wanglab/gogpt-training-data huggingface dataset:
Protein: L-selectin (CD62 antigen-like family member L) (Leukocyte adhesion molecule 1) (LAM-1) (Leukocyte surface antigen Leu-8) (Leukocyte-endothelial cell adhesion molecule 1) (LECAM1) (Lymph node homing receptor) (TQ1) (gp90-MEL) (CD antigen CD62L) (P14151)
Organism: Homo sapiens (Human)
Function: Calcium-dependent lectin that mediates cell adhesion by binding to glycoproteins on neighboring cells. Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia.
Subcellular location: Cell membrane {ECO:0000269|PubMed:2509939, ECO:0000269|PubMed:2663882, ECO:0000269|PubMed:28011641}; Single-pass type I membrane protein {ECO:0000305|PubMed:2663882}.
Interaction partners:
- Hematopoietic progenitor cell antigen CD34
- Mucosal addressin cell adhesion molecule 1
- P-selectin glycoprotein ligand 1
- CD44 antigen
- Protein N-terminal asparagine amidohydrolase
- E-selectin
- P-selectin
- Integrin beta-2
- Vascular cell adhesion protein 1
- Calmodulin-1
Sequence:
MIFPWKCQSTQRDLWNIFKLWGWTMLCCDFLAHHGTDCWTYHYSEKPMNWQRARRFCRDNYTDLVAIQNKAEIEYLEKTLPFSRSYYWIGIRKIGGIWTWVGTNKSLTEEAENWGDGEPNNKKNKEDCVEIYIKRNKDAGKWNDDACHKLKAALCYTASCQPWSCSGHGECVEIINNYTCNCDVGYYGPQCQFVIQCEPLEAPELGTMDCTHPLGNFSFSSQCAFSCSEGTNLTGIEETTCGPFGNWSSPEPTCQVIQCEPLSAPDLGIMNCSHPLASFSFTSACTFICSEGTELIGKKKTICESSGIWSNPSPICQKLDKSFSMIKEGDYNPLFIPVAVMVTAFSGLAFIIWLARRLKKGKKSKRSMNDPY
Protein: Sulfotransferase (EC 2.8.2.-) (Q1L875)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAQEECKMISDKLLKYKGTVLTMETNHDITPEYIDSLQDFETRDDDVFVVTFPKSGTVWTQRIMTLIYEEDFPEKANEITYEQMPWIEYREKGKDYNARPSPRLFCSHLLEPLMPRALQKKGKVIYVMRNPKDVMVSYFHFSNKMKNLDSSENYDEILENFFTGCMIGGSWFDHVKGWVTSKDKYNILILTYEEMIKDLRSVIVKICKFVGKNLSDAAINKVVERTTFNQMKVDPVANYESLPQEVTDQPKGVFMRKGTVGDWKNSLTVAQSECVDRVFEERMKHVPLNLVWDIAELRG
Protein: Ceramide phosphoethanolamine synthase (CPE synthase) (EC 2.7.8.-) (Sphingomyelin synthase-related 1) (SMSr) (Q9VS60)
Organism: Drosophila melanogaster (Fruit fly)
Function: A phosphatidylethanolamine (PE)/ceramide ethanolamine phosphotransferase that catalyzes the synthesis of ceramide phosphoethanolamines (CPE), a class of lipids that is a sphingomyelin analog and a major membrane constituent in Drosophila. Transfers the head group from PE (1,2-diacyl-sn-glycero-3-phosphoethanolamine) on to different ceramides such as N-acylsphinganine (dihydroceramide) and N-acyl-(4R)-hydroxysphinganine (phytoceramide) to form N-acyl-sphinganine-1-phosphoethanolamine and N-acyl-(4R)-hydroxysphinganine-1-phosphoethanolamine, respectively. Operates as a ceramide sensor to control ceramide homeostasis in the endoplasmic reticulum, which is critical for the integrity of the early secretory pathway.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19506037}; Multi-pass membrane protein {ECO:0000269|PubMed:19506037}.
