wanglab/gogpt-training-data huggingface dataset:
Protein: CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4 (Alpha 2,3-ST 4) (Beta-galactoside alpha-2,3-sialyltransferase 4) (EC 2.4.3.2) (EC 2.4.3.4) (Alpha 2,3-sialyltransferase IV) (Gal-NAc6S) (Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase) (Gal-beta-1,4-GlcNAc-alpha-2,3-sialyltransferase) (N-acetyllactosaminide alpha-2,3-sialyltransferase) (EC 2.4.3.6) (SAT-3) (ST-4) (ST3Gal IV) (ST3GalIV) (ST3GalA.2) (STZ) (Sialyltransferase 4C) (SIAT4-C) (Q11206)
Organism: Homo sapiens (Human)
Function: A beta-galactoside alpha2-3 sialyltransferase involved in terminal sialylation of glycoproteins and glycolipids. Catalyzes the transfer of sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc- and Galbeta-(1->4)-GlcNAc-terminated glycoconjugates through an alpha2-3 linkage. Plays a major role in hemostasis. Responsible for sialylation of plasma VWF/von Willebrand factor, preventing its recognition by asialoglycoprotein receptors (ASGPR) and subsequent clearance. Regulates ASGPR-mediated clearance of platelets (By similarity). Participates in the biosynthesis of the sialyl Lewis X epitopes, both on O- and N-glycans, which are recognized by SELE/E-selectin, SELP/P-selectin and SELL/L-selectin. Essential for selectin-mediated rolling and adhesion of leukocytes during extravasation. Contributes to adhesion and transendothelial migration of neutrophils likely through terminal sialylation of CXCR2 (By similarity). In glycosphingolipid biosynthesis, sialylates GM1 and GA1 gangliosides to form GD1a and GM1b, respectively. Metabolizes brain c-series ganglioside GT1c forming GQ1c (By similarity). Synthesizes ganglioside LM1 (IV3Neu5Ac-nLc4Cer), a major structural component of peripheral nerve myelin.
Subcellular location: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.
Interaction partners:
- 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3
- Galactoside alpha-
- Galactoside alpha-
- Beta-1,3-galactosyltransferase 2
- Beta-1,3-galactosyltransferase 5
- Beta-1,3-galactosyltransferase 1
- Asialoglycoprotein receptor 2
- Asialoglycoprotein receptor 1
- von Willebrand factor
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
Sequence:
MVSKSRWKLLAMLALVLVVMVWYSISREDRYIELFYFPIPEKKEPCLQGEAESKASKLFGNYSRDQPIFLRLEDYFWVKTPSAYELPYGTKGSEDLLLRVLAITSSSIPKNIQSLRCRRCVVVGNGHRLRNSSLGDAINKYDVVIRLNNAPVAGYEGDVGSKTTMRLFYPESAHFDPKVENNPDTLLVLVAFKAMDFHWIETILSDKKRVRKGFWKQPPLIWDVNPKQIRILNPFFMEIAADKLLSLPMQQPRKIKQKPTTGLLAITLALHLCDLVHIAGFGYPDAYNKKQTIHYYEQITLKSMAGSGHNVSQEALAIKRMLEMGAIKNLTSF
Protein: Outer surface protein (O50955)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Interaction partners:
Sequence:
MKIKPLIQLKLLGLFLFSCTIDANLNEDYKNKVKGILNKAADDQETTSADTNSNAAKNIPIADNDKVAAELKKQSQAAKTVAAAPNKGSQNQPQTTPNKGSQNQQAAPSPQLQSLSFSADLSNLPKTTAARAASLTKQRIPIQAVTTVPGNTRTFNSRNSGLPTFALNYSFSQPTRQQTNSSSAVQTTTSSGSKLQTLKNELIRAISEEKNKTQNNFGFRETYDQFKMKDSAFELLDVISSAKVYDRSYAPQLNSNTPEAENERNKFYALMDFDQYKIEQFGSIMEALYNENQNHSLIRELMISGLGTQISFELALEEINKKIEIFNQDYLNAKINSFDFTMKLKELKSKLNQILDKRKEWSRQADGLIANASSNSSLSDSKSLAEYIKKRYLDNMQNARQSVLEAYISIM
Protein: Pentatricopeptide repeat-containing protein At1g10270 (Protein GLUTAMINE-RICH PROTEIN 23) (Q9SY69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May function as a transcriptional regulator essential for early embryogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:16489121}.
