMYDFLYPFRPVGNQWLPEYIIFVCAVILRCTIGLGPYSGKGSPPLYGDFEAQRHWMEITQHLPLSKWYWYDLQYWGLDYPPLTAFHSYLLGLIGSFFNPSWFALEKSRGFESPDNGLKTYMRSTVIISDILFYFPAVIYFTKWLGRYRNQSPIGQSIAASAILFQPSLMLIDHGHFQYNSVMLGLTAYAINNLLDEYYAMAAVCFVLSICFKQMALYYAPIFFAYLLSRSLLFPKFNIARLTVIAFATLATFAIIFAPLYFLGGGLKNIHQCIHRIFPFARGIFEDKVANFWCVTNVFVKYKERFTIQQLQLYSLIATVIGFLPAMIMTLLHPKKHLLPYVLIACSMSFFLFSFQVHEKTILIPLLPITLLYSSTDWNVLSLVSWINNVALFTLWPLLKKDGLHLQYAVSFLLSNWLIGNFSFITPRFLPKSLTPGPSISSINSDYRRRSLLPYNVVWKSFIIGTYIAMGFYHFLDQFVAPPSKYPDLWVLLNCAVGFICFSIFWLWSYYKIFTSGSKSMKDL
Protein: Erythroid membrane-associated protein (Q9JLN5)
Organism: Mus musculus (Mouse)
Function: Possible role as a cell-adhesion or receptor molecule of erythroid cells.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96PL5}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:10721728}.
Interaction partners:
- Perilipin-2
- Xanthine dehydrogenase/oxidase
- Ammonium transporter Rh type A
- Kell blood group glycoprotein homolog
- Claudin-13
- Krueppel-like factor 1
Sequence:
MERPSPCGSWLVGCLFTIAVFQPPVQVLGDAGKVYIAPLRDTANLPCPLFLWPNMVLSEMRWYRPGHLPRTQAVHVFRDGQDRDEDLMPEYKGRTALVRDAHKESYILQISNVRLEDRGLYQCQVWVGNSSREDNVTLQVAVLGSDPYIHVKGYDAGWIELLCQSVGWFPKPWTEWRDTTGRALLSLSEVHSLDENGLFRTAVSSRIRDNALGNVSCTIHNEALGQEKTTAMIIGAPERGSLSSPAVALSVVLPVLGLLILLGIWLICKQKKSKEKLLYEQAMEVENLLEDHAKEKGRLHKALKKLRSELKLKRAAANAGWRRARLHFVAVTLDPDTAHPKLILSEDRRCVRLGDRKRPVPDNPERFDFVVSVLGSEYFTTGCHYWEVYVGEKTKWILGVCSESVSRKGKVTASPANGHWLVRQSRGNEYEALTSPQTSFRLKESPKCVGIFLDYEAGIISFYNVTDKSHIFTFTHSFSSPLRPFFEPCLHDEGKNTAPLIICTELQKSEESIVPKQEGKDRANGDVSLKMNPSLLSPQGSELFLLNDTWPSNLGPALKGLKVPSL
Protein: Protein UXT (Androgen receptor trapped clone 27 protein) (ART-27) (Ubiquitously expressed transcript protein) (Q9UBK9)
Organism: Homo sapiens (Human)
Function: Involved in gene transcription regulation. Acts in concert with the corepressor URI1 to regulate androgen receptor AR-mediated transcription. Together with URI1, associates with chromatin to the NKX3-1 promoter region. Negatively regulates the transcriptional activity of the estrogen receptor ESR1 by inducing its translocation into the cytoplasm. May act as nuclear chaperone that facilitates the formation of the NF-kappa-B enhanceosome and thus positively regulates NF-kappa-B transcription activity. Potential component of mitochondrial-associated LRPPRC, a multidomain organizer that potentially integrates mitochondria and the microtubular cytoskeleton with chromosome remodeling. Increasing concentrations of UXT contributes to progressive aggregation of mitochondria and cell death potentially through its association with LRPPRC. Suppresses cell transformation and it might mediate this function by interaction and inhibition of the biological activity of cell proliferation and survival stimulatory factors like MECOM.
