wanglab/gogpt-training-data huggingface dataset:
Protein: Protein OPG056 (Protein F12) (Q80HX6)
Organism: Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Function: Plays a role in intracellular enveloped virus (IEV) transport to the cell surface through microtubule transport. Together with protein OPG064/E2, forms a complex that interacts with host KLC2 (kinesin light chain isoform 2) to engage the kinesin-1 complex and thereby promote IEV trafficking.
Subcellular location: Virion membrane. Host endosome. Note=Associates with the membrane of IEV particles, but not intracellular mature virus (IMV), cell-associated enveloped virus (CEV) or EEV. Colocalizes with microtubules. {ECO:0000269|PubMed:20195521}.
Interaction partners:
Sequence:
MLNRVQILMKTANNYETIEILRNYLRLYIILARNEEGRGILIYDDNIDSIMSMMNITRLEVIGLTTHCTKLRSSPPIPMSRLFMDEIDHESYYSPKTSDYPLIDIIRKRSHEQGDIALALEQYGIENTDSISEINEWLSSKGLACYRFVKFNDYRKQMYRKFSRCTIVDSMIIGHIGHHYIWIKNLETYTRPEIDVLPFDIKYISRDELWARISSSLDQTHIKTIAVSVYGAITDNGPMPYMISTYPGNTFVNFNSVKNLILNFLDWIKDIMTSTRTIILVGYMSNLFDIPLLTVYWPNNCGWKIYNNTLISSDGARVIWMDAYKFSCGLSLQDYCYHWGSKPESRPFDLIKKSDAKRNSKSLVKESMASLKSLYEAFETQSGALEVLMSPCRMFSFSRIEDMFLTSVINRVSENTGMGMYYPTNDIPSLFIESSICLDYIIVNNQESNKYRIKSVLDIISSKQYPAGRPNYVKNGTKGKLYIALCKVTVPTNDHIPVVYHDDDNTTTFITVLTSVDIETAIRAGYSIVELGALQWDDNIPELKHGLLDSIKMIYDLNAVTTNNLLEQLIENINFNNSSIISLFYTFAISYCRAFIYSIMETIDPVYISQFSYKELYVSSSYKDINESMSQMVKL
Protein: Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (CD antigen CD117) (P05532)
Organism: Mus musculus (Mouse)
Function: Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KITLG/SCF binding, KIT can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the AKT1 signaling pathway by phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT also transmits signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is modulated by protein phosphatases, and by rapid internalization and degradation of the receptor. Activated KIT promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1.
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Note=Detected in the cytoplasm of spermatozoa, especially in the equatorial and subacrosomal region of the sperm head. {ECO:0000250}.
Interaction partners:
- Kit ligand
- Growth factor receptor-bound protein 2
- C-type lectin domain family 11 member A
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Tyrosine-protein phosphatase non-receptor type 11
- Stromal cell-derived factor 1
- Pro-epidermal growth factor
- GTPase NRas
- GTPase KRas
Sequence:
MRGARGAWDLLCVLLVLLRGQTATSQPSASPGEPSPPSIHPAQSELIVEAGDTLSLTCIDPDFVRWTFKTYFNEMVENKKNEWIQEKAEATRTGTYTCSNSNGLTSSIYVFVRDPAKLFLVGLPLFGKEDSDALVRCPLTDPQVSNYSLIECDGKSLPTDLTFVPNPKAGITIKNVKRAYHRLCVRCAAQRDGTWLHSDKFTLKVRAAIKAIPVVSVPETSHLLKKGDTFTVVCTIKDVSTSVNSMWLKMNPQPQHIAQVKHNSWHRGDFNYERQETLTISSARVDDSGVFMCYANNTFGSANVTTTLKVVEKGFINISPVKNTTVFVTDGENVDLVVEYEAYPKPEHQQWIYMNRTSANKGKDYVKSDNKSNIRYVNQLRLTRLKGTEGGTYTFLVSNSDASASVTFNVYVNTKPEILTYDRLINGMLQCVAEGFPEPTIDWYFCTGAEQRCTTPVSPVDVQVQNVSVSPFGKLVVQSSIDSSVFRHNGTVECKASNDVGKSSAFFNFAFKGNNKEQIQAHTLFTPLLIGFVVAAGAMGIIVMVLTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRDSFIFSKQEEQAEAALYKNLLHSTEPSCDSSNEYMDMKPGVSYVVPTKTDKRRSARIDSYIERDVTPAIMEDDELALDLDDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRNDSNYVVKGNARLPVKWMAPESIFSCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMVSPEHAPAEMYDVMKTCWDADPLKRPTFKQVVQLIEKQISDSTKHIYSNLANCNPNPENPVVVDHSVRVNSVGSSASSTQPLLVHEDA
Protein: Ectonucleotide pyrophosphatase/phosphodiesterase family member 5 (E-NPP 5) (NPP-5) (EC 3.1.-.-) (Q9EQG7)
Organism: Mus musculus (Mouse)
Function: Can hydrolyze NAD but cannot hydrolyze nucleotide di- and triphosphates. Lacks lysopholipase D activity. May play a role in neuronal cell communication (By similarity).
