wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein (Q57XW8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQRRKRSRTHSVGDEVSKNSGSKYVPQPEKIASAASGDTLEREDSIKLSNTVLRSLAIAPDVSGIRCVAVHPSEREIVLARENGSLILYAIERFQNVTHFQMLRSTGGRKSRTITRLRYLTRGTGNSKGISTRTAPLLLASYLSGQFVVYCGDTLAPLCVHQRTGGAIWDFCITDHTVYAAKADGSWHQLHVEYSSNVAGAAGPRAPTVPALTLKRIIPKVPGADRAISVCCSRQWGIVAGTDDAGNVVAWRLPRPESTDDRDEETINQDNRGGEGNTGTAGDRPQSLTEHEALWTSRLPEGMALCCTISTSSKNAAPVVAVGTSVGDVVIFEATRGQAVKTFTHHKGPISSLVSCQEYVSGNQCGVIYASGWHESLRSYRCSVEGEWRPAEVKRRTHHHETSELALLHRHQIILSASRDATVMYSPTQCLFSAPAMYLHTTCQKLAFAKERNVLLQTRSGRIEGFCTDAALRRWSPLFGYEVKGKFHLQGLWCDDSLGHIVFSTDERVSLLCCRWRNGLEGSLALKRIEEVRSLPAKYGIIDCCFVNTKTNKSCYLLFDDAIVQISLTKAYPVVTTQLVQRDGDPDEIDICPTRFMWLENRADVGEEEGTNHTKLMVYGRRGWLSCSTAVDGTIDTSTFTVHREVMQMVESVPHLSQSQGRVEHTIVALANGERYVAGIGTSQLLQLPRSLPHDTRFVALLPPRRRRNDSGNEVSEGLGSGPRFLATFSRGLLWVTRNSWCMLSRCSAEGAFVLRGNKKVLIVVRNLEGTLEVLPPCWRLRRFGN
Protein: Myelin and lymphocyte protein (T-lymphocyte maturation-associated protein) (O09198)
Organism: Mus musculus (Mouse)
Function: Could be an important component in vesicular trafficking cycling between the Golgi complex and the apical plasma membrane. Plays a role in the maintenance of the myelin sheath and in axon-glia and glia-glia interactions.
Subcellular location: Membrane; Multi-pass membrane protein. Cell membrane {ECO:0000269|PubMed:15337780}. Note=Found in lipid rafts. {ECO:0000269|PubMed:15337780}.
Interaction partners:
Sequence:
MAPAAASGGSTLPSGFSVFTTFPDLLFVCEFVFGGLVWILIASSLVPLPLAQGWVMFVSVFCFVATTSLMILYIIGTHGGETSWITLDAAYHCVAALFYLSASVLEALATISMFDGFTYKHYHENIAAVVFAYVVTLIYVVHAVFSLIRWKSS
Protein: Heat shock 70 kDa protein 1 (Heat shock cognate 70 kDa protein 1) (Heat shock cognate protein 70-1) (AtHsc70-1) (Heat shock protein 70-1) (AtHsp70-1) (Protein EARLY-RESPONSIVE TO DEHYDRATION 2) (P22953)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions (Probable). Probably involved in defense response. Chaperone involved in protein targeting to chloroplasts. May cooperate with SGT1 and HSP90 in R gene-mediated resistance towards the oomycete Hyaloperonospora parasitica (downy mildew). Plays a role with WPP-domain proteins in facilitating WIT1 nuclear envelope targeting. Modulates stomatal aperture in response to various environmental conditions and physiological responses to the hormone abscisic acid (ABA).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:28004282}. Nucleus {ECO:0000269|PubMed:28004282}.