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:21307340}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:33010352}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21307340, ECO:0000305|PubMed:28106301}. Nucleus {ECO:0000269|PubMed:11854421, ECO:0000269|PubMed:17620405, ECO:0000269|PubMed:21307340, ECO:0000305|PubMed:28106301}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16221885}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16221885}. Note=Predominantly localizes to the nucleus (PubMed:16221885). Localizes to spindle pole during mitosis (PubMed:16221885). {ECO:0000269|PubMed:16221885, ECO:0000269|PubMed:21307340}.
Interaction partners:
- p53 and DNA damage-regulated protein 1
- Prefoldin subunit 6
- Prefoldin subunit 2
- Dynein axonemal assembly factor 10
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- Unconventional prefoldin RPB5 interactor 1
- RNA polymerase II-associated protein 3
- PIH1 domain-containing protein 1
- RuvB-like 2
- RuvB-like 1
Sequence:
MATPPKRRAVEATGEKVLRYETFISDVLQRDLRKVLDHRDKVYEQLAKYLQLRNVIERLQEAKHSELYMQVDLGCNFFVDTVVPDTSRIYVALGYGFFLELTLAEALKFIDRKSSLLTELSNSLTKDSMNIKAHIHMLLEGLRELQGLQNFPEKPHH
Protein: Allene oxide cyclase 4, chloroplastic (EC 5.3.99.6) (Q93ZC5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the production of 12-oxo-phytodienoic acid (OPDA), a precursor of jasmonic acid.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:12777050}.
Interaction partners:
- Allene oxide synthase, chloroplastic
- 12-oxophytodienoate reductase 3
- 12-oxophytodienoate reductase 2
- 12-oxophytodienoate reductase 1
- Putative 12-oxophytodienoate reductase-like protein 1
- Lipoxygenase 3, chloroplastic
- Lipoxygenase 4, chloroplastic
- Lipoxygenase 6, chloroplastic
- Lipoxygenase 2, chloroplastic
- Jasmonate O-methyltransferase
Sequence:
MIMASSAAASISMITLRNLSRNHQSHQSTFLGFSRSFHNQRISSNSPGLSTRARSTTSSTGGFFRTICSSSSNDYSRPTKIQELNVYEFNEGDRNSPAVLKLGKKPDQLCLGDLVPFTNKLYTGDLTKRIGITAGLCVLIQHVPEKKGDRFEASYSFYFGDYGHISVQGPYLTYEDTFLAITGGSGVFEGAYGQVKLRQLVYPTKLFYTFYLKGVAADLPVELTGKHVEPSKEVKPAAEAQATQPGATIANFTN
Protein: Histone deacetylase 2 (EC 3.5.1.98) (Q8IJW3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Heterochromatin protein 1
- Histone deacetylase
- Zinc finger protein, putative
- SANT domain-containing protein
- Histone H4
Sequence:
