wanglab/gogpt-training-data huggingface dataset:
Protein: T-box transcription factor TBX18 (T-box protein 18) (Q9EPZ6)
Organism: Mus musculus (Mouse)
Function: Acts as transcriptional repressor involved in developmental processes of a variety of tissues and organs, including the heart, the coronary vessels, the ureter, and the vertebral column. Required for embryonic development of the sino atrial node (SAN) head area.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201, ECO:0000269|PubMed:17584735}.
Interaction partners:
- Histone deacetylase 2
- Short stature homeobox protein 2
- Transcription factor 21
- Homeobox protein Nkx-2.5
- Wilms tumor protein homolog
- T-box transcription factor TBX15
- Myc proto-oncogene protein
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
- Histone deacetylase 5
- ETS translocation variant 3
Sequence:
MAEKRRGSPCSMLSLKAHAFSVEALIGAEKQQQLQKKRRKLATEEAAGAVEDAGCSRSGGAGEHGCSEADEEAAAPPPAAGAASGPARSCADAERSCGSRGAAGSCEDGFLQGASPLASPGGSPKGSPVPGLARPGTPLPAPQAPRVDLQGAELWKRFHEIGTEMIITKAGRRMFPAMRVKISGLDPHQQYYIAMDIVPVDNKRYRYVYHSSKWMVAGNADSPVPPRVYIHPDSPASGETWMRQVISFDKLKLTNNELDDQGHIILHSMHKYQPRVHVIRKDCGDDLSPIKPVPSGEGVKAFSFPETVFTTVTAYQNQQITRLKIDRNPFAKGFRDSGRNRMGLEALVESYAFWRPSLRTLTFEDIPGIPKQGNTSSSALLQGTGNAVPATHPHLLSGSSCSSPAFHLGPNTSQLCSLTPADYSACARSGLALNRYSTSLAETYSRLTNQSSETFAPPRTPSYVSVSSNPSVNMSMGGTDGDTFSCPQTSLSMQISGMSPQLQYIMPSPSGNAFAANQTHQSSYNTFRLHSPCALYGYNFSTSPKLAASPEKIVSSQGSFLGSSPSGTMTDRQMLPPVEGVHLLSSGGQQSFFDSRTLGSLTLPSSQVSAHMV
Protein: Retinoic acid receptor beta (RAR-beta) (HBV-activated protein) (Nuclear receptor subfamily 1 group B member 2) (RAR-epsilon) (P10826)
Organism: Homo sapiens (Human)
Function: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence or presence of hormone ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. The RXRA/RARB heterodimer can act as a repressor on the DR1 element and as an activator on the DR5 element. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:28167758}. Cytoplasm {ECO:0000269|PubMed:28167758}.; SUBCELLULAR LOCATION: [Isoform Beta-1]: Nucleus.; SUBCELLULAR LOCATION: [Isoform Beta-2]: Nucleus.; SUBCELLULAR LOCATION: [Isoform Beta-4]: Cytoplasm.
Interaction partners:
- Retinoic acid receptor RXR-alpha
- Retinoic acid receptor RXR-beta
- Retinoic acid receptor alpha
- Nuclear receptor coactivator 1
- Retinoic acid receptor RXR-gamma
- Cellular retinoic acid-binding protein 2
- Arginine--tRNA ligase, cytoplasmic
- Mediator of RNA polymerase II transcription subunit 1
- Retinoic acid receptor gamma
- Ras association domain-containing protein 1
Sequence:
MTTSGHACPVPAVNGHMTHYPATPYPLLFPPVIGGLSLPPLHGLHGHPPPSGCSTPSPATIETQSTSSEELVPSPPSPLPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMIYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKETSKQECTESYEMTAELDDLTEKIRKAHQETFPSLCQLGKYTTNSSADHRVRLDLGLWDKFSELATKCIIKIVEFAKRLPGFTGLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFTFANQLLPLEMDDTETGLLSAICLICGDRQDLEEPTKVDKLQEPLLEALKIYIRKRRPSKPHMFPKILMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGHEPLTPSSSGNTAEHSPSISPSSVENSGVSQSPLVQ
Protein: Protein kinase C iota type (EC 2.7.11.13) (Atypical protein kinase C-lambda/iota) (aPKC-lambda/iota) (Heart and soul protein) (nPKC-iota) (Q90XF2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway (By similarity). Is required for the formation and maintenance of the zonula adherens during early epithelial development and plays a critical role in organ morphogenesis and in regulating the orientation of cell division.