Subcellular location: Secreted {ECO:0000305}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MIPEFLLASCTLATLCHSAPFSLQPEEQKVLVVSFDGFRWDYLYKVPTPHFHYIMKNGVHVNQVTNVFITKTYPNHYTLVTGLFAENHGIVANDMFDPILNKSFSLEHMDIYDSKFWEEATPIWITNQRAGHASGAAMWPGADVKIHDSFPTYYLPYNESVSFEDRVAKIIEWFTAKDPINLGFLYWEEPDDTGHDVGPDSPLMGSVISDVDHKLGYLIKMLKRAKLWNNVNLIVTSDHGMTQCSKQRVIELDRYLDKEHYTLIDHSPVAAILPKEGKFDEVYDALAGAHPNLTVYKKEEIPERWHYKHNDRVQPIVAVADEGWYILQNKSDDFLLGNHGYDNALAEMHPIFLAHGPAFRKNFTKEAMNSTDLYSLLCHLLNLTALPHNGSFWNVQDLLSSATPKPIPYTQSTTLLLGSDKPGEDEQEESYPYYIGVSLGSIIAMVFFVVLIKHLIRSQVHTLQYRQVEVAQPLLQA
Protein: Probable indole-3-acetic acid-amido synthetase GH3.11 (EC 6.3.2.-) (Auxin-responsive GH3-like protein 11) (OsGH3-11) (P0C0M3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May catalyze the synthesis of indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism for the plant to cope with the presence of excess auxin.
Interaction partners:
- Indole-3-acetic acid-amido synthetase GH3.8
Sequence:
MDDHNLDYKGSGALEELEMLTVNAKEAQELILTKILERNQATEYLSKFMNGSTNISAFKRHVPVVTYDKVHPYILRIATGEESSILCGEYILELLRSSGTSRGEPRLMPSILKDLDRRTYLYSLIMPIMNKYISGLGEGKAMYLLFVKAETLTDSGIPVRSVLTSYYKSPHFLHRKHDLYNNYTSPDEVILCPDSQQSMYCQLLCGLVERQHVLRIGAVFASAFLRSISFLEQHWRDLVNDIRIGQLNSSITSPACRLAMLNFLALPNPELADQVEAICSCGSWKGILGRLWPNVKYIEAVLTGTMAQYIPMLEFYGGGAIPFVCTMYASSESYFGVNLSPLCSPADVSYTILPNMAYFEFIPLEDGLRLTDHEEVIENDKLVSLVDVKVGCYYELVVTTFSGLYRYRVGDVLQVTGFYNRAPQFKFICRRNVILSIDSDKTNEEDLHNSVTTAKKILENQNYLLLEYTSYTDISTVPGHYVLFWEIKSTHDERPAPLDAQLLESCCAAVEESLDYVYRRCRAHDRSIGPLEIRLVEAGAFDALMDLLVSHGSSINQYKTPRCIESSLALKLLNSKVIACFFSPQDPECGM
Protein: Tubulin alpha chain (Q1ZYQ1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGVDSVEAEAEEGEEY
Protein: Cd80 molecule (G3V671)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
- Cytotoxic T-lymphocyte protein 4
- T-cell-specific surface glycoprotein CD28
- T-lymphocyte activation antigen CD86
- Programmed cell death 1 ligand 1
- CD40 ligand
- Inducible T-cell costimulator
- Tumor necrosis factor receptor superfamily, member 5, isoform CRA_a.