Interaction partners:
- Small ribosomal subunit protein mL104
- Small ribosomal subunit protein mS29
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- Small ribosomal subunit protein uS11m
- Pentatricopeptide repeat-containing protein At2g37320
- Pentatricopeptide repeat-containing protein At2g28050
- Pentatricopeptide repeat-containing protein At1g26460
- Pentatricopeptide repeat-containing protein At1g06270
- Pentatricopeptide repeat-containing protein At1g02370
- Pentatricopeptide repeat-containing protein At2g22410
Sequence:
MSLSHLLRRLCTTTTTTRSPLSISFLHQRIHNISLSPANEDPETTTGNNQDSEKYPNLNPIPNDPSQFQIPQNHTPPIPYPPIPHRTMAFSSAEEAAAERRRRKRRLRIEPPLHALRRDPSAPPPKRDPNAPRLPDSTSALVGQRLNLHNRVQSLIRASDLDAASKLARQSVFSNTRPTVFTCNAIIAAMYRAKRYSESISLFQYFFKQSNIVPNVVSYNQIINAHCDEGNVDEALEVYRHILANAPFAPSSVTYRHLTKGLVQAGRIGDAASLLREMLSKGQAADSTVYNNLIRGYLDLGDFDKAVEFFDELKSKCTVYDGIVNATFMEYWFEKGNDKEAMESYRSLLDKKFRMHPPTGNVLLEVFLKFGKKDEAWALFNEMLDNHAPPNILSVNSDTVGIMVNECFKMGEFSEAINTFKKVGSKVTSKPFVMDYLGYCNIVTRFCEQGMLTEAERFFAEGVSRSLPADAPSHRAMIDAYLKAERIDDAVKMLDRMVDVNLRVVADFGARVFGELIKNGKLTESAEVLTKMGEREPKPDPSIYDVVVRGLCDGDALDQAKDIVGEMIRHNVGVTTVLREFIIEVFEKAGRREEIEKILNSVARPVRNAGQSGNTPPRVPAVFGTTPAAPQQPRDRAPWTSQGVVHSNSGWANGTAGQTAGGAYKANNGQNPSWSNTSDNQQQQSWSNQTAGQQPPSWSRQAPGYQQQQSWSQQSGWSSPSGHQQSWTNQTAGQQQPWANQTPGQQQQWANQTPGQQQQLANQTPGQQQQWANQTPGQQQQWANQNNGHQQPWANQNTGHQQSWANQTPSQQQPWANQTTGQQQGWGNQTTGQQQQWANQTAGQQSGWTAQQQWSNQTASHQQSQWLNPVPGEVANQTPWSNSVDSHLPQQQEPGPSHECQETQEKKVVELRN
Protein: Glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) (A0A060XEX6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- 6-phosphogluconate dehydrogenase, decarboxylating
- 6-phosphogluconolactonase
- GDH/6PGL endoplasmic bifunctional protein
- 6-phosphogluconolactonase
- Hexose-6-phosphate dehydrogenase
- RRM domain-containing protein
- RRM domain-containing protein
- Transaldolase
- Transaldolase
- glucose-6-phosphate isomerase
Sequence:
MSSIPLSRSEVFGELRKELHEDEEFRQSDAHIFIIMGASGDLAKKKIYPTLWWLFRDGLLPEQTHFVGFARSDLTVDAIKTACMPYLKVADSEAERLSVFFSRNSYVSGKYADESAFSNLHTHLLSLPGGGEANRLFYLALPPSIYHDVTKNIKHHCMSTKGWNRVIVEKPFGRDLQSSEELSTHLSSLFTEDQIYRIDHYLGKEMVQNLMVLRFGNRIFGPIWNRDSIACVVLTFKEPFGTQGRGGYFDDFGIIRDVMQNHLLQMLSLVAMEKPASTSSDDVRDEKVKVLKCIAPITMSDVVLGQYVGDPEGEGDAKLGYLDDPTVPKGSTQATFATAVLYVHNERWDGVPFILRCGKALNERKAEVRLQFTDVPGDIFGAQCRRNELVVRVQPNEAVYAKMMSKKPGVYFHPEETELDLTYKSRYKDVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIENEKIPPTPYKYGSRGPTEADELSKRVGFRYEGTYKWVNPHRL