Interaction partners:
- Par-3 family cell polarity regulator alpha, b.
- LLGL scribble cell polarity complex component 2
- Par-6 family cell polarity regulator gamma b
- Par-6 family cell polarity regulator alpha.
- Par-3 family cell polarity regulator.
- Par-6 partitioning defective 6 homolog beta
- Par-6 family cell polarity regulator gamma a.
- LLGL scribble cell polarity complex component 1.
- Protein PALS1
- Serine/threonine kinase 11
Sequence:
MPTLRDSTMSHPGENPHQVRVKAYYRGDIMITHFEPSISYEGLCNEVRDMCSMDNDQLFTMKWIDEEGDPCTVSSQLELEEALRLYELNKDSELIIHVFPCVPEKPGMPCPGEDKSIYRRGARRWRKLYYATGHAFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTVECGRQVIQDPMIGRIDPGSTHPEHPDQVLGKKNSTESINHEGEEHEAVGSRESGKAVSSLGLIDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKGFLNKESKERLGCHPQTGFADIMAHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDAQFTNEPIQLTPDDDDAVKKIDQSEFEGFEYINPLLMSAEECV
Protein: Paxillin (Q8VI36)
Organism: Mus musculus (Mouse)
Function: Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P49023}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P49023}. Cytoplasm, cell cortex {ECO:0000269|PubMed:8940124}. Note=Colocalizes with integrins at the cell periphery. Colocalizes with PXN to membrane ruffles and the leading edge of migrating cells (By similarity). {ECO:0000250|UniProtKB:P49023}.
Interaction partners:
- Adapter molecule crk
- Protein-tyrosine kinase 2-beta
- Breast cancer anti-estrogen resistance protein 1
- ARF GTPase-activating protein GIT1
- Proto-oncogene tyrosine-protein kinase Src
- Focal adhesion kinase 1
- Alpha-parvin
- Scaffold protein ILK
- Vinculin
- Talin-1
Sequence:
MDDLDALLADLESTTSHISKRPVFLSEEPPYSYPTGNHTYQEIAVPPPVPPPPSSEALNGTVLDPLDQWQPSGSRYAHQQPPSPLPVYSSSAKNSSASNTQDGVGSLCSRAGEEEHVYSFPNKQKSAEPSPTVMSSSLGSNLSELDRLLLELNAVQHSPPGFPADEAESSPPLPGALSPLYGIPENNTPLGGKAGPLVKEKPKRNGGRGLEDVRPSVESLLDELESSVPSPVPAITVNQGEMSSPQRVTSSQQQTRISASSATRELDELMASLSDFKMQGLEQRVDGERPWAAGWPPSSRQSSPEGQDEGGFMAQGKTGSSSPPGGLSKPGSQLDSMLGSLQSDLNKLGVATVAKGVCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEKDYHSLFSPRCYYCNGPILDKVVTALDRTWHPEHFFCAQCGAFFGPEGFHEKDGKAYCRKDYFDMFAPKCGGCARAILENYISALNTLWHPECFVCRECFTPFVNGSFFEHDGQPYCEVHYHERRGSLCSGCQKPITGRCITAMAKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCQSCFVKLFC
Protein: Exocyst complex component EXO84 (Q59XM1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Plays a role in both the assembly of the exocyst and the polarization of this complex to specific sites of the plasma membrane for exocytosis. Also involved in assembly of the spliceosome (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Note=Cell periphery. The polarization of EXO84 requires actin cables (By similarity). {ECO:0000250}.
