wanglab/gogpt-training-data huggingface dataset:
Protein: Rho GTPase-activating protein 31 (Cdc42 GTPase-activating protein) (A6X8Z5)
Organism: Mus musculus (Mouse)
Function: Functions as a GTPase-activating protein (GAP) for RAC1 and CDC42. Required for cell spreading, polarized lamellipodia formation and cell migration.
Subcellular location: Cell projection, lamellipodium. Cell junction, focal adhesion.
Interaction partners:
- Zinc finger E-box-binding homeobox 2
- Intersectin-1
- Ras-related C3 botulinum toxin substrate 1
- Cell division control protein 42 homolog
Sequence:
MKNKGAKQKLKRKGAASAFGCDLTEYLESSGQDVPYVLKSCAEFIETHGIVDGIYRLSGITSNIQRLRQEFGSDQCPDLTREVYLQDIHCVGSLCKLYFRELPNPLLTYELYEKFTEAVSHRPEEGQLARIQNVILELPPPHYRTLEYLIRHLAHIASFSSKTNMHARNLALVWAPNLLRSKKIEATICNGDAAFLAVRVQQVVIEFILNHADQIFNGGAPGALQQDESRTITKSLTLPALSLPMKLVSLEEAQARSLATNHPARKERRENSLPEIVPPPFHTVLELPDNKRKLSSKSKKWKSIFNLGRSGSDSKSKLSRNGSVFVRGQRLSVEKATIRPAKSMDSLCSVPVEGKENKGNFSRTVTTGGFFIPATKMHASSTGSSCDLSKEGEWGQEGMPAGAEGGCEVGGQIRPLPEQLKVFRPIGDPESEQSAPKLLGMFYTSSDSPGKSVFTSSLFQMEPSPRHQRKALNISEPFAVSVPLRVSAVISTNSTPCRTPPKELQSLSSLEEFSFQGSESGGWPEEEKPLGAESFPGSVTKKAATEDTKPEPEVPGRAECSQSPPLDPGTQVEKKTLHVSLGSQVSKEAEKRPKAEKVMEESQGASQPKPSTPQESLGAGTEPLILHEMDEEDLAQALIWPEIQQELKIIESEEEFSSLPPAAQKTSPIPESSPAPFPFPEAPGSLPSSSAPREVWTRDAANQSIQEAAILTDREKLEPVCSLLESESQQELSPDPASLAPLEMLLFEKVSSPARIEIGGPRNLSPPLTPAPPPPTPLEEEPEVLLSKEGPDREDAARDSRTDVYTEQPTPKESPGIPTPCQREEAIASPNEKQNARHAVPENKGPGLPSPTKEVDIIPQEEGGAPHSAQEPSDCDEDDTVTDPAQHGLEMVEPWEEPQWVTSPLHSPTLKEVQESQTQGSQGHRLERRLCHRPSLRQSHSLDSKTTGNSHWTLEAPFSSSCANLETERNYEPLQPPAARTKIAGLEEKALKAFREFSGLKGLEVLPSQKGPSGIQPKPVETNFMGLAEGKEQEPQLELSNRQMKHSDVPGPDSSKESSPRAQDSTLPGEHPLQLQLKNTECGPSKGKHRPSSLNLDSATPIADLFRLENGAPFSSPGIELSELGDTKVTWMSSSHCKAAPWNSQDTQDLDIVAHTLTGRRNSAPVSVSAVRTSFMVKMCQAKAVPVIPPKIQYTQIPQPLPSQSTGEGGAQPLERSQEEPGSTPEIPQKSTKDDSPSSLGSPEEEQPKQETGASASRRQASITSCMYEGSSCSPEPSASTLASTQDAVVQCRKRTSETEPSGDNLLSSKLERASGGPKAFHRSRPGRPQSLILFPIMDHLPSSPTVIDSKVLLSPIRSPTQTVSPGLLCGELAENTWITPEGVTLRNKMTIPKNGQRLETSTSCFYQPQRRSVILDGRSGRQIE