MKKKITNHKKKNENAKLNIDHDNSSDDNDKTPQIDNIFKNLIVDSYKSINDINNYMRQSNLLYNEKKSKKNKTHPLDSKNTTDRKYNKYRRNEQNMNKVINYDDKKNYDDIENYDNIENYDNIENYDNVENYDYKLPYDEDIIYDEKQNNSDVVIIGYKNFKKGKKKISLDSFNSELSPQSNTSPIYIKKKINEINYHFIQKKKKKKNQKNGELNKKYSKKLSINKKNKKYEKHKKYEKHKKYEKHKKYEKNKKYEKNKKYEKNKKYEKNKKNEKNKKNEKNKKREKNKSGLINNVKKIKRNKKSLSEENLNDSLFSNDEQVNENKYILDKLLISLKNNSDANIHKKKNFYIEYEGNDDFTSFNSKENPNDYFLCMDNDEINNKLNKNKMYSSSYSTTKKKYIYKSHKGLYDNDYMFNNNIFNNKIYNNEMYNNKFNIYNHNIPSNKNYKTNLKGRMSLQMSHDISQEALNTRNYFENNKNFEKERLKKKMRKIRELNLLNNNVEYDCIGFVCDEEYMCEKLHFDENHVESPDRIKCIIKALKEKKLINKMVQIKCREALYDEIRECHSSTHINNIFYSLKKKLKHNNQSVIYPFDKHDTYYTSYTGTVSIRAIGGLLNLCDVILCDKKDKFKYIDFKKSLRYNYDFYKNVNTNSIKRNYESNNMYHKKFLRRSKSESSIYRKCTTYDTFNDFALLNHNKNVYKMNTYHEQIEKKNNNNIINSNNNNNNNNNNNINCSVYNYKNEIDVQNDIHNINNINMNNNIISEENNLDLEAADYNFGNEKDEHTNESYNEENNINQKKDYISQSNSSHNSYYNEIHQGDSIDYNNNNINNDSAISNKLSICEKLSMDNKLSSISNNSNHQDILPNCFKNDEENIHKDKNRDEIINCNNTNVIETEYLNKICENDNYTNNYEENYKNNSFLNSNNSDIFNLPYRSYSSTVYSMDDCNDVNTFTDINCGFAAIRPPGHHCSRSHPSGFCIFNNISVACKYIFKKYGIRKVFIFDWDVHHDNGTQEIFYGDKDVLCFSIHRFDKKVEEKNKKKRHVNKKKKKKKYDIKKDDDNKKDDDNKKDDDNKKDGDNKKDDDNKIYGDNKIYDDNKKDDDNKIYGDNKKDDDNKIYGDNKIYGDNKISNLEKNLKYEKTSNNYKKYKRKNKKSRKRYEENLFYPRTGAKNELGEKEGYKFNINVPLEKGYNNCDVYYVFKYLLLPILEKFRPEFIFISCGFDASINDPLGKCNLTHNLYQWMTFQLKHFANIFCNGRIILVLEGGYNLNYLPKCALACIKALIKKNKSTTTDKEFIKKLYQNNVNNKETNILNNQKECISNQDSSKRFLDAHEEKKKKNDEKNVNRCDNMNDAQHIHGSNNINDAQHIHGNNSMNDAQHINDNNSINDAQHINGNNSMNDAQHINGNNSMNDAQHINGNNSMNDAQLINGSNNTNDMYDKHYLNNHNLDNNIDEKLKSNKTYESLVSTNCVQKNEFLNYPKNNFINKKNMSDHANFYKLKYSSYDKYENKDINYYFRRLHTNNNIVSRTKKLITSGLLHYSTYKVIKYFLNVLKGEPYHLDIELPTYNEFIKKKKLEGREINPERKIKIKINRSSEFRKNDYCFNSYEIMNSYMQHKLNKLKHINNISNKNLQDMFIKQKNFKYTDSSTTISNISQSDLYLSNDDINYSSSCSSTCNRRKVILLNKLKHKINRGLNNIYNTSPNNNNNNNNNNNNNNNNYNNYNNYNNYNNYNNNMVHTEKKTYKKKRKNQINDINLNAPVQMNRTQIDTNEENENLNSNKNKSNRTIKTNQNKLLSYNLSNLQNINNINNTHIIPYADLEHINDDNHLESHNTSNENYINNYYMNCDLTNLKYNENQVLNTFNIYTKIKKGFIFFYGSGHRNQWILPVHNKITKIIKLCSESEAFFYAWLYLSCLKKINISRTKNNYTSILDNNETIENVSIQLPFEEREHILCKQFIKFTVPCYHIFLKRNQINSIRQKQSKQCKDDNNNNNHNITNNTFMDYMKKTYIEWSSSKIFKNNESIQYNDKINDGTNNMIYNSSSNEKKNNVLENDNSLYPLHINQNIQEEAEKDVEVEEEHKTAICLSNVLSSMRHPCVMDIKMGIRLYGDDCNEESIQKKIEKAKNRSCLSHGFHLTSLIGWSKKKKEPFFISKEDAHSIKNDDNFVQAFISYFTACDNIQLSILLIKKILIILEEMKIFFIEQNYFAFYGTSLLFVFDSDPSKKENEDNYSSKDKIEKNELTKNISLSNENMISNDEHNNSFYYKDKKNKLCDQDKINFEEILNFKLNIEKVFYESLSNEERNIILQNKLNQKIIKSVHVYIIDFAHASLNKNQNDEGFLLGIISLHRIMDKTIQRIKELYLSNTDVTNDTV
Protein: Bud site selection protein 22 (Q04347)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in positioning the proximal bud pole signal.