- Intercellular adhesion molecule 1
- CD276 antigen
- T-cell surface glycoprotein CD4
Sequence:
MAYSCQLMQESPLLGFPRLRFIHLFVLLLVGLFQISSGIVGQVSKSVREKALLSCDYKFCSEEQSIHRIYWQKHDKMVLSVISGVPEVWPEYKNRTVYDIANNYSFSLLGLILSDRGTYTCVVQRYEGGSYVVKHLTTVELSVRADFPTPNITESGNPSADIKRITCFASGGFPKPRLSWLENGRELNGINTTISQDPESELYTISSQLDFNTTYDHFIDCFIEYGDAHVSQNFTWEKPPEDPPDEKQTIPFAWAGSDAVKAIIIFFIAITVIAVIAAIAIIIFCITVKFRKHRRCFRRRNEASRETNKNLYIGPVEAAAEQTV
Protein: Serine/arginine-rich splicing factor 2 (Splicing component, 35 kDa) (Splicing factor SC35) (SC-35) (Splicing factor, arginine/serine-rich 2) (Q6PDU1)
Organism: Rattus norvegicus (Rat)
Function: Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with pre-mRNA. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Serine/arginine-rich splicing factor 1
- Serine/arginine-rich splicing factor 3
- Serine/arginine-rich splicing factor 9
- SRSF protein kinase 1
- Splicing factor U2AF subunit
- U2 small nuclear RNA auxiliary factor 1
- Serine/arginine-rich splicing factor 7
- Serine/arginine-rich splicing factor 5
- Heterogeneous nuclear ribonucleoprotein H
- Zinc finger
Sequence:
MSYGRPPPDVEGMTSLKVDNLTYRTSPDTLRRVFEKYGRVGDVYIPRDRYTKESRGFAFVRFHDKRDAEDAMDAMDGAVLDGRELRVQMARYGRPPDSHHSRRGPPPRRYGGGGYGRRSRSPRRRRRSRSRSRSRSRSRSRSRYSRSKSRSRTRSRSRSTSKSRSARRSKSKSSSVSRSRSRSRSRSRSRSPPPVSKRESKSRSRSKSPPKSPEEEGAVSS
Protein: tRNA uridine(34) hydroxylase (EC 1.14.-.-) (tRNA hydroxylation protein O) (P67330)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Interaction partners:
Sequence:
MAKDIRVLLYYLYTPIENAEQFAADHLAFCKSIGLKGRILVADEGINGTVSGDYETTQKYMDYVHSLPGMEELWFKIDEENEQAFKKMFVRYKKEIVHLGLEDNDFDNDINPLETTGAYLSPKEFKEALLDKDTVVLDTRNDYEYDLGHFRGAIRPDIRNFRELPQWVRDNKEKFMDKRVVVYCTGGVRCEKFSGWMVREGYKDVGQLHGGIATYGKDPEVQGELWDGKMYVFDERIAVDVNHVNPTIVGKDWFDGTPCERYVNCGNPFCNRRILTSEENEDKYLRGCSHECRVHPRNRYVSKNELTQAEVIERLAAIGESLDQAATV
Protein: Stomatin-like protein, putative (Q57VW1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- ATP synthase subunit beta
- Mitochondrial ATP-dependent zinc metallopeptidase, putative
- Prohibitin
- Prohibitin
Sequence:
MLRSLVHSSRTLSLPGTHVAPTCIVYTPPPTLPRGTTASFDCTAAGVRAISLVGSGLRRCGVSVSSGCGVSATSLGGTFRMYHSGSAGAGGYNYSQPPSPYGGAASNYMGGGYYAGSGDPNYSIDNNSNAVAAGSGGNAGGGAGGGGPVGSGRLPFVSRPFRSPVHPSSFIERVPRNTILNIVPQGRQYVVERLGRYHRTLDPGWWFVIPFVDKIRYAYSVKEQGIEIPNQSAITCDNVMVEIDGVLFLRIVDTCKASYNIENPIYNLLNLAQTTMRSEIGRLDLDTLFRERASLNKNIVEVLRSEAADWGIECKRYEIRDITVSELVRRSMDLQADAERRKRQLILQSEGEAQAGINRAGGLRRAQRLAARAQKYATVLRAEAEAAAMALKADAVGRSVGTVANAFNASPNPQSFRDAVALRVAEEYIEKFGELARRSNTVVLGGGGSGLPVSDPAAFTAQALSVFRAVSDSCGGNVGDAKVPAVGADPNIMNSSLGSGVGGTVDSNSVDNNSSSDSTSDDNNNNSSGFR
Protein: tRNA threonylcarbamoyladenosine dehydratase 2 (EC 6.1.-.-) (t(6)A37 dehydratase 2) (P36101)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine.