Interaction partners:
- Serine palmitoyltransferase 1
- serine C-palmitoyltransferase
- Ceramide kinase, isoform A
- Sphingolipid delta
- Putative neutral sphingomyelinase
Sequence:
MCDGEIGDPVTQPRSEGGGLVTMDQETRTHYLDAATDKHLTNGSPDPEPVDPLLVAQWSIENVTSWATCMEHFSRTLLDCLRQEAIDGEVLLSLTEEDVRDMRYKLGYKLTFGELKKFWIAVLKLQLLVKNSSAESVILGIECHGNGNSVYMPLASTGCGPPSSSTCPCPQAECPSYVSDCDTYLRMGGRYVPPEYFKTAMSLGYSFVVTWITSLTMVIVHERVPDMKRYPPLPDIFLDNVPHIPWAFNMCEITGSLLFTIWVVVLTFHKYRLVLLRRFFALAGTVFLLRCVTMLITSLSVPGTHLQCSQKDFAIDDPNVDMVGALIIRMSRAYRIWSGLGMSIQGVRTCGDYMFSGHTVALTLLNFFITEYTPRNLYFLHTLTWLLNMFGIFFILAAHEHYSIDVFVAFYITSRLFLYYHTLANNRALMQSDSKRTRVWFPMFSYFESSVDGMVPNEYDTLGSLIDGIIEQIFKAKDQLAISVKRCWLDAPLSGNSSAHMFGGESEQCLRNGTASAAFFSPHQSLIGGLGGQRSQTHLNSAQSGSSTPTPATSAPTKSLPTQKKTFRDASVDPFSRTTFAAVQQAENVKDSPMKEKKHL
Protein: Integrin beta (A0A8I5ZTY9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}. Membrane raft {ECO:0000256|ARBA:ARBA00035630}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00035630}.
Interaction partners:
Sequence:
MNSQTASPGWITSQLLFPLFSLIDRLCSSGTLHGGSESQCRAENFTGPGEPDSLRCDTRAQLLLKGCPADDIMDPKSFADLHPQYQVQRSQLSPQKVTLNLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLNNVKKLGGDLLQALNEITESGRIGFGSFVDKTVLPFVNTHPEKLRNPCPNKEKACQPPFAFRHVLKLTDNSNQFQTEVGKQLISGNLDAPEGGLDAIMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNMYKRSNEFDYPSVGQLAHKLSESNIQPIFAVTKKMVKTYEKLTEIIPKSAVGELSDDSSNVVQLIKKAYYKLSSRVFLDHTTIPDTLKVTYDSFCNNRVSSIGKSRGDCDGVQINNPVTFQVKVTASECIQEQSFVIRALGFTDTVTVQVHPQCECQCRDQSRMRNLCGGKGVMECGICRCESGYIGKNCECQTQGRSSQELEGNCRKDNSSIVCSGLGDCICGQCVCHTSDIPNKVIFGQYCECDNFNCERYDGQVCGGLKRGSCSCGQCNCKEGFEGSACQCQRSTTGCLNARLVECSGRGRCQCNRCICEKGYQPPLCEECPGCPLPCSTYVFCAECLKFDKGPFQKNCSVQCANVTLQTVPFKKKPCKERDSEGCWITYTLQQKDGNAYNIHVDDDRECVKGPNVAAIIGGTVAGVVLIGVLLLVIWKALTHLTDLNEYRRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAES
Protein: Zinc chaperone YeiR (EC 3.6.5.-) (P33030)
Organism: Escherichia coli (strain K12)
Function: Zinc chaperone that directly transfers zinc cofactor to target proteins, thereby activating them (By similarity). Zinc is transferred from the CXCC motif in the GTPase domain to the zinc binding site in target proteins in a process requiring GTP hydrolysis (By similarity).