Interaction partners:
- Exocyst complex component SEC5
- Exocyst complex component SEC15
- Exocyst complex protein EXO70
- Exocyst complex component Sec8
- Exocyst subunit
- SNARE-binding exocyst subunit
- Rcy1p
- GTP-Rho binding exocyst subunit
- Ras-related protein SEC4
- Rab guanine nucleotide exchange factor SEC2
Sequence:
MDNLDPNSSLQVEKLRNRKSRAVWQNNNTTTHNNPYANLSTGEKSRSRHNTGSSYVSPYGGGNGEENAYTGNNNKSNTSGNLLQVPGAGGGGDLNSNKKQSRRMSIHVSARQHGRSFSQTGPIDMANLPALPKIGGVTTSGVGGAGGDVMTRTGGLTIEQKIFKELSQGSAAEVDDYYKTLLKQKNLITRDIKDNINQNQKNILQLTKDLKETQEELIELRGTTKELYEVLGYFKESAQRRLELEFEPETQKELHSPQKSNQLGIPSNKKKDRSSIMVLKKMWDSQLQSLFKHVDGASKFVQPLPNRHIVAESGRWFEVNVGNWKPSYPTHLFIFNDLILIAVKKSSSSSQEPTTGGSNGGSKSRLQAVQCWPLTQVSLQQIKSPKKDDDKMYFINLKSKSLSYVYSTDRYDHFVKVTEAFNKGRNEMIQSERLLDSRLSSPSNNNGDSKEEKRQLRESLRNSGNYKEGVTDDAGGAATGGGRKSAGTPNRNSTDYVLHDISARVHSRNRSQDLGNNFKLANNGKSQFFNEIKTLEDRLDDVDVEISHNQYAEAVELISIIESKLRNIENALTNQRNGGKNVNIADELLLLDVSKLKIKNRKENVSNGLIFDLQHNIAKLKQDDIDNILTLFDNLEQLDRGVQGYLDSMSAYLSTTVSKLIVGLQGSTKIDVVNYLSNLMVINVSIVKRTIQTYEQIIAPILKRHGDVDSSGLINWCIDEFTKLCKQIKKHLYGTLLISSGINMETDEPIYKVKERKLYDNFLKIMQPQLEELKSVGLNVDYIFESILNLE
Protein: Proprotein convertase subtilisin/kexin type 5 (A0A669KA35)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MGWGSRCCCPGRLDLLCVLALLGGCLLPVCRTRVYTNHWAVKIAGGFPEANRIASKYGFINIGQIGALKDYYHFYHSRTIKRSVISSRGTHSFISMEPKVEWIQQQVVKKRTKRDYDFSRAQSTYFNDPKWPSMWYMHCSDNTHPCQSDMNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMPRYDASNENKHGTRCAGEVAAAANNSHCTVGIAFNAKIGGVRMLDGDVTDMVEAKSVSFNPQHVHIYSASWGPDDDGKTVDGPAPLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDHCSCDGYTNSIYTISISSTAESGKKPWYLEECSSTLATTYSSGESYDKKIITTDLRQRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSRAGHLNANDWKTNAAGFKVSHLYGFGLMDAEAMVMEAEKWTTVPRQHVCVESTDRQIKTIRPNSAVRSIYKASGCSDNPNRHVNYLEHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLFDHSMEGFKNWEFMTIHCWGERAAGDWVLEVYDTPSQLRNFKTPGKLKEWSLVLYGTSVQPYSPTNEFPKVERFRYSRVEDPTDDYGTEDYAGPCDPECSEVGCDGPGPDHCNDCLHYYYKLKNNTRICVSSCPPGHYHADKKRCRKCAPNCESCFGSHGDQCMSCKYGYFLNEETNSCVTHCPDGSYQDTKKNLCRKCSENCKTCTEFHNCTECRDGLSLQGSRCSVSCEDGRYFNGQDCQPCHRFCATCAGAGADGCINCTEGYFMEDGRCVQSCSISYYFDHSSENGYKSCKKCDISCLTCNGPGFKNCTSCPSGYLLDLGMCQMGAICKDGEYVDEHGHCQTCEASCAKCQGPTQEDCTTCPMTRIFDDGRCVSNCPSWKFEFENQCHPCHHTCQRCQGSGPTHCTSCGADNYGREHFLYQGECGDSCPEGHYATEGNTCLPCPDNCELCHSVHVCTRCMKGYFIAPTNHTCQKLECGQGEVQDPDYEECVPCEEGCLGCSLDDPGTCTSCAMGYYRFDHHCYKTCPEKTYSEEVECKACDSNCGSCDQNGCYWCEEGFFLLGGSCVRKCGPGFYGDQEMGECESCHRACETCTGPGHDECSSCQEGLQLLRGMCVHATKTQEEGKFWNEAVSTANLSVVKSLLQERRRWKVQIKRDILRKLQPCHSSCKTCNGSATLCTSCPKGAYLLAQACVSSCPQGTWPSVRSGSCENCTEACAICSGADLCKKCQMQPGHPLFLHEGRCYSKCPEGSYAEDGICERCSSPCRTCEGNATNCHSCEGGHVLHHGVCQENCPERHVAVKGVCKHCPEMCQDCIHEKTCKECTPEFFLHDDMCHQSCPRGFYADSRHCVPCHKDCLECSGPKADDCELCLESSWVLYDGLCLEECPAGTYYEKETKECRDCHKSCLTCSSSGTCTTCQKGLIMNPRGSCMANEKCSPSEYWDEDAPGCKPCHVKCFHCMGPAEDQCQTCPMNSLLLNTTCVKDCPEGYYADEDSNRCAHCHSSCRTCEGRHSRQCHSCRPGWFQLGKECLLQCREGYYADNSTGRCERCNRSCKGCQGPRPTDCLSCDRFFFLLRSKGECHRSCPDHYYVEQSTQTCERCHPTCDQCKGKGALNCLSCVWSYHLMGGICTSDCLVGEYRVGEGEKFNCEKCHESCMECKGPGAKNCTLCPANLVLHMDDSHCLHCCNTSDPPSAQECCDCQDTTDECILRTSKVRPATEHFKTALFITSSMMLVLLLGAAVVVWKKSRGRVQPAAKAGYEKLADPNKSYSSYKSSYRESTSFEEDQVIEYRDRDYDEDDDDDIVYMGQDGTVYRKFKYGLLDDDDIDELEYDDESYSYYQ
Protein: Aklanonic acid methyl ester cyclase DnrD (AAME cyclase) (EC 5.5.1.23) (Methyl aklanonate cyclase) (Q54808)
Organism: Streptomyces peucetius
Function: Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the cyclization of aklanonic acid methyl ester to yield aklaviketone presumably via an intramolecular aldol condensation mechanism, although water is not eliminated.
Interaction partners:
Sequence:
MSTQIDLVRRMVEAYNTGKTDDVAEFIHLEYLNPGALEHNPELRGPEAFAAAVTWLKYAFSEEAHLEEIEYEENGPWVRAKLALYGRHVGNLVGMPATGRRFSGEQIHLIRIVDGKIRDHRDWPDYLGTYRQLGEPWPTPEGWRP
Protein: RNA-binding protein (Q382B5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDSITANDYDTESMKGLYNVTLEVTKSPSGVHSDNNGDADEAETNKGYKNVNPDCVNALAANNSRKQEEKYLAMFNDFNSHNLLDVPDSASPPRYQPTLSGVDYTFSYVGSSPFASVVQTNDADGTPEGRMEPLSDAYPSANGNAHQSSANEPSNNAPCVYASIETSPLQGRRLNFRAFLTKKTVPTSIMKEGQAGVFVGQLPSTYTEEDTAALLRAIGDDAGVPVHVRDVKSHNQSRTCAFVTVNQGALQVLLGYSKRVLCDSVCVWVVEPEKAQYLKDFVDGLVRERLRGVPKAALVLEQLTPQYVRGQASGGKEWKGASPHGRDVMGPVDGFFMAMPTMITSTAPPPPPPNGSEGQVVAGTHMPMSVLMPSWGAVQQTAGRRPTAAPNGSQVVGAFPGANIYGNPGACFIAVPPPGPVAARSQQVNLCVMAPGTGAMQPVPYVTNYAGGNMYAQAATAGSAPATVTMQQAGTSASPVQVGMGGFGQQVAGGSTVYLQSVPPYALHQVLQQPQQ
Protein: Mannose-specific lectin (Agglutinin) (LecGNA 2) (Snowdrop lectin) (P30617)
Organism: Galanthus nivalis (Common snowdrop)
Function: Mannose-specific lectin which binds alpha-D-linked mannose. Displays a high affinity for alpha-(1-3)-mannose oligomers. Displays antiviral activity and therefore may contribute to defense against infections.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MAKASLLILAAIFLGVITPSCLSDNILYSGETLSTGEFLNYGSFVFIMQEDCNLVLYDVDKPIWATNTGGLSRSCFLSMQTDGNLVVYNPSNKPIWASNTGGQNGNYVCILQKDRNVVIYGTDRWATGTHTGLVGIPASPPSEKYPTAGKIKLVTAK