Subcellular location: Mitochondrion outer membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVEKDTWKLITATALFTVAVTTITDYAWTSWQAQKQVIAQQKNKNKGGQTKSDTDKYHQYDEQFIRQSLKNNVEFLGEDTIEKLSNQYVVVVGAGGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGTPKVECLRRHMREIAPWCEIDPINELWTLQNGERLTLGNGTPDFIVDCIDNIDTKVDLLEFAYNHGIKVISSMGASAKSDPTKLNVGDLATTEEDPLARVVRRKLKKRGILSGIPVVFSAEKPDPKKAKLLPLPDEEYERGKVDELSALKDFRVRILPVLGTMPSLFGLTITTWILSNISDKPLEPVEGKNRIKVYDGIYQSLAGQMSRVGIPSQRIPLALKDVSYLVEEVFKGKSPISGISTRLTLTKWDPSKPISLQNVVVLTKNEQKVHEDRVLKGKESLQDVYDAKVLKLVSQRFREEAYYSQFR
Protein: Holocarboxylase synthetase (A0A8I6A968)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLITLCYLYLWARWGRRPAALVLSTVRRLRASRCSFTFCRAAAQPGGARVCLSRGGRVFCVGESQSVDDLNKWALFLVSPFILEAEHIAFVTESIWVQGTSFQEPSSSETVVKWSDCCLPLACRPGDPYQLIAKASVDNFSKLGVAFMEDRLQMDNGLIAQKIVSVHLKDPALKELSKASNKQVQAPLPSPEASLEAQPAQGVMEQAGQGDWKAAGEGPSPQRRGCAPVSESAADGDPGQGSTELCQLHLSSCHECLELENSTIESVRCASAENIPDLPHDCSSSVEGTAGELCPERKGKRVNISGKAPNILLYVGSGSEEALGQLQQVRSVLTDCVDTDSYTLYHLLEDSALRDPWPDNCLLLVIASRDPIPKGIHHRFMAYLSQGGKVLGLSSSFTFGDLRVARRDVLRNTAQNLVFSKADGSEVRLSVLSSGYVYEEGPSLGRLQGHLENEDKDKMIVHVPFGTHGGEAILCQVHLELPPSAPLVQTTDDFNVLKSSNTRRLEVLKEILTALGLSCDAPQAPALTPLYLLLAAEEIQGPFMQWLARHVDPEGVIKSSKLSLKFVSSYTSEAEITPSSIPVVTDPEGFSSEHFNLETYRQNLQSTRLGRVILFAEVTSTTMSLLDGLMFEMPQEMGLIAIAVRQTQGKGRGPNAWLSPVGCALSTLLVSIPLRSQLGQRIPFVQHLMSLAVVEAVRSIPEYEDINLRVKWPNDIYYSDLMKIGGVLVNSTLVGETFYILIGCGFNVTNSNPTICINDLIEEHNKQNKAGLKPLQADCLIARAVTVLEKLIDRFQDQGPDGVLPLYYKYWAHSGQQVRLGSSEGPAVSIVGLDDSGFLQVHQEGGGVVSVHPDGNSFDMLRNLIVPKRP
Protein: RAB30, member RAS oncogene family (E9PNB9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSMEDYDFLFKIVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEINGEKVKLQIWDTAGQERFRSITQSYYRSANALILTYDITCEESFRCLPEWLREIEQYASNKVITVLVGK
Protein: Translation elongation factor EF1B/ribosomal protein S6 family protein (A8MRC4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAAFPNLNSDAGLKKLDEHLLTRSYITGYQASKDDITVFAALAKPPTSQYVNASRWYNHIDALLRISGVSAEGSGVIVEGSAPITEEAVATPPAADSKDAAADEEDDDDVDLFGEETEEEKKAAEERAASVKASTKKKESGKSSVLIDIKPWDDETDMKKLEEAVKSIQMEGLFWGASKLVPVGYGIKKLQILCTIVDDLVSIDTMIEEQLTVEPINEYVQSCDIVAFNKICKMEKASRNVCVHVVWFFFFFYIQFPKFL
Protein: Immunoglobulin kappa variable 2D-28 (Ig kappa chain V-II region FR) (Ig kappa chain V-II region GM607) (Ig kappa chain V-II region MIL) (Ig kappa chain V-II region TEW) (P01615)
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:
MRLPAQLLGLLMLWVSGSSGDIVMTQSPLSLPVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKPGQSPQLLIYLGSNRASGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQALQTP
Protein: Son of sevenless homolog 2 (SOS-2) (Q07890)
Organism: Homo sapiens (Human)
Function: Promotes the exchange of Ras-bound GDP by GTP.