Interaction partners:
- 1-phosphofructokinase
- Type 1 fimbriae regulatory protein FimB
- Elongation factor P-like protein
- Ornithine carbamoyltransferase subunit F
- Type 1 fimbriae regulatory protein FimE
- Uncharacterized protein YjiX
- Lipid A 1-diphosphate synthase
- GTPase ArgK
- UPF0259 membrane protein YciC
Sequence:
MTRTNLITGFLGSGKTTSILHLLAHKDPNEKWAVLVNEFGEVGIDGALLADSGALLKEIPGGCMCCVNGLPMQVGLNTLLRQGKPDRLLIEPTGLGHPKQILDLLTAPVYEPWIDLRATLCILDPRLLLDEKSASNENFRDQLAAADIIVANKSDRTTPESEQALQRWWQQNGGDRQLIHSEHGKVDGHLLDLPRRNLAELPASAAHSHQHVVKKGLAALSLPEHQRWRRSLNSGQGYQACGWIFDADTVFDTIGILEWARLAPVERVKGVLRIPEGLVRINRQGDDLHIETQNVAPPDSRIELISSSEADWNALQSALLKLRLATTA
Protein: Uncharacterized protein DinQ (A5A624)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Small toxic protein TisB
- Small toxic protein ShoB
- Toxic protein SymE
- Small toxic polypeptide LdrD
- Endodeoxyribonuclease toxin RalR
- Toxic protein HokB
Sequence:
MIDKAIIVLGALIALLELIRFLLQLLN
Protein: Small integral membrane protein 5 (Q71RC9)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAATDFVQEMRAVGERLLLKLQRLPQAEPVEIVAFSVIILFTATVLLLLLIACSCCCTHCCCPERRGRKVQVQPTPP
Protein: Mediator of RNA polymerase II transcription subunit 13 (Mediator complex subunit 13) (Suppressor of RNA polymerase B srb9) (Q9HE02)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the srb8-11 complex. The srb8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The srb8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:16630887}.
Interaction partners:
- Serine/threonine-protein kinase srb10
- Mediator of RNA polymerase II transcription subunit 12
- RNA polymerase II holoenzyme cyclin-like subunit
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 14
Sequence:
MSYQVCFKKYVKMRQWPHVLSLRVYASYFLLYNNLPLSSAMVHDGVHLISIKTILTDQPCPNTIYYAKYQVQRKDNEDAASLLEDKEAYLRNQDCIVHAKNDLLFVYDFQAIPSIPEESSSFMLLNSGAFSRLALFQKDELALLLDLYINFLQGLKKTVLYWLCKEYNFVPIYGVLLPLKLHPSFDTQLWNIYGYPVVDLQLSVLSKGHIEFYLKPTRQTVYRLSEVDNLVKKLDTVIRLAPTGCLATLTSVHANASAQTVDALKHRYGFSLTTTSKWVGVTLESSALEFSWPLELCFLETSALRMNDDSLSSNLTDLNNLVLPSNVVNNKKELTEFANEEAEASDKRKEGFTEKEETADAVVTLVPSHSSSPVNYSINSAKSTPASIKVNEEILVADHNVSDDILMEEIDDVGITEADFDYFDLPNVEEKVEMIEPNFANTMTTLDNEEINTSISQSNTSPNLNTHENIPKQMEIQSDDRMVTEDLNPYNVEVDIPEISLNISDSKIPTSAYMPSYYSAVIFPSSISSIFQKYNYGGKYWCPSPSLSTEDLFESFSVAESVTSTDEDICSTNFIQQDFTMEYNHDFFSSSKTPTNISEQSNPDSNYDTLSLAHQVLMNESKSANFDFSFLKSLDLQPTITLGKNDLLNAILSQNLWFRSLPFWKSMTTSFMMSQDVLNFSSYMRKPIRDYLEKILLGESSAVFLSKSPENYLSSINNGHHALNDNPPSQVNFSETLVNFSQPPRVLLKYNEKKLSLDSSAPENWISLCLQPYGESKDFEVFLLSSKSPDVSSKAISFFYDVQLAYENCKLGKLNLSETSINERVMGFSTNINETDNYDDNETTQSDTATSYEQLASVCVNELSGKNVLFFYFLEDDSEKLLKACQHFICVKDSIKRLGDNKFEDKSLRICTIPNSIFDSPNSHTTNSNSFFTKVSLDIYNNDPLLMDGSLKRREPAFLLKKPLLSTLNYQLKDINPRSSALGEYALHVTYTTVEEHLLICNWNDSYGEFETERRYFLQDLEIEDALQQILEVTFTFLNSMHMDWIVIVMKIGEMSDAEYLFWDQAIIPENLQGNVSLTVGYCSAEHGPGSTSKVFSRIPYSASSTVIRNNSSHELSLVAFIREMAMPVPNDEFKKISTILARGYLALDEDESYLPLLSIHLLISRNHDPYLMLNLILKHYLSMIYLQFRTYVSFSSLPLHISTVLYQKQLLQFMASDITHPVTS
Protein: Histone-arginine methyltransferase CARMER (EC 2.1.1.319) (Coactivator-associated arginine methyltransferase 1) (AgCARM1) (Q7Q2B7)
Organism: Anopheles gambiae (African malaria mosquito)
Function: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 at 'Arg-17' and activate transcription via chromatin remodeling.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9VH48}. Nucleus {ECO:0000250|UniProtKB:Q9VH48}.