Protein: Mediator of RNA polymerase II transcription subunit 28 (Mediator complex subunit 28) (dMED23) (Q9VBQ9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 29
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 18
Sequence:
MASNESGGGNLMDEFEEAFQSCLLTLTKQEPNSGTNKEEIDLEVQKTTNRFIDVARQMEAFFLQKRFLVSTLKPYMLIKDENQDLSIEIQRKEALLQKHYNRLEEWKACLSDIQQGVHSRPTPPIGSGMLQGPGGGMPPMGGTPPRPGMMPGMPPGAMQPGGPMQPSPHMLQAQQMQQLRMISRQMPPK
Protein: Falstatin (Cysteine protease inhibitor) (PfICP) (Q8I333)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Secreted {ECO:0000250|UniProtKB:A0A509AJA5}. Cytoplasmic vesicle, secretory vesicle, microneme {ECO:0000250|UniProtKB:A0A509AJA5}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:A0A509AJA5}. Parasitophorous vacuole lumen {ECO:0000269|PubMed:23421981}. Host cytoplasm {ECO:0000269|PubMed:23421981}. Note=During the asexual blood stage, localizes to the parasitophorous vacuole (PV) and to exomembrane structures beyond the limits of the PV (PubMed:23421981). Localizes to punctate peripheral structures in schizonts and rings (PubMed:17083274). Released after host erythrocyte rupture (PubMed:17083274). Secreted by gliding sporozoites (By similarity). Localizes partially with micronemes at the apical pole of sporozoites (By similarity). Released into the host cytoplasm by sporozoites (By similarity). During the host liver stage and in late schizont and cytomere stages, localizes mainly to the PV, but is also present in the parasite cytoplasm (PubMed:23421981). After completion of daughter parasite development, localizes to the host hepatocyte cytoplasm following the rupture of the PV membrane (PubMed:23421981). {ECO:0000250|UniProtKB:A0A509AJA5, ECO:0000269|PubMed:17083274, ECO:0000269|PubMed:23421981}.
Interaction partners:
Sequence:
MNLLVFFCFFLLSCIVHLSRCSDNNSYSFEIVNRSTWLNIAERIFKGNAPFNFTIIPYNYVNNSTEENNNKDSVLLISKNLKNSSNPVDENNHIIDSTKKNTSNNNNNNSNIVGIYESQVHEEKIKEDNTRQDNINKKENEIINNNHQIPVSNIFSENIDNNKNYIESNYKSTYNNNPELIHSTDFIGSNNNHTFNFLSRYNNSVLNNMQGNTKVPGNVPELKARIFSEEENTEVESAENNHTNSLNPNESCDQIIKLGDIINSVNEKIISINSTVNNVLCINLDSVNGNGFVWTLLGVHKKKPLIDPSNFPTKRVTQSYVSPDISVTNPVPIPKNSNTNKDDSINNKQDGSQNNTTTNHFPKPREQLVGGSSMLISKIKPHKPGKYFIVYSYYRPFDPTRDTNTRIVELNVQ
Protein: Acinus, isoform A (Acinus, isoform B) (Acinus, isoform C) (LD23757p) (Q9VJ12)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD23870p