Subcellular location: Nucleus {ECO:0000269|PubMed:11452010, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- RNA polymerase I-specific transcription initiation factor RRN11
- Acyl carrier protein, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome c oxidase subunit 3
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
Sequence:
MPSESSVSIYKLDQLEYQYHYLTKSLQKFEPRYPKTAKLYNCIGKKNKKKIEKLLNSLELKTLDKELDESYSKLLNNKIHYYETHLSKCIKEQIQKISKKNSSKVKDAQKNKSPSIDIEKMLATQLSLDDLALFMTRFRLIKILHQRIKQKSKKIEGDTNNKTWLNNNDYSGYINDKTSKWNPSNIWNEVITKLPSCEKLNALIGQSKIVQNLTESFDLSICLIFGFDVSAMKAKKYGAREKTANANQTHSNIDYDTDDGNEKNAIDSKSNAIGAQTQSNKETTSDNEDLLIKEYEGMLGSSGDEGEGGGYLNPNINYNEVTDEEPSEASSDEDDSDERFSDSEENEPRRKKPKLHNLPELMAGYYSGNDTEEESDEDNKNVKGKKKKRDTAEDRTAREQMSNEPKRKNRRGQRARRKIWEKKYGSQAKHVQRELEKEMEDRKQRQIEYEARVAKREAKAASLEASRSREREDRRTETNNKKEKESASTGEEHPSWIAKRLAEEKLQKAKFEGKKIKFD
Protein: NDR1/HIN1-like protein 2 (Q9SRN1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in plant immunity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9FNH6}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Late embryogenesis abundant
- Late embryogenesis abundant
- Non-race specific disease resistance protein
- RBR-type E3 ubiquitin transferase
Sequence:
MGSKQPYLNGAYYGPSIPPPPKAHRSYNSPGFGCCCFSCLGSCLRCCGCCILSLICNILIAVAVILGVAALILWLIFRPNAVKFYVADANLNRFSFDPNNNLHYSLDLNFTIRNPNQRVGVYYDEFSVSGYYGDQRFGSANVSSFYQGHKNTTVILTKIEGQNLVVLGDGARTDLKDDEKSGIYRINAKLRLSVRFKFWFIKSWKLKPKIKCDDLKIPLGSSNSTGGFKFQPVQCDFDLS
Protein: Synaptic vesicle glycoprotein 2A (Q7L0J3)
Organism: Homo sapiens (Human)
Function: Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles (By similarity).
Subcellular location: Presynapse {ECO:0000250|UniProtKB:Q9JIS5}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q02563}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q02563}. Note=Enriched in chromaffin granules, not present in adrenal microsomes. Associated with both insulin granules and synaptic-like microvesicles in insulin-secreting cells of the pancreas (By similarity). Colocalizes with ATP2B1 at photoreceptor synaptic terminals. {ECO:0000250|UniProtKB:Q02563, ECO:0000250|UniProtKB:Q9JIS5}.