Interaction partners:
- histone acetyltransferase
- [histone H3]-lysine
- AGAP009664-PA
Sequence:
MARMQGCSVLVLDDSDKLVNKYDHKVTVVCSYDPQGMAVRLLQEGATPPKQLEEYLVSGAGTTHLSRGHTSHMLVVGGELVLFRFASRGDCQQFRSLLHKLSGKVNSVFNLRTEDSSASQYFQFYGYLSQQQNMMQDFVRTSTYQRAIYNNAQDFQNKIVLDVGAGSGILSFFAVQAGAAKVYAVEASNMAQYAQQLVSSNNLTDRIIVIAGKIEEIDLPERVDVIISEPMGYMLYNERMLETYLHGKKWLKPDGKMYPSRGDLHVAPFTDEALYMEQYNKANFWMQTEFHGVNLVALRDAAMKEYFRQPIVDTFDIRICMAKSIRHTTNFLTADEKDLHRIQIDVEFHMLETGTCHGLAFWFDVEFAGTCSQIWLSTSPTEPLTHWYQVRCLLQTPIFVKQGQVLSGKVVLAANQRQSYDVEIDLKLEGTMISSSNTLDLKNPYFRYTGAPVAAPPGSNTTSPSEAFWSQLDAQGARNAVNLVNGITVNGLGEVDMSSTIINTNLMAIGGGANGGGPGGHQPNIHPGLISSTGRQQQQQQQQQQQQAAVGPQQQQQQQSTTAQQLAMTPPIGCAATSTQNVAQHQLIGGAISPSLFTSPAQPILNSHHHHPGQPIHGNQFY
Protein: APC membrane recruitment protein 1 (Amer1) (Protein FAM123B) (Q7TS75)
Organism: Mus musculus (Mouse)
Function: Regulator of the canonical Wnt signaling pathway. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex. Acts both as a positive and negative regulator of the Wnt signaling pathway, depending on the context: acts as a positive regulator by promoting LRP6 phosphorylation. Also acts as a negative regulator by acting as a scaffold protein for the beta-catenin destruction complex and promoting stabilization of Axin at the cell membrane. Promotes CTNNB1 ubiquitination and degradation. Involved in kidney development (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm. Detected in nuclear paraspeckles that are found close to splicing speckles. Translocates to the cell membrane following binding to PtdIns(4,5)P2 (By similarity). {ECO:0000250}.