Interaction partners:
- SHC-transforming protein 1
- Growth factor receptor-bound protein 2
- Epidermal growth factor receptor
- Tyrosine-protein phosphatase non-receptor type 11
- GRB2-associated-binding protein 2
- GTPase KRas
- GTPase HRas
- GRB2-associated-binding protein 1
- Son of sevenless homolog 1
- GTPase NRas
Sequence:
MQQAPQPYEFFSEENSPKWRGLLVSALRKVQEQVHPTLSANEESLYYIEELIFQLLNKLCMAQPRTVQDVEERVQKTFPHPIDKWAIADAQSAIEKRKRRNPLLLPVDKIHPSLKEVLGYKVDYHVSLYIVAVLEYISADILKLAGNYVFNIRHYEISQQDIKVSMCADKVLMDMFDQDDIGLVSLCEDEPSSSGELNYYDLVRTEIAEERQYLRELNMIIKVFREAFLSDRKLFKPSDIEKIFSNISDIHELTVKLLGLIEDTVEMTDESSPHPLAGSCFEDLAEEQAFDPYETLSQDILSPEFHEHFNKLMARPAVALHFQSIADGFKEAVRYVLPRLMLVPVYHCWHYFELLKQLKACSEEQEDRECLNQAITALMNLQGSMDRIYKQYSPRRRPGDPVCPFYSHQLRSKHLAIKKMNEIQKNIDGWEGKDIGQCCNEFIMEGPLTRIGAKHERHIFLFDGLMISCKPNHGQTRLPGYSSAEYRLKEKFVMRKIQICDKEDTCEHKHAFELVSKDENSIIFAAKSAEEKNNWMAALISLHYRSTLDRMLDSVLLKEENEQPLRLPSPEVYRFVVKDSEENIVFEDNLQSRSGIPIIKGGTVVKLIERLTYHMYADPNFVRTFLTTYRSFCKPQELLSLLIERFEIPEPEPTDADKLAIEKGEQPISADLKRFRKEYVQPVQLRILNVFRHWVEHHFYDFERDLELLERLESFISSVRGKAMKKWVESIAKIIRRKKQAQANGVSHNITFESPPPPIEWHISKPGQFETFDLMTLHPIEIARQLTLLESDLYRKVQPSELVGSVWTKEDKEINSPNLLKMIRHTTNLTLWFEKCIVEAENFEERVAVLSRIIEILQVFQDLNNFNGVLEIVSAVNSVSVYRLDHTFEALQERKRKILDEAVELSQDHFKKYLVKLKSINPPCVPFFGIYLTNILKTEEGNNDFLKKKGKDLINFSKRRKVAEITGEIQQYQNQPYCLRIEPDMRRFFENLNPMGSASEKEFTDYLFNKSLEIEPRNCKQPPRFPRKSTFSLKSPGIRPNTGRHGSTSGTLRGHPTPLEREPCKISFSRIAETELESTVSAPTSPNTPSTPPVSASSDLSVFLDVDLNSSCGSNSIFAPVLLPHSKSFFSSCGSLHKLSEEPLIPPPLPPRKKFDHDASNSKGNMKSDDDPPAIPPRQPPPPKVKPRVPVPTGAFDGPLHSPPPPPPRDPLPDTPPPVPLRPPEHFINCPFNLQPPPLGHLHRDSDWLRDISTCPNSPSTPPSTPSPRVPRRCYVLSSSQNNLAHPPAPPVPPRQNSSPHLPKLPPKTYKRELSHPPLYRLPLLENAETPQ
Protein: C-C motif chemokine 15 (Chemokine CC-2) (HCC-2) (Leukotactin-1) (LKN-1) (MIP-1 delta) (Macrophage inflammatory protein 5) (MIP-5) (Mrp-2b) (NCC-3) (Small-inducible cytokine A15) [Cleaved into: CCL15(22-92); CCL15(25-92); CCL15(29-92)] (Q16663)
Organism: Homo sapiens (Human)
Function: Chemotactic factor that attracts T-cells and monocytes, but not neutrophils, eosinophils, or B-cells. Acts mainly via CC chemokine receptor CCR1. Also binds to CCR3. CCL15(22-92), CCL15(25-92) and CCL15(29-92) are more potent chemoattractants than the CCL15.