Protein: Sulfotransferase 4A1 (ST4A1) (EC 2.8.2.-) (Brain sulfotransferase-like protein) (hBR-STL) (hBR-STL-1) (Nervous system sulfotransferase) (NST) (Q9BR01)
Organism: Homo sapiens (Human)
Function: Atypical sulfotransferase family member with very low affinity for 3'-phospho-5'-adenylyl sulfate (PAPS) and very low catalytic activity towards L-triiodothyronine, thyroxine, estrone, p-nitrophenol, 2-naphthylamine, and 2-beta-naphthol. May have a role in the metabolism of drugs and neurotransmitters in the CNS.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Adenosine 3'-phospho 5'-phosphosulfate transporter 1
- Sulfotransferase 1C2
- Sulfotransferase 1A1
- Sulfotransferase 1A2
- Solute carrier family 35 member D3
Sequence:
MAESEAETPSTPGEFESKYFEFHGVRLPPFCRGKMEEIANFPVRPSDVWIVTYPKSGTSLLQEVVYLVSQGADPDEIGLMNIDEQLPVLEYPQPGLDIIKELTSPRLIKSHLPYRFLPSDLHNGDSKVIYMARNPKDLVVSYYQFHRSLRTMSYRGTFQEFCRRFMNDKLGYGSWFEHVQEFWEHRMDSNVLFLKYEDMHRDLVTMVEQLARFLGVSCDKAQLEALTEHCHQLVDQCCNAEALPVGRGRVGLWKDIFTVSMNEKFDLVYKQKMGKCDLTFDFYL
Protein: SPI-2 type III secretion system effector SifA (Type III secretion system effector protein-necessary for Sif formation and maintaining the SCV. Has GAP activity) (A0A0H3NFP4)
Organism: Salmonella typhimurium (strain SL1344)
Interaction partners:
Sequence:
MPITIGNGFLKSEILTNSPRNTKEAWWKVLWEKIKDFFFSTGKAKADRCLHEMLFAERAPTRERLTEIFFELKELACASQRDRFQVHNPHENDATIILRIMDQNEENELLRITQNTDTFSCEVMGNLYFLMKDRPDILKSHPQMTAMIKRRYSEIVDYPLPSTLCLNPAGAPILSVPLDNIEGYLYTELRKGHLDGWKAQEKATYLAAKIQSGIEKTTRILHHANISESTQQNAFLETMAMCGLKQLEIPPPHTHIPIEKMVKEVLLADKTFQAFLVTDPSTSQSMLAEIVEAISDQVFHAIFRIDPQAIQKMAEEQLTTLHVRSEQQSGCLCCFL
Protein: Quinate dehydrogenase (EC 1.1.1.24) (P25415)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Catabolic 3-dehydroquinase
- Quinate permease
- Pentafunctional AROM polypeptide
- Quinic acid utilization activator
- Uncharacterized protein
- Zn
- Multifunctional tryptophan biosynthesis protein
Sequence:
MEPITIPTDRDGVAYLYGHPLRNSLSPPLHQTVYNALGLNWTQIPLSTATGTSFTRSPEISTFLSSVRSNPKFVGSSVTMPWKVAIMPHLDDLTEDARQAGACNTIYLRKEDDGKTQYVGTNTDCIGIREALLQGSPNGAEHFKGKPALIVGGGGTARTAIYVLRKWLGVSKIYIVNRDAKEVEAILAEDKQRNPSPQVALVPVSDPSAAATLEAPVAVVSGIPNYPPQTEEEIRARETLRVFLNRQTHEKDQGVILEMCYHPLPWTDIAQIAQDARWKVILGSEALIWQGLEQARLWTGKDVVSEPGLVEKVQAFVAQTIAERSKSNL
Protein: Flagellar M-ring protein (P15928)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: The M ring may be actively involved in energy transduction.