Interaction partners:
- Axin-1
- Glycogen synthase kinase-3 beta
- Adenomatous polyposis coli protein
- Catenin beta-1
- Kelch-like ECH-associated protein 1
- F-box/WD repeat-containing protein 1A
- Casein kinase I isoform alpha
- Low-density lipoprotein receptor-related protein 6
- Segment polarity protein dishevelled homolog DVL-1
- Axin-2
Sequence:
MESQQDEAVQTKGASTSSDAQDQGAEKGAKNKTTEATEGPTSEPPLSGPGRLKKTAMKLFGGKKGICTLPSFFGGGRSKGSGKVSSKKSLNKSKTHDGLSEASQGPEDVVIEETDLSTPLSKSSAQFPSSQSANGALEIGSKHKTSGTEAIEKAGVEKVPSVHKPKKSLKSFFSSIRRHRKGKTSGADQSVPGAKELEGARTRSHEHVSSISLPSSEEIFRDTRKENAKPQDAPGPKMSPAQVHFSPTTEKAACKNPEKLTRTCASEFMQPKPVLEGGSLEEPHTSETEGKVVAGEVNPPNGPVGDQLSLLFGDVTSLKSFDSLTGCGDIIAEQDMDSMTDSMASGGQRANRDGTKRSSCLVTYQGGGEEMALPDDDDNDDEEEEEEEEEEEEEEEEEEEEEEEEEEEELLEDEEEVKDGEENDDLEYLWASAQIYPRFNMNLGYHTAISPSHQGYMLLDPVQSYPNLGLGELLTPQSDQQESAPNSDEGYYDSTTPGFEDDSGEALGLAHRDCLPRDSYSGDALYEFYEPDDSLEHSPPGDDCLYDLRGRNSEMLDPFLNLEPFSSRPPGAMETEEERLVTIQKQLLYWELRREQREAQEACAREAHAREAYARDTHTRESYGRNVRARETQALEAHSQEGRVQETKVRQEKPALEYQMRPLGPSVMGLVAGTSGGSQTSHRGTTSAFPATSSSEPDWRDFRPLEKRFEGTCSKKDQSTCLMQLFQSDAMFEPDMQEANFGGSPRKAYPSYSPPEEPEEEEEEKEGNATVSFSQALVEFTSNGNLFTSMSYSSDSDSSFTQNLPELPPMVTFDIADVERDGEGKCEENPEFNNDEDLTASLEAFELGYYHKHAFNSYHSRFYQGLPWGVSSLPRYLGLPGVHPRPPPAAMALNRRSRSLDNAESLELELSSSHLAQGYMESDELQAHQEDSDEEGEEEEGEWGRDSPLSLYTEPPGVYDWPPWAHCPLPVGPGLAWMSPNQLYEPFNQSSYVQATCCVPPVAMPVSVPGRTPGDSVSQLARPSHLPLPMGPCYNLQSQASQSGRAKPRDVLLPVDEPSCSSISGANSQSQAKPVGITHGIPQLPRVRPEPFQLQPNHYRASNLDLSKERGEQGASLSTSYSSTAMNGNLAK
Protein: Eukaryotic translation initiation factor 5B (Translation initiation factor IF-2) (M9NFL1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVKAKKGKKEILTKVEGGSSVDEISDVDSDQLSLNNKQNHALKGNQAGDDDVKAVTKGVKKLNVKGKGKAGKNDDSDEEEVVPAKGKASKKSAFELLMDDDEQDEPAAQESQSEKEEKVVVSKPQKNEKKGKKAKRKGKDDDDEDLDKVLAELQAEYAGEAAPAATTVVSPEELADEFSKKKKNKKQAKQAAVAENAGEDEASDDEEGGSTVKSAAQKKKEKKERQKREAALAKQKAATEPKPKPVEKPAPEPEPVATEEVQPAAEEEEEKSSKNKKKGKKDKKAEPEEEKKDAKKKGMSASMVAAMQEQLRKRKEEEERLEREEAERIRLEDEREEARLEAVRLEAERKEKKKQREAERKARLKAEGKLLTKKQKEDRARAQALLESLKAQGLEIPDPNDKRPTRPGTRIRPNKKKGPKEEAAEEEAKAAEAEAQSAAAAAAAAAAEKAEEERVKESWDATDSEAEPEPEEETSQATNNGKTEAAEEENEDTDDDEDDDDDEDDSDDSDGDSDDSREVSVLANDPESRRLRAEARILKRQAEAEKKRSTDELRAGVVCVLGHVDTGKTKILDKLRRTHVQDSEAGGITQQIGATNVPIEAIKEQTKYVKAAAGFEHRLPGLLIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESIQLLKKKKCPFIVALNKIDRLYDWKQLARRDVRDVLKEQQSNTQLEFQQRTKDVILQFAEQGLNAALFYENTDPKTYISLVPTSAISGEGMGNLLFMIADFCQNMLAKRLMYSEELQATVLEVKALPGLGTTIDAILINGKLREGQTMVVAGTDGPIVTQIRSLLMPQPMKELRVKNAYVEYKEVKAAQGVKIAAKDLEKAIAGINLLIAHKPDEVEICTEEVARELKSALSHIKLAQTGVHVQASTLGSLEALLEFLRTSKIPYSAIRIGPVVKRDVMKASTMLEHEAQYATILAFDVKIEREAQEMADSLGVKIFQADIIYHLFDKFTAYREELKQKKREEFRSVAVFPCKLRILPQFVFNSRDPIVMGVMVENGIVKVGTPICVPSKEISRQSIDACKDYFRDDLIKADWALMVELKKLFEIL
Protein: Protein pellino (O77237)
Organism: Drosophila melanogaster (Fruit fly)
Function: Scaffold protein involved in the Toll signaling pathway via its interaction with pelle/pll kinase.