Subcellular location: Secreted.
Interaction partners:
- C-C motif chemokine 2
- C-C chemokine receptor type 1
- C-C chemokine receptor type 3
- C-C chemokine receptor type 2
- C-C chemokine receptor type 5
- C-X-C chemokine receptor type 4
- C-C motif chemokine ligand 4 like 2.
- C-X-C chemokine receptor type 5
- C-X-C chemokine receptor type 6
- Guanine nucleotide-binding protein G
Sequence:
MKVSVAALSCLMLVAVLGSQAQFTNDAETELMMSKLPLENPVVLNSFHFAADCCTSYISQSIPCSLMKSYFETSSECSKPGVIFLTKKGRQVCAKPSGPGVQDCMKKLKPYSI
Protein: E3 ubiquitin-protein ligase NRDP1 (EC 2.3.2.27) (RING finger protein 41) (RING-type E3 ubiquitin transferase NRDP1) (Q7ZW16)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as E3 ubiquitin-protein ligase and regulates the degradation of target proteins.
Interaction partners:
- Ubiquitin-specific peptidase 8
- Erb-b2 receptor tyrosine kinase 3b.
- Ubiquitin carboxyl-terminal hydrolase
- Ankyrin repeat and SOCS box-containing 6.
- Vacuolar protein sorting-associated protein 52 homolog
- Epidermal growth factor receptor precursor.
- C-type lectin domain-containing 16A.
- Dual E2 ubiquitin-conjugating enzyme/E3 ubiquitin-protein ligase BIRC6
Sequence:
MGYDVTRFQGEVDEDLLCPICSGVLEEPVRAPHCEHAFCNACITQWFAQQQICPVDRTVVTLAHLRPVPRIMRNMLSKLQISCDNAGFGCTATLRLDQLQSHLKDCEHNPKRPVTCEEGCGLEMPKDEMPNHNCIKHLRSVVQQQQTKIADLEKTAAEHKHQLAEQKRDIQLLKAYMRAIRSANPNLQNLEESIEYNEILEWVNSLQPARVTRWGGMISTPDAVLQAVIKRSLIDSGCPLSIVNDLIENAHERNWPQGLATLETRQMNRRYYENYVAKRIPGKQAVVVMACENQHMGEDMILEPGLVMIFAHGVEEIL
Protein: Alpha-actinin-1 (Alpha-actinin cytoskeletal isoform) (F-actin cross-linking protein) (Non-muscle alpha-actinin-1) (Q3B7N2)
Organism: Bos taurus (Bovine)
Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P12814}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:P12814}. Cell membrane {ECO:0000250|UniProtKB:P12814}. Cell junction {ECO:0000250|UniProtKB:Q9Z1P2}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q7TPR4}. Note=Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and central reticular structures. {ECO:0000250|UniProtKB:Q7TPR4}.