Interaction partners:
- Synaptophysin
- Synaptotagmin-1
- Synaptic vesicle glycoprotein 2B
- Synaptic vesicle glycoprotein 2C
- Pancreatic secretory granule membrane major glycoprotein GP2
- Laminin subunit alpha-5
- Synaptotagmin-2
- Laminin subunit alpha-1
- Synapsin-1
- Synaptosomal-associated protein 25
Sequence:
MEEGFRDRAAFIRGAKDIAKEVKKHAAKKVVKGLDRVQDEYSRRSYSRFEEEDDDDDFPAPSDGYYRGEGTQDEEEGGASSDATEGHDEDDEIYEGEYQGIPRAESGGKGERMADGAPLAGVRGGLSDGEGPPGGRGEAQRRKEREELAQQYEAILRECGHGRFQWTLYFVLGLALMADGVEVFVVGFVLPSAEKDMCLSDSNKGMLGLIVYLGMMVGAFLWGGLADRLGRRQCLLISLSVNSVFAFFSSFVQGYGTFLFCRLLSGVGIGGSIPIVFSYFSEFLAQEKRGEHLSWLCMFWMIGGVYAAAMAWAIIPHYGWSFQMGSAYQFHSWRVFVLVCAFPSVFAIGALTTQPESPRFFLENGKHDEAWMVLKQVHDTNMRAKGHPERVFSVTHIKTIHQEDELIEIQSDTGTWYQRWGVRALSLGGQVWGNFLSCFGPEYRRITLMMMGVWFTMSFSYYGLTVWFPDMIRHLQAVDYASRTKVFPGERVEHVTFNFTLENQIHRGGQYFNDKFIGLRLKSVSFEDSLFEECYFEDVTSSNTFFRNCTFINTVFYNTDLFEYKFVNSRLINSTFLHNKEGCPLDVTGTGEGAYMVYFVSFLGTLAVLPGNIVSALLMDKIGRLRMLAGSSVMSCVSCFFLSFGNSESAMIALLCLFGGVSIASWNALDVLTVELYPSDKRTTAFGFLNALCKLAAVLGISIFTSFVGITKAAPILFASAALALGSSLALKLPETRGQVLQ
Protein: Tryptophan-rich antigen (Pv-fam-a) (A5K5E5)
Organism: Plasmodium vivax (strain Salvador I)
Interaction partners:
Sequence:
MELKKNNAALTSQRSSSRTTSTRSYKNAPKNSTSFLSRLSILIFALSCAIFVNTASGAAANRPNANGFVSPTLIGFGELSIQESEEFKRMAWNNWMLRLESDWKHFNDSVEEAKTKWLHERDSAWSDWLRSLQSKWSHYSEKMLKEHKSNVMEKSANWNDTQWGNWIKTEGRKILEAQWEKWIKKGDDQLQKLILDKWVQWKNDKIRSWLSSEWKTEEDYYWANVERATTAKWLQEAEKMHWLKWKERINRESEQWVNWVQMKESVYINVEWKKWPKWKNDKKILFNKWSTNLVYKWTLKKQWNVWIKEANTAPQV
Protein: Plexin-A2 (Semaphorin receptor OCT) (O75051)
Organism: Homo sapiens (Human)
Function: Coreceptor for SEMA3A and SEMA6A. Necessary for signaling by SEMA6A and class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Neuropilin-1
- Semaphorin-3A
- Semaphorin-6A
- Rho-related GTP-binding protein Rho6
- Semaphorin-6B
- Semaphorin-3C
- Neuropilin-2
- Tyrosine-protein kinase Fyn
- Ras-related C3 botulinum toxin substrate 2
- Tyrosine-protein kinase Fes/Fps