Interaction partners:
- Serine/threonine-protein kinase pelle
- LD20892p
- GH01161p
- Splicing factor Cactin
- GEO06356p1
- Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
- Protein Tube
Sequence:
MVKRTDGTESPILAEDGGDGHDKPRLRYGELVILGYNGYLPQGDRGRRRSKFVLHKRTEASGVKRSKHYIVQSPQTSKAILDANQHSISYTLSRNQAVIVEYKEDTETDMFQVGRSSESPIDFVVMDTLPGDKKDAKVMQSTISRFACRILVNRCEPAKARIFAAGFDSSRNIFLGEKATKWQDNVEIDGLTTNGVLIMHPKGSFCGGNAKCGLWRECSVGGDVFSLRESRSAQQKGQPIYDECNILQDGTLIDLCGATLLWRSAEGLQHSPTKHDLEKLIDAINAGRPQCPVGLNTLVIPRKVNIGDQVNQPYVYLNCGHVQGHHDWGQDENTGARRCPMCLELGPVVTLCMGLEPAFYVDVGAPTYAFNPCGHMATEKTVKYWANVEIPHGTNGFQAVCPFCATPLDGATGYIKLIFQDNLD
Protein: LP05709p (Q8MS79)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEGLCGDCNGNAGNDLQPNPAKKKAGVDVIQSWQADEPKLGLVEECLSEDVPKEHCIPLPPEKDPCLQFYNAELFGKCPLAVDPIAYVSACQQDICKPGNTQQGVCVALAAYAKECNQHGICTNWRRPQLCPYECPSDMVYEPCGCAKNCDTIKALSEFDAVSLKNEAVVHTVKTDEMCLSSERFEGCFCPPGKVMDGGQCVPEIACTKCDDGLHLPDEKWKKDKCTECQCDSKGKTTCVEKKCQVEENICAEGYRPETIVSVDECCPRYRCVPETKDPSKLCLAPLVPICGPGQFKKEKKDVNGCSQYICECIPKDQCEIIELRELLPGEIIVNVEEGCCPTQKIECKPETCPKAPVNCQERFYEVKTIKEPGMCCSKHSCVPPKDLCIVQYELDEATKFTKTVGDKWTHAKEVCKQETCSYGPDGNAQVVSTLEQCLTDCAPGFSYQNLDKTKCCGKCVQTSCIFEQKLYEVNALWKSADNCTTYSCLKKDGQFLVTTSREVCPDVGSCLSHLLYQDGCCKRCKSEPLVEDKSSCLPVSLAESRTKEILKFPVQGHGTCVNADPIQGFTDCEGACSSGSKYNTLTDMHEKFCTCCSIKSYHPISVKMICDDGHTFTQKHEVPSNCGCSPCSEFSDSAIDVRMQQDAQSPLLQLLGNHRH
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B (Oligosaccharyl transferase subunit STT3B) (STT3-B) (EC 2.4.99.18) (Protein STAUROSPORIN AND TEMPERATURE SENSITIVE 3-LIKE B) (Q9FX21)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22923678}; Multi-pass membrane protein {ECO:0000269|PubMed:22923678}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1B
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD2
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dol-P-Glc:Glc
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
Sequence:
MGGKSEPAKSESMATKPDLLNTSFFSFKSLKLKTKQQELLLRISILGLVYILAFIARLFSVLRYESMIHEFDPYFNYRTTLFLTEKGFYEFWNWFDSESWYPLGRIIGGTLYPGLMVTAALIYWTLRFLRFFVHIREVCVLTAPFFASNTTLVAYFFGKELWDTGAGLVAAVLIAICPGYISRSVAGSYDNEAVAIFALLLTFYLFVKAVNTGSLAWALASAFGYFYMVSAWGGYVFIINLVPLYVLVLLITGRYSMRLYIAYNCMYILGMLLAMQIRFVGFQHVQSGEHMGAMGVFLLMQVFYFLDWVKYQLNDTKLFQTFLRITVTSAILVGGVAVGVGTASGYISPWTGRFYSLLDPTYAKDHIPIIASVSEHQPTAWSSFMFDYHILLFLFPAGLYFCFKRLTDATIFIVMYGLTSLYFAGVMVRLILVATPAVCLISAIAVSATIKNLTSLLRTKQKVSQTGSTKGAGSSKASSKVTLDQSQPFQKNGAIALLVGVFYLLSRYAIHCTWVTAEAYSSPSIVLAARGAHGNRIIFDDYREAYYWLRQNTATDAKIMSWWDYGYQITAMGNRTVIVDNNTWNNTHIATVGRAMSSYEDDAYDIMRSLDVNYVLVVFGGVTGYSSDDINKFLWMVRIGGGVFPVIKEPDYLVNGEFRVDKGASPKMLNCLMYKLCYYRFGELTTEYGKPPGYDRARGVEIGNKDIKLEHLEEAYTTSNWIVRIYRVKPPTNRL