Subcellular location: Cell inner membrane; Multi-pass membrane protein. Bacterial flagellum basal body.
Interaction partners:
- Flagellar hook-basal body complex protein FliE
- Flagellar hook-length control protein
- Flagellar biosynthetic protein FliR
- Flagellar biosynthetic protein FliQ
- Flagellar P-ring protein
- Flagellum-specific ATP synthase
- Flagellar FliJ protein
- Flagellar hook protein FlgE
- Peptidoglycan hydrolase FlgJ
- Flagellar basal body rod protein FlgB
Sequence:
MSATASTATQPKPLEWLNRLRANPRIPLIVAGSAAVAIVVAMVLWAKTPDYRTLFSNLSDQDGGAIVAQLTQMNIPYRFANGSGAIEVPADKVHELRLRLAQQGLPKGGAVGFELLDQEKFGISQFSEQVNYQRALEGELARTIETLGPVKSARVHLAMPKPSLFVREQKSPSASVTVTLEPGRALDEGQISAVVHLVSSAVAGLPPGNVTLVDQSGHLLTQSNTSGRDLNDAQLKFANDVESRIQRRIEAILSPIVGNGNVHAQVTAQLDFANKEQTEEHYSPNGDASKATLRSRQLNISEQVGAGYPGGVPGALSNQPAPPNEAPIATPPTNQQNAQNTPQTSTSTNSNSAGPRSTQRNETSNYEVDRTIRHTKMNVGDIERLSVAVVVNYKTLADGKPLPLTADQMKQIEDLTREAMGFSDKRGDTLNVVNSPFSAVDNTGGELPFWQQQSFIDQLLAAGRWLLVLVVAWILWRKAVRPQLTRRVEEAKAAQEQAQVRQETEEAVEVRLSKDEQLQQRRANQRLGAEVMSQRIREMSDNDPRVVALVIRQWMSNDHE
Protein: Tail tape measure protein gp18 (Gene product 18) (gp18) (Q0PDK7)
Organism: Bacillus phage SPP1 (Bacteriophage SPP1)
Function: Serves as a base for tail tube protein polymerization and acts as a template for tail length determination.
Subcellular location: Virion. Note=Probably present inside the tail tube. {ECO:0000305|PubMed:17611601}.
Interaction partners:
Sequence:
MEGARLQAVVTANIREFQRKMAAVNRIVRTTANRVTVTVDSRTEKFENAMNRLARITGSLSTVIGGALRGALMSAFPAAVPAAASLVGVVGSLGPMLGVAAGGAAGLGSAFATAGAGAVAYGALAATSIGGVIKASQDLDKLQAKLDDATDAKERAKIMEQIKNLQASLGKEERKALDTLEDFKSNWQDIAKSVQKPILRTFTTSLNTFKSVLNQLQPMFRGLARGGESLAKSMQNAFKAPDMKNFINYLNTEAPGAFVSFGKISGNIIRTVMNLMVAFGPLGKNMTKSIEGATAAWVKWSASLGSSVKFQKFIAYVQTNGPKLLKIIGNLSSGITSLFTGFAPLSADMMTSLVNLTARFKEWAASAKDSKEFKSFIDYIRTNGPIVWDSLGKIAKTLINLAVAMAPVGSEVLKMVNSFAQWTAATTKAHPEIGKFMAVAISLGGALRALTPVIISFQTLFGGFSSIGKAIDLIKKFKTSAAGIKLAAAIADMKLFTKTNALMAAQMAKTKFTNMITQLGLFGTKLRLQMSIMAAYLKQLVVAAAQQTAFAVKMAASYAQMKITSFITALKNGIIQMGLWIKNMAIMAAQSAANAVKMAAAWTAARISAFASMLAAGIKQMIAFGVRLAALAAAAAANAARMAASWVIAMGPIGWITAAVIALVALIIANWDKIKEYTVKIWGAVSKWLSDAWNKIKQAASVVWQALVTLIKKNFEMQKKIVTTVWNTIKSVSSKVWNGIKSFLSSVWNGIVNAGKTVWNGLKTFFTAWLNFQKKTWSTIWNAVKTAVTKVWKGIVSVGKTVWNGLKSFFTSWLNGQKKLFSTVWNAVKTAVTNVWNKLKSAASSTFNALKSSVTNIMNKVKDKIKSIWNSVMSFFKGINLGSIGRNIMQGLINGVTSMWGRVTSTFSRLTNAIPKTIKKILGIHSPSRLMRDEIGYHIGTGLVKGITGTEGMVTKAAASLAKSAVPEVPTVPELAVNSSYSGGMVEQSVNASLENFDLPEKNIIIQMDKREVGRAVEEPVREFTGRKRKRR
Protein: EH domain-containing protein 2 (AtEHD2) (EC 3.6.5.2) (B3LF48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in endocytosis negative regulation, probably by influencing actin organization. Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Exhibits an inhibitory effect on endocytosis when over-expressed.