Interaction partners:
- Heat shock protein 90-4
- Heat shock protein 90-1
- Heat shock protein 90-2
- Chaperone protein dnaJ 3
- Heat shock 70 kDa protein 17
- Heat shock protein 90-3
- Chaperone protein dnaJ 2
- Heat shock protein 90-5, chloroplastic
- Heat shock 70 kDa protein BIP2
- WPP domain-containing protein 2
Sequence:
MSGKGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRFSDSSVQSDMKLWPFKIQAGPADKPMIYVEYKGEEKEFAAEEISSMVLIKMREIAEAYLGVTIKNAVVTVPAYFNDSQRQATKDAGVIAGLNVMRIINEPTAAAIAYGLDKKATSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFVQEFKRKSKKDITGNPRALRRLRTSCERAKRTLSSTAQTTIEIDSLYEGIDFYSTITRARFEELNMDLFRKCMEPVEKCLRDAKMDKSTVHDVVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQGAILSGEGNEKVQDLLLLDVTPLSLGLETAGGVMTTLIPRNTTIPTKKEQVFSTYSDNQPGVLIQVYEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCFDIDANGILNVSAEDKTTGQKNKITITNDKGRLSKDEIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNTIQDEKIGEKLPAADKKKIEDSIEQAIQWLEGNQLAEADEFEDKMKELESICNPIIAKMYQGAGGEAGGPGASGMDDDAPPASGGAGPKIEEVD
Protein: Cell polarity protein mod5 (Tea1-anchoring protein mod5) (O59740)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: With tea1, acts in a positive-feedback loop in the microtubule-mediated regulation of cell polarity. Involved in the anchoring of tea1 at the cortex as well as the correct localization of tea3.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12789340}; Peripheral membrane protein {ECO:0000269|PubMed:12789340}; Cytoplasmic side {ECO:0000269|PubMed:12789340}. Note=localizes to the cell tips.
Interaction partners:
Sequence:
MSALSESPAIPSFWRPETSEISKKPRPNTTVGFQFDNRNVGTSAPSTPAIRRNNTDSFERGLSLPLPSSKQDTGSSVLDPDGDAYVNRYARPVTAGSIYIPSNYHKSFSPNTFSGFNVKRSASKSPKRSANGSTSEDISIEGSPSETAKGARSSFNSNFRTFDIGSERRRRILEASQDSSRPGRYSYRTKSASPALIDTSTLDSRLNFTMGRLERSIAQLSKNTMRAVSHLENPPKDITLPKLNVKNSAWPLQPYSPPANETPASSSSSAKARPVSVPDMSSPVPASSVEYESLKAAVTYSPSQNPKKVAETDSESRKSSFQSSYNDADRPFQVGAQTQSTPNRISRSDSPIVYDVDTHSEDNASTASSEAISQSMRSFQPQPNTGSPFPRFTSTNTEDEQESDIPQSDANDSTVNLNQPNYANLTPTPQVSPKRPTYSRSSPLPSASVPALGDGSPDPPAAPSIQNSLSVHESEMPPHVTRDYTQPAASATPVPKEKPSEKSEKPPKKKGSKLEKFCCILM
Protein: Noggin-1 (Q9W741)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Inhibitor of bone morphogenetic proteins (BMP) signaling. May play an important role in the dorsoventral patterning of the embryo.
Subcellular location: Secreted.
Interaction partners:
- Bone morphogenetic protein 4.
- Bone morphogenetic protein 7
- Bone morphogenetic protein 2
- Chordin
- Bone morphogenetic protein 2a.
- Bone morphogenetic protein 6.
- Noggin-2
- Noggin-3
- Growth differentiation factor 5
- Bone morphogenetic protein 5.
Sequence:
MDFPRFLLSAYLLLLSFAQCQHYYLLRPIPSDTLPLLELKEDPDPIYDPREKDLNETELRSALGDFDSRFLSVGPPQDRYAGNEDLDEQELQLNLAGMMPKDIKNLDFDAPWGKKRKASKKLKRRLQMWLWSYSFCPVLYAWNDLGSRFWPRFVRAGSCYTKRSCSVPEGMVCKPAKSTHITLLRWRCVARRGALKCAWIPVQYPIITECKCSCAN
Protein: Rab11 family-interacting protein 4A (FIP4-Rab11) (Rab11-FIP4-A) (zRab11-FIP4-A) (Q3LGD4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as a regulator of endocytic traffic by participating in membrane delivery. Required for the abcission step in cytokinesis, possibly by acting as an 'address tag' delivering recycling endosome membranes to the cleavage furrow during late cytokinesis (By similarity). May play a role in differentiation during retinal development.
Subcellular location: Recycling endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Recruited to the cleavage furrow and the midbody during cytokinesis. {ECO:0000250}.
Interaction partners:
- Rab11 family-interacting protein 3
- Rab11 family-interacting protein 4B
- small monomeric GTPase
- Transcription elongation factor
- RAB11B, member RAS oncogene family, a.
- Dystrotelin
- Uncharacterized protein.