- Histone deacetylase complex subunit SAP18
- Pinin, isoform B
- Eukaryotic initiation factor 4A-III
- Serine-arginine repetitive matrix 2/3/4, isoform F
- Protein mago nashi
- Polyadenylate-binding protein 2
- Serine/arginine repetitive matrix protein 1
- Caspase-8
- Scaffold attachment factor B, isoform B
Sequence:
MRRRSERKKSSSPAPVPVAVARRSRRSRKVSENEKTEVETPVVAQNNEAECPKVPPASQEINEARASSEERAGSGASPVRRSRGSRTTPRKRTESKGGDKKVDTIPEEEPENGKDVEKDAVEEEKTVAPPAANESESEDRAKTEDQQAQDDESCAEPAVVKDDDVEKEDLKPQQEVPTSTDDDTKQSEPEQEVKVPSPSSKDEEHLKTTSDVLDIQTEEVDERDEEASAPAERRETKKRHKEQIKEQQPAEEEEHKENHKQIDENPEQIHDEPADLSNDKHDPCLNSSATNTTGAPVLQQQRSVRKRKWLTNKKSSDRTPPVLAISTDSLKNIIADVVQPVPLSDVQLESSSEEEGLVTSDRDSERSASPAPPSEASKDRDNKGNTANTCDTTAEASADNEGAGAAPPAAADTVSAQVSLSKATVSTAAPHIVRDPSPARNRASHVLYITNLVRPFTVLQLKGLLARTGKIVEEDGFWIDRIKSKCYVAYSTEDEAIETRHALHGVRWPVSNPKCLNVDFGSRTDMDRAILSTKDEAPRYGQENTRDNQQSGNAWSRLEPSDKKPARPVREWDVGKKEPSDHDKHSNDRRRDSKDRLDSRSRDAERAGQERKRSRDREGRGRDRERERLDRNAHARSRSGSPASKTKKENEPPIRLLDDLFRKTKGTPCIYWLPLTPEAIAEKEAFRQKRIEEHKLRIKEREERQKEREKDRDRQRETRRNRSNERRRSRSRERERRRY
Protein: Immunoglobulin lambda variable 3-25 (Ig lambda chain V-IV region Hil) (P01717)
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:
MAWIPLLLPLLTLCTGSEASYELTQPPSVSVSPGQTARITCSGDALPKQYAYWYQQKPGQAPVLVIYKDSERPSGIPERFSGSSSGTTVTLTISGVQAEDEADYYCQSADSS
Protein: At2g23270 (Expressed protein) (Transmembrane protein) (O22181)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At4g37295
- Transmembrane protein
- Precursor of CEP16
- F28L1.2 protein
- Protein CASPARIAN STRIP INTEGRITY FACTOR 1
- Protein CASPARIAN STRIP INTEGRITY FACTOR 2
- Protein IDA
- PAMP-induced secreted peptide 1
- Kinase family with leucine-rich repeat domain-containing protein
- Precursor of CEP1
Sequence:
MMMNKVVLGSFLFFMLVSSNFVVEARPLGLTKAEENLVAKFFDGLSLGAIKESGPSSGGEGHRFVDRTETLEYGKHSGPSTSGPGH
Protein: Leucyl-cystinyl aminopeptidase (Cystinyl aminopeptidase) (EC 3.4.11.3) (Oxytocinase) (OTase) (Q8C129)
Organism: Mus musculus (Mouse)
Function: Release of an N-terminal amino acid, cleave before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endomembrane system {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Localized mainly in intracellular vesicles together with GLUT4. Relocalizes to the plasma membrane in response to insulin. The dileucine internalization motif and/or the interaction with tankyrases may be involved in intracellular sequestration (By similarity). {ECO:0000250}.