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:Q641Z6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q641Z6}. Cell membrane {ECO:0000269|PubMed:18547399, ECO:0000269|PubMed:19936242}; Peripheral membrane protein {ECO:0000269|PubMed:18547399, ECO:0000269|PubMed:19936242}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9WVK4}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:18547399, ECO:0000269|PubMed:19936242}. Cytoplasm {ECO:0000269|PubMed:18547399}.
Interaction partners:
- EH domain-containing protein 1
- Eukaryotic translation initiation factor 3 subunit L
- AP-4 complex subunit sigma
- Methionine aminopeptidase 2B
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Transcription factor MYB3R-5
- Transcription factor MYB3R-3
- At1g28510/F3M18_5
- Dynamin
Sequence:
METSSTISIGSCLKEHQKIYKEWFNIADSDGDGRVSGNDATKFFAMSKLSRQELKQVWAVADSKRQGFLGLSEFITAMKLVSLAQEGHEITSDLLKGSIDMKSVELPVLEGLENVVSKQKVSKTNVDVEDNVVTKPQVTAKTPWFKSKSIIKPQVNVVTIVDGLKRLYTEKLKPLEVTYRFNDFASPVLTSSDFDAKPMVMLLGQYSTGKTTFIKHLLGCDYPGAHIGPEPTTDRFVVAMSGPDERTIPGNTMAVQADMPFNGLTSFGGAFLSKFECSQMPHPVLDQITLVDTPGVLSGEKQRMQRSYDFTGVISWFASKCDMILLLFDPHKLDISDEFKRVITSLRGNEDKIRVVLNKADQVDTQQLMRVYGALMWSLGKVLNTPEVVRVYIGSFNDKPINEVAVGPIGKELFEKEQNDLLADLMDVPKKACDRKINEFVKRARSAKINAYIMSHLKKEMPAMMGKSKAQQRLMDNLEEEFGKVQREFHLPAGDFPSVEHFREVLGGYNIDKFEKLKPKMIQAVDDMLGYDIPDLLKKFRNPYDN
Protein: E3 ubiquitin-protein ligase (EC 2.3.2.26) (A2VCZ7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAAASVSQSASIQAIEKSQLTLKVLSAKPQSPKLPNRHSRLSSFVEVTADGLSSETKKTGKRSGHLELQWNEDLTLNVTPQSRLDLKVWSCHTLRKELLGSATIDLLDTLRTHDGKMENVQLSLVLQTENKGSVVAGGELNVCLDGLVVDLGSLPNGSAASDKIHSSRSSLHRAHSEETPSTSSPRGRLGQSSRGSCGDSPAEIQGAALTNGDVNGALAETTSRHNSKTTVNNLSSAGKGETAANGLESAHLTCPAPSSPSLSSNPPDGTVPPPAAEPPASTEQSDTTSDTQNTDALPAGWEQRILPHGRVYYVDHNTKTTTWERPLPPGWEKRVDQRGRFYYVDHNTRTTTWQRPTAESVRNYEQWQSQRSQLQGAMQQFNQRYLYQPSGAVVENDPLGALPPGWEKRQDNGRVYYVNHNTRTTQWEDPRTQGMIQEPPLPPGWEMKYTAEGVRYFVDHNSRTTTFKDPRPGFESGSRQGGSPGAYDRSFRWKYHQFRFLCHSNALPSHVKISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKKPTLKDLESIDPEFYNSIMWVKENDLEECGVELYFAQDMEILGKVTTHQLKDDGENELVTQDNKEEYIGLLTDWRFTRGVEEQTKAFLDGFNEVVPLEWLRYFDEKELELMLCGMQEIDLNDWQKNTIYRHYTKNSKQIHWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDKVGKETWLPRSHTCFNRLDLPPYKNLEQLREKLLFAIEETEGFGQE
Protein: Interferon-induced transmembrane protein 2 (Dispanin subfamily A member 2c) (DSPA2c) (Interferon-inducible protein 1-8D) (Q01629)
Organism: Homo sapiens (Human)
Function: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS-CoV and SARS-CoV-2 S protein-mediated viral entry and VSV G protein-mediated viral entry. Induces cell cycle arrest and mediates apoptosis by caspase activation and in p53-independent manner. In hepatocytes, IFITM proteins act in a coordinated manner to restrict HCV infection by targeting the endocytosed HCV virion for lysosomal degradation. IFITM2 and IFITM3 display anti-HCV activity that may complement the anti-HCV activity of IFITM1 by inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome.