- Rab11 family-interacting protein 2
- Homeobox protein goosecoid
- Serine/arginine-rich splicing factor 3
Sequence:
MDGNVFPDQEQLLAFLKKLKEVFDVCDEDADGYIRVEHFVDLGLQFGQGDEVKKFAKYLDPNAHGRINFKDFCHGVFAIKGCEEILKSALGTPTIAAQPYQTDNGYYYQHQEGSLGPPIIVCTRPYPECQLYSDEEGMGGRDMQESDMDSAADSGAGSESSEGGRQDDKEEGLGGFFLRGNNCGQMVSSAAASVISVEEQFEDYGEGEDVDFTPSSPIPDDDTRTNGFSDLGSSLPSSAGQTPQKIRHLYNSELLDVYCSQCCKKVNLLNDLEARLKNLKANSPNRKISSTAFGRQLFHHSNFSSSQGSTEDLFRDSIDSCDVDITEKVSYLEKKISELENDSLANGDLKSKLKQENTQLVHRVHELEEQIKDQETRAEQCLEEELKRHREAYSKMERDKSTEIELLSNRVQQLEEENAEMKVNVCRLKSQTEKLDQEKQRMTDKLEDTSLRLKDEMDLYRKMMDKLWQNRHEFQKEREAMQELIEDLRRELEHLQLFKLETEKPGRGRTAAGLSEYNAKTREIELEHEVKRLKQENHKLRDQNDDLNGQILSLSLYEAKNLFACHTKAQSLAAEIDNASRDELVDALKEQEEINFRLRQYMDKIILAILDHNPSILEIKH
Protein: Putative type II secretion system protein F (T2SS protein F) (General secretion pathway protein F) (Protein transport protein HofF) (P41441)
Organism: Escherichia coli (strain K12)
Function: Component of the type II secretion system inner membrane complex required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Putative type II secretion system protein E
- Type II secretion system core protein G
- Putative type II secretion system protein M
- Putative type II secretion system protein L
- Putative type II secretion system protein C
- Type II secretion system protein H
- Type II secretion system protein J
- Putative type II secretion system protein K
- Putative type II secretion system protein I
- Prepilin leader peptidase/N-methyltransferase
Sequence:
MNYRYRAMTQDGQKLQGIIDANDERQARLRLREEGLFLLDIRPQKSSGVKTRRPRISHSELTLFTRQLATLSAAALPLEESLAVIGQQSSNKRLGDVLNQVRSAILEGHPLSDALQHFPTLFDSLYRTLVKAGEKSGLLAPVLEKLADYNENRQKIRSKLIQSLIYPCMLTTVAIGVVIILLTAVVPKITEQFVHMKQQLPLSTRILLGLSDTLQRTGPTLLATVFIVAVGFWLWLKRGNNRHRFHAMLLRVALIGPLICAINSARYLRTLSILQSSGVPLLDGMNLSTESLNNLEIRQRLANAAENVRQGNSIHLSLEQTAIFPPMMLYMVASGEKSGQLGTLMVRAADNQETLQQNRIALTLSIFEPALIITMALIVLFIVVSVLQPLLQLNSMIN
Protein: BAG domain-containing protein (O61980)
Organism: Caenorhabditis elegans
Interaction partners:
- BAG family molecular chaperone regulator 1
- Heat shock protein 110
- Heat shock protein hsp-1
- DnaJ homolog subfamily B member 13
- J domain-containing protein
- E3 ubiquitin-protein ligase CHIP
- Heat shock protein 70
- Heat shock protein 70
- SHSP domain-containing protein
- DUF148 domain-containing protein
Sequence:
MPVVNIPIKILGQNQSHSRSNSSSSVDNDRNQPPQQPPQPQPQQQSQQQYQQAPNVNTNMHHSNGFSPNFPSRSPIPDFPSFSSGFPNDSEWSSNFPSFPNFPSGFSNGSSNFPDFPRFGRDGGLSPNPPMQGYRRSPTPTSTQSPTSTLRRNSQQNQAPPQYSQQQPQQAQQRQTTPPSTKASSRPPSRTREPKEPEVPERPAVIPLPYEKKEKPLEKKGSRDSGKGDENLEENIAKITIGKNNCELCPEQETDGDPSPLTSPITEGKPKRGKKLQRNQSVVDFNAKTIVTLDKIELQVEQLRKKAAELEMEKEQILRSLGEISVHNCMFKLEECDREEIEAITDRLTKRTKTVQVVVETPRNEEQKKALEDATLMIDEVGEMMHSNIEKAKLCLQTYMNACSYEETAGATCQNFLKIIIQCAADDQKRIKRRLENLMSQIENAERTKADLMDDQSE
Protein: Transmembrane protein (Q381B1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSGDSSGGGGGVRELGTVTAGMAMMNFDEKTKPYTRTDLIKFLQNYEENLTPPEKQLVWQGMLGTLVGMPLAFFVGYKVSSRFAWHRVRRALTPIGGKGREEKPSWLIRNISTVGQVMFGLAASTIPYIVVQQWFISRVLAADEHEGNLSFHVRRLMITQRSSMMFTRTATREVTREEQERLMGEAAQHSAENRSGRQGGAPLGVTDVNLRLGQQAMTPVAQTGYKPMPGQSS
Protein: RNA transcription, translation and transport factor protein (A0A8I6GBA2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MFRRKLTALDYHNPTGFNCKDETEFRNFIVWLEDQKIRHYKIEDRGNLRNIHSSDWPKFFEKYLRDVNCPFKIQDRQEAIDWLLGLAVRLEYGDNAEKYKDSVPDNRKNADNAAKNSEPLINLDVNNPDFKAGVMALANLLQIQRHDDYLVMLKGLPVALDKHILGFDTGDAVLNEAAQILRLLHIEELRELQTKINEAIVAVQAIIADPKTDHRLGKVGR
Protein: TATA-box-binding protein 1 (AtTBP1) (TATA sequence-binding protein 1) (TBP-1) (TATA-binding factor 1) (TATA-box factor 1) (Transcription initiation factor TFIID TBP-1 subunit) (P28147)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II.
Subcellular location: Nucleus {ECO:0000269|PubMed:19929880}.
Interaction partners:
- Transcription initiation factor IIF subunit alpha
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 9
- Homeodomain-like superfamily protein
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor IIA subunit 2
- DNA-directed RNA polymerase II subunit 4
Sequence:
MTDQGLEGSNPVDLSKHPSGIVPTLQNIVSTVNLDCKLDLKAIALQARNAEYNPKRFAAVIMRIREPKTTALIFASGKMVCTGAKSEDFSKMAARKYARIVQKLGFPAKFKDFKIQNIVGSCDVKFPIRLEGLAYSHAAFSSYEPELFPGLIYRMKVPKIVLLIFVSGKIVITGAKMRDETYKAFENIYPVLSEFRKIQQ
Protein: Outer membrane protein assembly factor BamD (P0AC02)
Organism: Escherichia coli (strain K12)
Function: Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamA, the core component of the assembly machinery. Probably involved in transient protein interactions. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_00922, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00922, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:27686148}.
Interaction partners:
- Outer membrane protein assembly factor BamA
- Outer membrane protein assembly factor BamB
- Outer membrane protein assembly factor BamE
- Outer membrane protein assembly factor BamC
- LPS-assembly protein LptD
- Chaperone SurA
- Chaperone protein Skp
- Outer-membrane lipoprotein LolB
- Maltose/maltodextrin-binding periplasmic protein
- Outer membrane protein A
Sequence:
MTRMKYLVAAATLSLFLAGCSGSKEEVPDNPPNEIYATAQQKLQDGNWRQAITQLEALDNRYPFGPYSQQVQLDLIYAYYKNADLPLAQAAIDRFIRLNPTHPNIDYVMYMRGLTNMALDDSALQGFFGVDRSDRDPQHARAAFSDFSKLVRGYPNSQYTTDATKRLVFLKDRLAKYEYSVAEYYTERGAWVAVVNRVEGMLRDYPDTQATRDALPLMENAYRQMQMNAQAEKVAKIIAANSSNT