Interaction partners:
- T-cell surface glycoprotein CD4
- TBC1 domain family member 4
- Complement C4-B
- RAC-alpha serine/threonine-protein kinase
- C-C chemokine receptor type 5
- RAC-beta serine/threonine-protein kinase
- CD209 antigen-like protein A
- Beta-2-microglobulin
- Angiotensinogen
Sequence:
MESFTNDRLQLPRNMIENSMFEEEPDVVDLAKEPCLHPLEPDEVEYEPRGSRLLVRGLGEHEMDEDEEDYESSAKLLGMSFMNRSSGLRNSAAGYRQSPDGTCSLPSARTLVICVFVIVVAVSVIMVIYLLPRCTFTKEGCHKTNQSAELIQPVATNGKVFPWAQIRLPTAIIPLCYELSLHPNLTSMTFRGSVTISLQALQDTRDIILHSTGHNISRVTFMSAVSSQEKQVEILEYPYHEQIAVVAPEPLLTGHNYTLKIEYSANISNSYYGFYGITYTDKSNEKKYFAATQFEPLAARSAFPCFDEPAFKATFIIKITRNEHHTALSNMPKKSSVPAEEGLIQDEFSESVKMSTYLVAFIVGEMRNLSQDVNGTLVSVYAVPEKIGQVHHALDTTIKLLEFYQTYFEIQYPLKKLDLVAIPDFEAGAMENWGLLTFREETLLYDNATSSVADRKLVTKIIAHELAHQWFGNLVTMQWWNDLWLNEGFATFMEYFSVEKIFKELNSYEDFLDARFKTMRKDSLNSSHPISSSVQSSEQIEEMFDSLSYFKGASLLLMLKSYLSEDVFRHAVILYLHNHSYAAIQSDDLWDSFNEVTDKTLDVKKMMKTWTLQKGFPLVTVQRKGTELLLQQERFFLRMQPESQPSDTSHLWHIPISYVTDGRNYSEYRSVSLLDKKSDVINLTEQVQWVKVNSNMTGYYIVHYAHDDWTALINQLKRNPYVLSDKDRANLINNIFELAGLGKVPLRMAFDLIDYLKNETHTAPITEALFQTNLIYNLLEKLGHMDLSSRLVARVHKLLQNQIQQQTWTDEGTPSMRELRSALLEFACAHSLENCTTMATNLFDSWMASNGTQSLPTDVMVTVFKVGARTEKGWLFLFSMYSSMGSEAEKNKILEALASSEDVHKLYWLMKSSLDGDIIRTQKLSLIIRTVGRHFPGHLLAWDFVKENWNKLVHKFHLGSYTIQSIVAGSTHLFSTKTHLSEVQAFFENQSEATLKLRCVQEALEVIQLNIQWMVRNLKTLSQWL
Protein: Zona pellucida sperm-binding protein 3 (Sperm receptor) (ZP3A/ZP3B) (Zona pellucida glycoprotein 3) (Zp-3) (Zona pellucida protein C) [Cleaved into: Processed zona pellucida sperm-binding protein 3] (P21754)
Organism: Homo sapiens (Human)
Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation.
Subcellular location: [Processed zona pellucida sperm-binding protein 3]: Zona pellucida {ECO:0000269|PubMed:29895852}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48833}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Zona pellucida sperm-binding protein 2
- Zona pellucida sperm-binding protein 1
- Zona pellucida sperm-binding protein 4
- Polycystin family receptor for egg jelly
- Placenta-specific protein 1
- Oviduct-specific glycoprotein
- Growth/differentiation factor 9
- Hyaluronidase PH-20
- Beta-1,4-galactosyltransferase 1
- NHP2-like protein 1
Sequence:
MELSYRLFICLLLWGSTELCYPQPLWLLQGGASHPETSVQPVLVECQEATLMVMVSKDLFGTGKLIRAADLTLGPEACEPLVSMDTEDVVRFEVGLHECGNSMQVTDDALVYSTFLLHDPRPVGNLSIVRTNRAEIPIECRYPRQGNVSSQAILPTWLPFRTTVFSEEKLTFSLRLMEENWNAEKRSPTFHLGDAAHLQAEIHTGSHVPLRLFVDHCVATPTPDQNASPYHTIVDFHGCLVDGLTDASSAFKVPRPGPDTLQFTVDVFHFANDSRNMIYITCHLKVTLAEQDPDELNKACSFSKPSNSWFPVEGSADICQCCNKGDCGTPSHSRRQPHVMSQWSRSASRNRRHVTEEADVTVGPLIFLDRRGDHEVEQWALPSDTSVVLLGVGLAVVVSLTLTAVILVLTRRCRTASHPVSASE
Protein: LP01553p (Q8MRH3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKLRDDDVWIVTLPKCGTTWMQELLWLLLNNCDFEGALAKDQELRTPFLEFGYSVFHDPNRSFGPIEDLKSPRLIKSHLSLALLPSKLWEGKNKVIYVSRNPLDSYVSRYYHGVSFGFNYGKSLHQYFDEVLASDDFPTEFIEHAHEFYQLRNEPWVFYTSFEMMKKDLRGVINDVSRFLNKPINDQQMEKLLKHLSFAEMKKNPTTNHLWELAQVQHENAGKEMHPFVRRGDVNGYKDELKPEQIEKANVRIQEVLAKNGVTLDELLLLKDHSEVNNSERGEQIKQGQAV