Subcellular location: Cell membrane {ECO:0000305|PubMed:33563656}; Single-pass type II membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:26354436}; Single-pass type II membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:26354436}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Interferon-induced transmembrane protein 3
- Interferon-induced transmembrane protein 1
- Interferon regulatory factor 9
- Interferon-induced protein with tetratricopeptide repeats 3
- Signal transducer and activator of transcription 1-alpha/beta
- Interferon-induced protein with tetratricopeptide repeats 2
- Signal transducer and activator of transcription 2
Sequence:
MNHIVQTFSPVNSGQPPNYEMLKEEQEVAMLGVPHNPAPPMSTVIHIRSETSVPDHVVWSLFNTLFMNTCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGIFMTILLIIIPVLVVQAQR
Protein: Histone gene-specific epigenetic repressor in late S phase, isoform C (Q9VWC2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNSLEPNSKTGRHRNNFAMCLLYGYYQPAGPLISPHVIAAPPPPAQVKKLQEEDGPVSAAGSPTQLQQQQAAAEAAAAAADQAAAQSQSQSQGQSHGHAHSHAHNPQQAQHPPQPQPYPAGAVAAAAAAAAAHQGVPYSRSMHAAQMHYSTGYPPNYYAPYPGEVMCYSPPTYPPYFSSKVYQPSHPAHPAAHPQGPPPPGAYRRYPYYQHAGPPPPHELYEQQPPPPPVSSGSVSGPAQQQPPTSSPASVGAAGAGTAGAPSGSQLVPAHQQQHQQQHLEHYPGPPSYYAGYSPGGGASAGQCYTRGLQGPYMEYPPQCPCPMPQSCPKNVHTGPHIGSNIISNIDQSSSCSSSMLLSATSNSNIGGGSSSSSSSSSSTTLPACSSATTTTTASALTTSRGPVKNVTPNNSNSSGHTSTNSCRSSNNSNNSSNSSCQTIEMTSWATAATNTTSTTATTATTGTQCQMLVKTELKGENPQVTKMQYEAHVMPPPTPPESYCASDEKLLDDQEQEAELELRLRLGLGLEKSHGGQQHIEAYDLTCSTPPPVTVPQAAAVPRKARIGKSMAREMVYAAQQQLLPEKQLKQPKEAAAKLEAEPEMPFVLKAEIKAETKIKIEHDGEAQASTHISQLPDLKPTIKTEPEQELEQEAASVPSVAKTEPQPEVEVEREQQEPPVDEEQQPTPGGSKQRFNLLALSSGNKKTKTNNSYKSLIKQAEPKSYLCPGRRFIRRHGRAPAKYVKRRQMILTQRQQQRMRLQRREQQQQRRQQREAAAEVVAGAVVTPSLAGNPIEQAGSEVSIVKDQAPNSSATPSASPKRARPRKQEIAALHLLEGLDTTLSRGYFSDPELNHSSRKQAPTAVGGLYAASSPLTTATDHRGKQTTAEKRSKSETKKPPSGESSESGLPCKKPRKEPAGKVKGKGKKTTAGAAATTIASTAETQTEAVNAITASNQETNNNEYQTADLQAQKFRECPAVTDAKVAGTATSTSTASQQQNQQHSDEQHQFLVPSQPATASATAALAATPPPSRQGQATHTKRTRSRCKFGNRKRQRHRPGGVSYELDVTQPPATKANVVPKWNNGWMWAGKAFQGAVFLNSDDPLVLRTCYPAMRHVEGDIIRIRDCVLLKANEDNELPYVAKVAHLWQNPEDGEMMMSLLWYYRPEHTDQGRQRNDCPDEVYASRHRDHNSVACVEDKCYVLTFSEYCRYRRRLRAAEEDVEDVSIVPRRPSIATAPGFPVRTVPEHTNPELVMFCRRAYEFRTRRLLKLPHKNGLVCSSS
Protein: Importin subunit alpha (Karyopherin subunit alpha) (Pendulin) (P52295)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs (By similarity).