Protein: Pentatricopeptide repeat-containing protein At5g14080 (Q9FMU2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Putative pentatricopeptide repeat-containing protein At3g01580
- Pentatricopeptide repeat-containing protein At3g62890
- Pentatricopeptide repeat-containing protein At5g06540
- Pentatricopeptide repeat-containing protein At5g03800
- Putative pentatricopeptide repeat-containing protein At5g47460
- Pentatricopeptide repeat-containing protein At2g44880
Sequence:
MRPATELAVRIGRELLKVSGSSRAARIWSPLIEQSLHGLGFRHSISPSLVARVIDPFLLNHHSLALGFFNWAAQQPGYSHDSISYHSIFKSLSLSRQFSAMDALFKQVKSNKILLDSSVYRSLIDTLVLGRKAQSAFWVLEEAFSTGQEIHPDVCNRLLAGLTSDGCYDYAQKLFVKMRHKGVSLNTLGFGVYIGWFCRSSETNQLLRLVDEVKKANLNINGSIIALLILHSLCKCSREMDAFYILEELRNIDCKPDFMAYRVIAEAFVVTGNLYERQVVLKKKRKLGVAPRSSDYRAFILDLISAKRLTEAKEVAEVIVSGKFPMDNDILDALIGSVSAVDPDSAVEFLVYMVSTGKLPAIRTLSKLSKNLCRHDKSDHLIKAYELLSSKGYFSELQSYSLMISFLCKAGRVRESYTALQEMKKEGLAPDVSLYNALIEACCKAEMIRPAKKLWDEMFVEGCKMNLTTYNVLIRKLSEEGEAEESLRLFDKMLERGIEPDETIYMSLIEGLCKETKIEAAMEVFRKCMERDHKTVTRRVLSEFVLNLCSNGHSGEASQLLREREHLEHTGAHVVLLKCVADAKEVEIGIRHMQWIKEVSPSLVHTISSDLLASFCSSSDPDSILPFIRAIENT
Protein: Chromatin modification-related protein EAF1 B (ESA1-associated factor 1 B) (F4J7T2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A.
Subcellular location: Nucleus {ECO:0000269|Ref.3}.
Interaction partners:
- SWR1-complex protein 4
- Phosphatidylinositol 3-and 4-kinase family protein with FAT domain-containing protein
- Phosphotransferases/inositol or phosphatidylinositol kinase
- Transcription initiation factor TFIID subunit 14
- Transcription initiation factor TFIID subunit 14b
- Actin-related protein 4
- Chromatin modification-related protein EAF1 A
- Enhancer of polycomb-like protein
- Enhancer of polycomb-like protein
- RuvB-like protein 1
Sequence:
MHGSVSGYLLVNAEVDSMGGVIDSGGGIGVKTSPRRTAIEKAQAELRQEYDVREERRRELEFLEKGGNPLDFKFGIATSHSVQSTSLTDQQAEHFVNSEVKDSFALTASPHGDSVESSGRPGVPTISEPNTADNLLLFDSENKSVEGERNLRHPNRQNRTSESERSSKAHTNQNTKETEDSAIFRPYARRNRSKISRDPARSSSTDLVQNRGGLATSISIRRGSVEGKGCIPEAANQKDMHTTSVSCPVFANSNGNIVPKNRVSSNSLNTKVDGEPVVRESTAGSKTSLLKDEADISYSKSSAYLPVGESGLAGEKAQLVSTGGSPKAATIAGQKNSSTQLNGLRDSTVEEESLTNRGATGTNGLESESSHANNVEVNVDNERDLYKVDKLDSDEISMQKTLRVEGLLDQTVGEMTKTKIEDETGQSTTIISECIPECEMQMKSVKIENQSHRSTAEMQTKEKSSETEKRLQDGLVVLENDSKVGSILSENPSSTLCSGIPQASVDTSSCTVGNSLLSGTDIEALKHQPSSDAVMLDTVKEDAILEEARIIQAKKKRIAELSCGTAPVEVREKSQWDFVLEEMAWLANDFAQERLWKMTAATQICHRVALTCQLRFEERNQHRKLKKIASVLSYAILQFWSSVEAEVPGELEETSLGIVKETCQESNCLNGIRCLAAGVKEYASRFLKYNNSSISYHSAALSTPDNMCDPEILDISMVDQLTEASLFYSVPSGAMEVYLKSIESHLTRCEKSGSSMQEEVDTSAYDTAGDIGYNVTAFDEDEGETSTYYLPGAFESSRSFNISHKKRKNLMKSHSARSYDLGDDLPYVNNTGGSNSSSLIVKRPDSNINAGSVPTRRVRTASRHRVVSPFGCATTGNLPVPSKTDASSGDTSSFQDEYSSLHGGSAVQKGTEVESSVNFEKLLPYDMAETSGKPKKKKKTHQGSAYDQTWHLNPSVHVEQKDHWKKRPENNFDMNGLYGPHSAKKQKTTKQLVENNFDMAIPHTGSIPSPAASQMSNMSNPNKSIKFIGGRDRGRKIKGLKISPGQHGSGNPWSLFEDQALVVLVHDMGPNWELISDAMNSTLKIKYIYRNPTECKDRHKILMDKTAGDGADSAEDSGNSQSYPSTLPGIPKGSARQLFQRLQGPMEEDTLKSHFEKICLIGKKLHYRKTQNDGRDPKQIVPVHNSQVMALSQVFPNNLNGGVLTPLDVCDASTSGQDVFSLENPGLPMLNQGTPVLPTSGAHPSTPGSSGVVLSNNLPTTSGLQSASVRDGRFNVPRGSLPLDEQHRLQQFNQTLSGRNLQQPSLSTPAAVSGSDRGHRMVPGGNAMGVSGMNRNTPMSRPGFQGMASAAMPNTGNMHTSGMVGIPNTGNIHSGGGASQGNSMIRPREAVQHMMRMQAAQGNSPGIPAFSNLSSGFTNQTTPVQAYPGHLSQQHQMSPQSHVLGNSHHPHLQSPSQATGAQQEAFAIRQRQIHQRYLQQQQQQFPASGSMMPHVQQPQGSSVSSSSQNSPQTQPPVSPQPLSMPPVSPSPNINAMAQQKPQKSQLALHGLGRSPQSGTSGVNNQAGKQRQRQLQQSARQHPHQRQPTQGQQLNKQLKGMGRGNMIHQNITVDQSHLNGLTMPQGNQATEKGEIAVSVRPDQQSSVGTTTSTDLQSKPFVSPLSSNHSQQLPKSFPGALSPSPQQQMQLHSDNSIQGQSSPATPCNILSTSSLSIAPAVAPSNHQHLLIHQKQRNQVQSTAQRVVQHNHLGNSELSKKSQAECMPRVPQSVTNTTQTASMGTTKGMPQASNDLKNIKAVGSTAVPALEPPSCVASVQSTASKVVNNSNTDSAGNDPVSTPNQGLAQKHGIKGVTQRQQQSLPSEEKRPKLPEKPTVQNQKHLASEEQPHLEEAQELSSSKPPDTKVE
Protein: Alpha-N-acetylneuraminate alpha-2,8-sialyltransferase ST8SIA3 (EC 2.4.3.-) (Alpha-2,8-sialyltransferase 8C) (Alpha-2,8-sialyltransferase III) (Ganglioside GD3 synthase ST8SIA3) (EC 2.4.3.8) (ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3) (Sia alpha 2,3Gal beta 1,4GlcNAc alpha 2,8-sialyltransferase) (Sialyltransferase 8C) (SIAT8-C) (Sialyltransferase St8Sia III) (ST8SiaIII) (Q64689)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of sialic acid from a CMP-linked sialic acid donor onto the terminal sialic acid of an acceptor through alpha-2,8-linkages. Is active with alpha-2,3-linked, alpha-2,6-linked and alpha-2,8-linked sialic acid of N-linked oligosaccharides of glycoproteins and glycolipids. Displays preference for substrates with alpha-2,3-linked terminal sialic acid. It can form polysialic acid in vitro directly on alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:O43173}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O43173}.
Interaction partners:
Sequence:
MRNCKMARVASVLGLVMLSVALLILSLISYVSLKKENIFTTPKYASPGAPRMYMFHAGFRSQFALKFLDQSFVPITNSLTHELQEKPSKWTFNRTAFLHQRQEILQHVDVIKNFSLTKSSVRIGQLMHYDYSSHKYVFSISNNFRSLLPDVSPIMNKRYNVCAVVGNSGILTGSQCGQEIDKSDFVFRCNFAPTEAFHKDVGRKTNLTTFNPSILEKYYNNLLTIQDRNNFFLSLKKLDGAILWIPAFFFHTSATVTRTLVDFFVEHRGQLKVQLAWPGNIMQHVNRYWKNKHLSPKRLSTGILMYTLASAICEEIHLYGFWPFGFDPNTREDLPYHYYDKKGTKFTTKWQESHQLPAEFQLLYRMHGEGLTKLTLSHCA
Protein: Potassium voltage-gated channel subfamily A member 3 (HGK5) (HLK3) (HPCN3) (Voltage-gated K(+) channel HuKIII) (Voltage-gated potassium channel subunit Kv1.3) (P22001)
Organism: Homo sapiens (Human)
Function: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:36852591}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:36852591}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:36852591}.