Protein: Actin-related protein 2/3 complex subunit 3 (Arp2/3 complex 21 kDa subunit) (p21-ARC) (Q9Y7J4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Subcellular location: Cytoplasm, cytoskeleton, actin patch.
Interaction partners:
- Actin-related protein 2/3 complex subunit 1
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 2
- Actin
- Structure-specific endonuclease subunit slx4
- Actin-binding protein wsp1
- Protein dip1
Sequence:
MPAYHSSFLSLTDVPTTGNIAMLPLKTKFRGPAYPADESQMDIIDECIGLFRANCFFRNFEIKGPADRTLIYGTLFISECLGRVNGLNYRDAERQLNSLALENFSIPGSAGFPLNALYAPPLSPQDAEIMRTYLTQFRQELAYRLLSHVYATEKDHPSKWWTCFSKRRFMNKAL
Protein: Ammonium transporter 2 (AtAMT2) (Q9M6N7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High affinity ammonium transporter that may play an important role in moving ammonium between the apoplast and symplast of cells throughout the plant. Does not transport methylammonium.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12481062}; Multi-pass membrane protein {ECO:0000269|PubMed:12481062}.
Interaction partners:
- Nitrogen regulatory protein P-II homolog
- Protein NRT1/ PTR FAMILY 6.3
- Ferredoxin--nitrite reductase, chloroplastic
- Glutamine synthetase cytosolic isozyme 1-3
- Glutamine synthetase cytosolic isozyme 1-1
- High affinity nitrate transporter 2.4
- Glutamine synthetase, chloroplastic/mitochondrial
- Glutamine synthetase cytosolic isozyme 1-4
- Glutamine synthetase cytosolic isozyme 1-5
- High-affinity nitrate transporter 2.1
Sequence:
MAGAYDPSLPEVPEWLNKGDNAWQLTAATLVGLQSMPGLVILYASIVKKKWAVNSAFMALYAFAAVLLCWVLLCYKMAFGEELLPFWGKGGPAFDQGYLKGQAKIPNSNVAAPYFPMATLVYFQFTFAAITTILVAGSVLGRMNIKAWMAFVPLWLIFSYTVGAYSIWGGGFLYQWGVIDYSGGYVIHLSSGVAGFVAAYWVGPRPKADRERFPPNNVLLMLAGAGLLWMGWSGFNGGAPYAANLTSSIAVLNTNLSAATSLLVWTTLDVIFFGKPSVIGAIQGMVTGLAGVTPGAGLIQTWAAIIIGVVSGTAPWASMMIIHKKSALLQKVDDTLAVFYTHAVAGLLGGIMTGLFAHPDLCVLVLPLPATRGAFYGGNGGKQLLKQLAGAAFIAVWNVVSTTIILLAIRVFIPLRMAEEELGIGDDAAHGEEAYALWGDGEKFDATRHVQQFERDQEAAHPSYVHGARGVTIVL
Protein: Signal transducer and activator of transcription 5B (P51692)
Organism: Homo sapiens (Human)
Function: Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Binds to the GAS element and activates PRL-induced transcription. Positively regulates hematopoietic/erythroid differentiation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29844444}. Nucleus {ECO:0000269|PubMed:29844444}. Note=Translocated into the nucleus in response to phosphorylation. {ECO:0000269|PubMed:29844444}.