Subcellular location: Cytoplasm. Nucleus. Note=Shuttles between the cytoplasm and nucleus in a cell cycle-dependent manner.
Interaction partners:
- Importin subunit beta
- Nibrin
- Nuclear pore complex protein Nup153
- Nuclear pore complex protein Nup50
- Exportin-2
- Maternal protein exuperantia
- E3 SUMO-protein ligase RanBP2
- Regulator of chromosome condensation
- Nuclear cap-binding protein subunit 2
- Alsin homolog
Sequence:
MSKADSNSRQGSYKANSINTQDSRMRRHEVTIELRKSKKEDQMFKRRNINDEDLTSPLKELNGQSPVQLSVDEIVAAMNSEDQERQFLGMQSARKMLSRERNPPIDLMIGHGIVPICIRFLQNTNNSMLQFEAAWALTNIASGTSDQTRCVIEHNAVPHFVALLQSKSMNLAEQAVWALGNIAGDGAAARDIVIHHNVIDGILPLINNETPLSFLRNIVWLMSNLCRNKNPSPPFDQVKRLLPVLSQLLLSQDIQVLADACWALSYVTDDDNTKIQAVVDSDAVPRLVKLLQMDEPSIIVPALRSVGNIVTGTDQQTDVVIASGGLPRLGLLLQHNKSNIVKEAAWTVSNITAGNQKQIQAVIQAGIFQQLRTVLEKGDFKAQKEAAWAVTNTTTSGTPEQIVDLIEKYKILKPFIDLLDTKDPRTIKVVQTGLSNLFALAEKLGGTENLCLMVEEMGGLDKLETLQQHENEEVYKKAYAIIDTYFSNGDDEAEQELAPQEVNGALEFNATQPKAPEGGYTF
Protein: Large ribosomal subunit protein mL42 (J3KPP0)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MAVAAVKWVMSKRTILKHLFPVQNGALYCVCHKSTYSPLPDDYNCNVELALTSDGRTIVCYHPSVDIPYEHTKPIPRPDPVHNNEETHDQVLKTRLEEKVEHLEEGPMIEQLSKMFFTTKHRWYPHGRCRKNLNPPKDR
Protein: G2/mitotic-specific cyclin-4 (Q5A0A9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: 2/mitotic-specific cyclin essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis. Degradation is necessary for the cell to exit from mitosis. Plays a role in morphogenesis by negatively regulating polarized growth. Through binding to CDC28 regulates cytokinesis, partly by phosphorylation of the actomyosin ring component IQG1.