Interaction partners:
- Voltage-gated potassium channel subunit beta-2
- Potassium voltage-gated channel subfamily A member 1
- Sedoheptulokinase
- Voltage-gated potassium channel subunit beta-1
- Potassium voltage-gated channel subfamily A member 2
- Ubiquitin-like protein FUBI
- Immunoglobulin heavy variable 4-38-2
- Potassium voltage-gated channel subfamily A member 6
- Intermediate conductance calcium-activated potassium channel protein 4
- Caveolin-1
Sequence:
MDERLSLLRSPPPPSARHRAHPPQRPASSGGAHTLVNHGYAEPAAGRELPPDMTVVPGDHLLEPEVADGGGAPPQGGCGGGGCDRYEPLPPSLPAAGEQDCCGERVVINISGLRFETQLKTLCQFPETLLGDPKRRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRIRRPVNVPIDIFSEEIRFYQLGEEAMEKFREDEGFLREEERPLPRRDFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPEFRDEKDYPASTSQDSFEAAGNSTSGSRAGASSFSDPFFVVETLCIIWFSFELLVRFFACPSKATFSRNIMNLIDIVAIIPYFITLGTELAERQGNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEADDPTSGFSSIPDAFWWAVVTMTTVGYGDMHPVTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQSQYMHVGSCQHLSSSAEELRKARSNSTLSKSEYMVIEEGGMNHSAFPQTPFKTGNSTATCTTNNNPNSCVNIKKIFTDV
Protein: Aminopeptidase P1, putative (EC 3.4.11.9) (Q57ZA2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTNSAKILSRVREAMKLHSINALIVPSSDPHNSEYVMDSYKCRGFLTNFNGSAGTCLITMEEAYLWTDGRYWLEAGHCLYPEWQLMRDGHPGVPSLEDFVRLNLQPDLLVGMNDNLATVAEWERRRKAINLVPIPEIVRPLMPQNSDAKAEMLSIRPEQFCGQTREEKVMALVEELKGQKCEAMILSALDEVAWLTNLRGSDVPYNPVFYSYALVRSAPDPTVALFVDSAKVSSPVEAELTQSGRSVVSVSLHPYEALEDYVRALPAGTAFLVDEYQTSQRLYSLLESCKMKVNRVKCGPAQRLKAVKNAVEIEGFRRCHVRDGVALTRYLAWLHDMIVVKGDTTITECSGADVVEGFRREQEHFVQLSFPTISSVGPNGAVVHYTPPKEGSATIVPDQLYLVDSGAQYLDGTTDVTRTVCFNPPSDEERQAYTLVLKGHLALHNAVWPTGTTGHRLDALARVHLWRYGLDYAHGTGHGVGSFLNVHEGPQGIGYRPTPTEATLAAGMIMSNEPGYYKAGKYGIRIENLEVIVRAPTRHSQEGFLTFEALTMVPLCRDLIDVSMLTADEVRLVNDYHRTVRDALTPHLRRVNDSCALAYVERHTAELCALEGGC
Protein: GH01829p (TEP2 protein) (Thioester-containing protein 2, isoform A) (Q9NFV7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFRIFLTGIILQYALLVNATGIYSVVGPGTLRSNSKYNVVVSVHKADGPSQIKVSLNGPSYNETKQIELPPMSTQNVEFEVPKLATGNYNLSAEGVSGVVFKNSTKLNYADKKPSVFVQTDKATYKPADLVQFRILFLDENTRPAKIEKPISVIIIDGAQNRIKQLSDVKLTKGVFSGELQLSEQPVLGTWKISVSVDGDNRETKSFEVDKYVLPKFEVIVDTPKAVVIADKVIKATIRAKYTYGKPVKGKATVSMERSYGYFGDLNANGNKQEKTIDVDGKGHVEFDIIHWAQRGQYLPPIKLFAVVTEELTGNKQNATATVVLHQQRYSIEPYERPEHFEANKSFIYQVVVKNVDGSPVTNSAKNVKIGFDKSYSYFHEPSPKTRINFEAPVNENGIATFNVRLPDSDSRYYRIFASFDGSENTIGSISKFEPTPMSREPLKIQVNTKKPRLGEQVSFDVVSIEDLPYFVYTIVARGNVILSDYVDVPDGQKTYTVKFTPTFSMVPKATIYVYYVVNNDLQFEEKTIDFEKEFSNSIDVSAPTNAKPSEEVKLRIKTDADSFVGLLGVDQSVLLLKSGNDLSQDDIFNSLNIYQTSTPWMNGYGRYPGQTSGLVTLTNANYPYNTGPLVMSYVFEGSRHPWITRPRYRVGIRGDSGDRISFLSQSLNDRNLKEILLKQTPQRTTIRKEFPETWFFENVGEEEFTLTKKIPDTITSWVVTGFSLNPTSGIALTKNPSKIRVFQPFFVSTNLPYSVKRGEVIAIPVVIFNYLDKTLDADVVMDNSDQEYEFTEATNEVLEKAIDEVRRVKRVTIPANSGKSVSFMIRPKNVGFTTLKITATSALAGDAIHQKLKVEPEGVTLFENRAVFINLKDQPEMSQSLDADIPNEVVPQSEFIEFSVVGDLLGPTLQNLDNLVRMPYGCGEQNMVNFVPNILVLKYLEVTGRKLPSVESKARKFLEIGYQRELTYKHDDGSYSAFGKSDASGSTWLTAYVMRSFHQAGTYTDIDPKVITAGLDFLVSKQKESGEFPEVGKLFDNANQNPLALTSFVLLAFFENHELIPKYQSAIKKAVRYVAEEADKTDDQYSLAIAAVALQLAKHPQSEKVIAKLESVARKENDRMWWSKATESTGEDGRVFHWKPRSNDVEITSYVLLALLEKDPAEKALPIIKWLISQRNSNGGFSSTQDTVIGLQALTKFAYKTGSGSGTMDIEFSSAGESKNTIKVNPENSLVLQTHDLPKSTRKVDFTAKGTGSAMVQLSYRYNLAEKEKKPSFKVTPTVKDTPNQLLIVDVCAEYVPLEDADKDKDSNMAVMEIALPSGFVGDSTSLGKIQAVDRVKRVETKNSDSTVVVYFDSLTPGDVRCLPLEASKAHAVAKQKPASVSLYDYYDTERKATEYYQVKSSLCDICEGADCGEGCKKD
Protein: DC-STAMP domain-containing protein 2 (A0A140LIJ0)
Organism: Mus musculus (Mouse)
Function: Essential sperm cell-surface protein required for sperm-egg fusion and fertilization.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:35393517}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in the anterior acrosome before the acrosome reaction and then translocates to the equatorial segment in acrosome-reacted sperm. {ECO:0000269|PubMed:35393517}.
Interaction partners:
- Sperm-egg fusion protein TMEM95
Sequence:
MEEGSSTARAVVRSTCGFTVGLSLATAFGLLELLGEGHSPFGCLVTTVTLAAFLSLGMGFSRQVRVSVLLLLPQAFSKQSRLLLLVASFGLVLQGPCANTLQNFTRASEAVACGAELALNQTAEMLERAKQPLISALSKIKAIAQKAKVVGDRIRKFFRSIIDAVKHIARCLQNVWYWLLHIGDMCNSELGNPYSKCTQVFDDAKIHCMKVVSGFPHLCYALLPYKLLVCGLASLVQKFCVLPSYLEFFLRTVIRTPVMKLLGKLRREFEFNMTATHYFSVDLNSSRSLSQVALDLQEAVSMKLYTAREALSLMGYTMPLLIGFLYIQALCYRYYYLNSDKFDNVYITRRFLDMEAVRSLAGMPTVLPLSSHEAKHYIQPDSMFLSQREQMFYTLEIFNLTRHLLIMLLLVFLDYGVFWLLDLARYHLQGEIVARSPVVVSISVEGSGYSGNIYRDLASAFDVMQQGNVSVLSPRCTLHPSEPDAKGYIVIGTMYGLCFFVTLFGSYVSRLRRAICASYYPSREQERITYLYNMLLSHRTNITATVQRAVRRRSADQGQMNILQVLAIRLPFLRPLLGPFSLQQSYCMGCGEPEDKGGMENFVSCSTPGCRGLYCPTCFRLLNNTCSVCSAPLSNQGHLDLELDSSDEESPQLWLAAARRKAPEQELKLRQQLQEALGTNLSDKSTSKPERAGNRNQDRKQ