Interaction partners:
- Tyrosine-protein kinase JAK2
- Tyrosine-protein kinase JAK1
- Signal transducer and activator of transcription 3
- Epidermal growth factor receptor
- Tyrosine-protein kinase JAK3
- Receptor tyrosine-protein kinase erbB-4
- Interleukin-2 receptor subunit alpha
- Non-receptor tyrosine-protein kinase TYK2
- Crk-like protein
- Tyrosine-protein kinase ABL1
Sequence:
MAVWIQAQQLQGEALHQMQALYGQHFPIEVRHYLSQWIESQAWDSVDLDNPQENIKATQLLEGLVQELQKKAEHQVGEDGFLLKIKLGHYATQLQNTYDRCPMELVRCIRHILYNEQRLVREANNGSSPAGSLADAMSQKHLQINQTFEELRLVTQDTENELKKLQQTQEYFIIQYQESLRIQAQFGPLAQLSPQERLSRETALQQKQVSLEAWLQREAQTLQQYRVELAEKHQKTLQLLRKQQTIILDDELIQWKRRQQLAGNGGPPEGSLDVLQSWCEKLAEIIWQNRQQIRRAEHLCQQLPIPGPVEEMLAEVNATITDIISALVTSTFIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSLLKNENTRNDYSGEILNNCCVMEYHQATGTLSAHFRNMSLKRIKRSDRRGAESVTEEKFTILFESQFSVGGNELVFQVKTLSLPVVVIVHGSQDNNATATVLWDNAFAEPGRVPFAVPDKVLWPQLCEALNMKFKAEVQSNRGLTKENLVFLAQKLFNNSSSHLEDYSGLSVSWSQFNRENLPGRNYTFWQWFDGVMEVLKKHLKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSQERMFWNLMPFTTRDFSIRSLADRLGDLNYLIYVFPDRPKDEVYSKYYTPVPCESATAKAVDGYVKPQIKQVVPEFVNASADAGGGSATYMDQAPSPAVCPQAHYNMYPQNPDSVLDTDGDFDLEDTMDVARRVEELLGRPMDSQWIPHAQS
Protein: V-type proton ATPase subunit H (B0R0V8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- V-type proton ATPase subunit D
- V-type proton ATPase subunit F
- V-type proton ATPase subunit G
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit C 1-A
- ATPase H+-transporting V1 subunit E1b.
- V-type proton ATPase proteolipid subunit
- Vacuolar proton pump subunit B
- Vacuolar proton pump subunit B
- V-type proton ATPase 21 kDa proteolipid subunit c''
Sequence:
MDIRGAVDAAVPTNIIAAKAAEVRANKVNWQSYLQGQMISGEDCEFIKKFEVAGSEDKQAILTNEGHQCAKTFLNLMAHISKEQTVQYILTLIDDTLQENHQRVNIFFDYAKKTKNTAWSYFLPMLNRQDLFTVHMAARIIAKLAAWGRDLMEGSDLNYYFNWIKTQLSSQKLHGTGAEPGTGTISPSESSQYVQCVAGCLQLMLRVNEYRFAWVEADGVNCITAVLSNKCGFQLQYQMIFCVWLLAFSPQLCEQLRRYNVVPALSDILQESVKEKVTRIILAAFRNLLEKSAERETRQEYALAMIQCKVLKQLENLDQQKYDDEDITDDIKFLLERLGESVQDLSSFDEYSSELKSGRLEWSPVHKSEKFWRENAVRLNEKNYELLKILTRLLEVSDDPQVIAVAAHDVGEYVRHYPRGKRVIEQLGGKQLVMNHMHHEDQLVRYNALLAVQKLMVHNWEYLGKQLQSTEQTTPAVAARS