Interaction partners:
- Cyclin-dependent kinase 1
- Nucleoporin NSP1
- Negative regulator of the PHO system
- Mitosis inhibitor protein kinase SWE1
- Serine/threonine-protein kinase
- Cyclin-dependent kinases regulatory subunit
- Anaphase promoting complex subunit
- Anaphase promoting complex subunit
- separase
- Ubiquitin-protein transferase activating protein
Sequence:
MRSYKSSITDENELTKQRLRAKSIANLSSNHTTAGQPSTSSQHREALTDLTSQENKNHPRVKLTQTNTNHHRNSSSSSNKIQIYQQIEQKKTDIHQFKKPRLEKVLLNDDDDETDDEFDDEEDKENRYHDLELNEDDSKHQLISEAFETIDDRGISEGENDTAQEARERLEEETQSHTQDMRSIYGVHVPMQPMWNNAIINELKYVIQKYSRNTLDENDEDTYDTTMVAEYSPEIFNYLHELENKFTPDPNYMDFQDDLKWEMRAVLIDWVVQVHARFNLFSETLYLTVNYIDRFLSKRRVSLSRFQLVGAVALFIAAKYEEINCPTVQEIAYMADNAYSIDEFLKAERFMIDVLEFDLGWPGPMSFLRRISKADDYDYETRTLAKYFLEITIMDSKFVASPPSWLAAGAHYISRILLGRGEWTELHVFYSGYTEKQLQPLADVLLENCRHAEINHKAIFEKYKERRYRKSSLFVQEYFRHIMSQS
Protein: Prosaposin receptor GPR37 (G-protein coupled receptor 37) (Q9QY42)
Organism: Mus musculus (Mouse)
Function: Receptor for the neuroprotective and glioprotective factor prosaposin. Ligand binding induces endocytosis, followed by an ERK phosphorylation cascade (By similarity).
Subcellular location: Cell projection, dendrite {ECO:0000250|UniProtKB:O15354}. Synapse {ECO:0000250|UniProtKB:O15354}. Cell membrane {ECO:0000250|UniProtKB:O15354}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15354}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15354}.
Interaction partners:
- Prosaposin
- E3 ubiquitin-protein ligase parkin
- Programmed cell death protein 1
- G-protein coupled receptor 37-like 1
Sequence:
MPARGAPLSRTSRLLLLLLFKVSVSAALSFVPEPRNGTCLGESCSPLIQRRSRDARGPGNSAKDALRVHVPREKLEAEVRGATSWDLPPPRGGDTGVIEEAAAAGPLGPPTKPPSAWRWKSAQGKEPSGHLRRRDPTDPQLFFPTSEGGEMSSKRDGIPQSRQEHSVKTEPRDLFYWPRRTGQLQDSQHRPSAVHEGRTLAPPGRALPQNGSADDWVPDQGGPRRGNTTRRVRLKNPFYPLTQESYGAYAVMCLSVVIFGTGIIGNLAVMCIVCHNYYMRSISNSLLANLAFWDFLIIFFCLPLVIFHELTKKWLLEDFSCKIVPYIEVASLGVTTFTLCALCIDRFRAATNVQMYYEMIENCSSTTAKLAVIWVGALLLALPEVVLRQLSKEDLGFSGQAPAERCVIKISPDLPDTIYVLALTYDGARLWWYFGCYFCLPTLFTITCSLVTARKIRKAEKASTRGNKRQIHLESQMNCTVVALTILYGFCIIPENICNIVTAYMATGVSQQTMDLLNIISQFLLFFKSCVTPVLLFCLCRPFSRAFMECCCCCCEECIQKSSTVTSDDNDNEYTTELELSPFSTIRREMSTFASVGTHC
Protein: diguanylate cyclase (EC 2.7.7.65) (Q9HZ57)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Cyclic di-GMP phosphodiesterase PA4781
- Cyclic di-GMP phosphodiesterase RocR
- EAL domain-containing protein
- Cyclic di-GMP phosphodiesterase PA2567
- GGDEF domain-containing protein
- cyclic-guanylate-specific phosphodiesterase
- cyclic-guanylate-specific phosphodiesterase
- EAL domain-containing protein
- FimX
- cyclic-guanylate-specific phosphodiesterase
Sequence:
MAPPKQSNTIDFDAAKQKRGPQPGGNASGPRASNLTELRQQLTLQLQSSLEAERILGLFFEEVRQLIPLDALGYRHPGSDLRLEFGSSAKHSVSYRLSHDSDYLGELIFRRRQRLGEDEQRQLESLLGTLLFPLRNALLYRAAIQTALRDALTGTGNRIAMDQALGRELELARRNLQPLSVLMLDIDHFKRVNDHYGHAVGDEALKAVAETIKDHLRNVDMVFRFGGEEFLVLLSSTPLQAACMVGERLRQAVEELDYRHAGEPLKLSISLGCADLRPGEGSDDLLRRVDEALYEAKRDGRNRLRCA