Interaction partners:
- Vinculin
- Actin, cytoplasmic 2
- Actin, cytoplasmic 1
- Zyxin
- Catenin alpha-1
- Parvin beta
- Alpha-actinin-4
- Synovial sarcoma, X breakpoint 2 interacting protein
- Catenin alpha 3
- Catenin alpha-2
Sequence:
MDHYDSQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRAPENTMHAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNAWGCLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLRQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERLAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWDHVRQLVPRRDQALTEEHARQQHNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLNHLRQYEKSIVNYKPKIDQLEGDHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYDIGNDPQGEAEFARIMSIVDPNRLGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITVDELRRELPPDQAEYCIARMAPYTGPDAVPGALDYMSFSTALYGESDL
Protein: Fumarate reductase 1 (FRDS1) (EC 1.3.1.6) (FAD-dependent oxidoreductase) (NADH-dependent fumarate reductase) (Soluble fumarate reductase, cytoplasmic isozyme) (P32614)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Irreversibly catalyzes the reduction of fumarate to succinate. Together with the second isozyme of soluble fumarate reductase (OSM1), essential for anaerobic growth. Involved in maintaining redox balance. Reduction of fumarate is the main source of succinate during fermentation, and under anaerobic conditions, the formation of succinate is strictly required for the reoxidation of FADH(2).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8946166, ECO:0000269|PubMed:9587404}.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Fumarate hydratase, mitochondrial
- Succinate dehydrogenase cytochrome b subunit
- Mitochondrial inner membrane protein SHH3
- 2-oxoglutarate dehydrogenase, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate dehydrogenase assembly factor 2, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
Sequence:
MSLSPVVVIGTGLAGLAAANELVNKYNIPVTILEKASSIGGNSIKASSGINGACTETQRHFHIEDSPRLFEDDTIKSAKGKGVQELMAKLANDSPLAIEWLKNEFDLKLDLLAQLGGHSVARTHRSSGKLPPGFEIVSALSNNLKKLAETKPELVKINLDSKVVDIHEKDGSISAVVYEDKNGEKHMVSANDVVFCSGGFGFSKEMLKEYAPELVNLPTTNGQQTTGDGQRLLQKLGADLIDMDQIQVHPTGFIDPNDRSSSWKFLAAESLRGLGGILLNPITGRRFVNELTTRDVVTAAIQKVCPQEDNRALLVMGEKMYTDLKNNLDFYMFKKLVQKLTLSQVVSEYNLPITVAQLCEELQTYSSFTTKADPLGRTVILNEFGSDVTPETVVFIGEVTPVVHFTMGGARINVKAQVIGKNDERLLKGLYAAGEVSGGVHGANRLGGSSLLECVVFGRTAAESIANDRK
Protein: Liprin-gamma, isoform D (A8DYM1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTADNQPLQQQLQHHQHRSPAYPGKPAEAAGGVPQQQQQQQQLPNGIGSSHCNSNSNGISSTCNSGTAMIHANNSNLIAAGHLAQAAGPAHNAPSSGSALNAVDKRNANLSEPDQDLPPNLNVNLSPNPSLALGAPHSPTSAASAALLLLESCDGNRNDESRFHHLHSAPRPEATMKLREENDRLNAELLRLRRLLELSTDGAVGGVDTAPEMEAVASGEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTNAKISGDRDRERFQLLKQARDEAERSLALAQQLSARDLQLQRLQEQLQEARRQLTGCLSDQESLHSFAPLTPPSAASGMLSQMAAASGMGGGLAGMRGTTEDSGRGNSLSAFSGSLSGGSGATAGDRNSCSNDSGLRNSSDRESTGGELNFSDGTCDNGPCITVDPDSISLVSSQNMYQFGTPKERSPTLSPLNSAAYSRSVEQLGSPVDPEGPGNGAISRKFANASKSGPLGARNGRGGTWGSISRVFARSRNKNKALSADGVTEYADYSWNPLTEEGYAEKLRLLREASQLPIDRWRATQVLAWLEVALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEEQRRPEMVRYPLITQLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLRIVKYDRQTLAMRRVQSETVDTDPIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALILPARYLIYCQMEEFQMEASRQLAKLQGH
Protein: CAMPATH-1 antigen (CDw52) (Cambridge pathology 1 antigen) (Epididymal secretory protein E5) (Human epididymis-specific protein 5) (He5) (CD antigen CD52) (P31358)
Organism: Homo sapiens (Human)
Function: May play a role in carrying and orienting carbohydrate, as well as having a more specific role.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- CD48 antigen
- Sialic acid-binding Ig-like lectin 10
- T-cell surface antigen CD2
- T-cell surface glycoprotein CD3 epsilon chain
- Leukocyte surface antigen CD53
- B-lymphocyte antigen CD19
- Receptor-type tyrosine-protein phosphatase C
- T-cell surface glycoprotein CD3 delta chain
Sequence:
MKRFLFLLLTISLLVMVQIQTGLSGQNDTSQTSSPSASSNISGGIFLFFVANAIIHLFCFS