Sequence:
MEQRRPWPRALEVDSRSVVLLSVVWVLLAPPAAGMPQFSTFHSENRDWTFNHLTVHQGTGAVYVGAINRVYKLTGNLTIQVAHKTGPEEDNKSCYPPLIVQPCSEVLTLTNNVNKLLIIDYSENRLLACGSLYQGVCKLLRLDDLFILVEPSHKKEHYLSSVNKTGTMYGVIVRSEGEDGKLFIGTAVDGKQDYFPTLSSRKLPRDPESSAMLDYELHSDFVSSLIKIPSDTLALVSHFDIFYIYGFASGGFVYFLTVQPETPEGVAINSAGDLFYTSRIVRLCKDDPKFHSYVSLPFGCTRAGVEYRLLQAAYLAKPGDSLAQAFNITSQDDVLFAIFSKGQKQYHHPPDDSALCAFPIRAINLQIKERLQSCYQGEGNLELNWLLGKDVQCTKAPVPIDDNFCGLDINQPLGGSTPVEGLTLYTTSRDRMTSVASYVYNGYSVVFVGTKSGKLKKIRADGPPHGGVQYEMVSVLKDGSPILRDMAFSIDQRYLYVMSERQVTRVPVESCEQYTTCGECLSSGDPHCGWCALHNMCSRRDKCQQAWEPNRFAASISQCVSLAVHPSSISVSEHSRLLSLVVSDAPDLSAGIACAFGNLTEVEGQVSGSQVICISPGPKDVPVIPLDQDWFGLELQLRSKETGKIFVSTEFKFYNCSAHQLCLSCVNSAFRCHWCKYRNLCTHDPTTCSFQEGRINISEDCPQLVPTEEILIPVGEVKPITLKARNLPQPQSGQRGYECVLNIQGAIHRVPALRFNSSSVQCQNSSYQYDGMDISNLAVDFAVVWNGNFIIDNPQDLKVHLYKCAAQRESCGLCLKADRKFECGWCSGERRCTLHQHCTSPSSPWLDWSSHNVKCSNPQITEILTVSGPPEGGTRVTIHGVNLGLDFSEIAHHVQVAGVPCTPLPGEYIIAEQIVCEMGHALVGTTSGPVRLCIGECKPEFMTKSHQQYTFVNPSVLSLNPIRGPESGGTMVTITGHYLGAGSSVAVYLGNQTCEFYGRSMSEIVCVSPPSSNGLGPVPVSVSVDRAHVDSNLQFEYIDDPRVQRIEPEWSIASGHTPLTITGFNLDVIQEPRIRVKFNGKESVNVCKVVNTTTLTCLAPSLTTDYRPGLDTVERPDEFGFVFNNVQSLLIYNDTKFIYYPNPTFELLSPTGVLDQKPGSPIILKGKNLCPPASGGAKLNYTVLIGETPCAVTVSETQLLCEPPNLTGQHKVMVHVGGMVFSPGSVSVISDSLLTLPAIVSIAAGGSLLLIIVIIVLIAYKRKSRENDLTLKRLQMQMDNLESRVALECKEAFAELQTDINELTSDLDRSGIPYLDYRTYAMRVLFPGIEDHPVLRELEVQGNGQQHVEKALKLFAQLINNKVFLLTFIRTLELQRSFSMRDRGNVASLIMTGLQGRLEYATDVLKQLLSDLIDKNLENKNHPKLLLRRTESVAEKMLTNWFAFLLHKFLKECAGEPLFMLYCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIEYKTLILNCVNPDNENSPEIPVKVLNCDTITQVKEKILDAVYKNVPYSQRPRAVDMDLEWRQGRIARVVLQDEDITTKIEGDWKRLNTLMHYQVSDRSVVALVPKQTSSYNIPASASISRTSISRYDSSFRYTGSPDSLRSRAPMITPDLESGVKVWHLVKNHDHGDQKEGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETLFSTVHRGSALPLAIKYMFDFLDEQADRHSIHDTDVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKGSITDACLSVVAQTFMDSCSTSEHRLGKDSPSNKLLYAKDIPSYKSWVERYYADIAKLPAISDQDMNAYLAEQSRLHAVEFNMLSALNEIYSYVSKYSEELIGALEQDEQARRQRLAYKVEQLINAMSIES