Protein: Serine/threonine-protein kinase/endoribonuclease IRE2 (Endoplasmic reticulum-to-nucleus signaling 2) (Inositol-requiring protein 2) (hIRE2p) (Ire1-beta) (IRE1b) [Includes: Serine/threonine-protein kinase (EC 2.7.11.1); Endoribonuclease (EC 3.1.26.-)] (Q76MJ5)
Organism: Homo sapiens (Human)
Function: Induces translational repression through 28S ribosomal RNA cleavage in response to ER stress. Pro-apoptotic. Appears to play no role in the unfolded-protein response, unlike closely related proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11175748}; Single-pass type I membrane protein {ECO:0000269|PubMed:11175748}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- X-box-binding protein 1
- Cyclic AMP-dependent transcription factor ATF-6 alpha
- Cyclic AMP-dependent transcription factor ATF-6 beta
- TNF receptor-associated factor 2
Sequence:
MASAVRGSRPWPRLGLQLQFAALLLGTLSPQVHTLRPENLLLVSTLDGSLHALSKQTGDLKWTLRDDPVIEGPMYVTEMAFLSDPADGSLYILGTQKQQGLMKLPFTIPELVHASPCRSSDGVFYTGRKQDAWFVVDPESGETQMTLTTEGPSTPRLYIGRTQYTVTMHDPRAPALRWNTTYRRYSAPPMDGSPGKYMSHLASCGMGLLLTVDPGSGTVLWTQDLGVPVMGVYTWHQDGLRQLPHLTLARDTLHFLALRWGHIRLPASGPRDTATLFSTLDTQLLMTLYVGKDETGFYVSKALVHTGVALVPRGLTLAPADGPTTDEVTLQVSGEREGSPSTAVRYPSGSVALPSQWLLIGHHELPPVLHTTMLRVHPTLGSGTAETRPPENTQAPAFFLELLSLSREKLWDSELHPEEKTPDSYLGLGPQDLLAASLTAVLLGGWILFVMRQQQPQVVEKQQETPLAPADFAHISQDAQSLHSGASRRSQKRLQSPSKQAQPLDDPEAEQLTVVGKISFNPKDVLGRGAGGTFVFRGQFEGRAVAVKRLLRECFGLVRREVQLLQESDRHPNVLRYFCTERGPQFHYIALELCRASLQEYVENPDLDRGGLEPEVVLQQLMSGLAHLHSLHIVHRDLKPGNILITGPDSQGLGRVVLSDFGLCKKLPAGRCSFSLHSGIPGTEGWMAPELLQLLPPDSPTSAVDIFSAGCVFYYVLSGGSHPFGDSLYRQANILTGAPCLAHLEEEVHDKVVARDLVGAMLSPLPQPRPSAPQVLAHPFFWSRAKQLQFFQDVSDWLEKESEQEPLVRALEAGGCAVVRDNWHEHISMPLQTDLRKFRSYKGTSVRDLLRAVRNKKHHYRELPVEVRQALGQVPDGFVQYFTNRFPRLLLHTHRAMRSCASESLFLPYYPPDSEARRPCPGATGR
Protein: Putative cellulose-binding protein (A0AEF5)
Organism: Ruminococcus flavefaciens
Interaction partners:
Sequence:
MKNSLFKRVAAAAAAVPLALTQCLTFSSVAAENDAVQIVGNTVQDGAAQTVSLESLLYIPANKTESTWNVTGSAALAKMVGTKGSINNAKILDLVKYVPANYREAAKAALEEYVLVNPVTYEVTADKNIVLKATVSQPNFNGNWANTPGKALSDLAKAYNAPELNAVDFSSVKVGGDLVVTIKTSKLDEGTTVPVEVVYKTADGDIYAGDFAKFANDKLTELENIAKKAIENDVAAQYAKEATDKFLAKTALIRDKINKAEKALDQALTKTADYKSISEAADAANKFLAKKNINKKVPSSAAEVAAKETVKKYYDAAVKKASAKADIQITVEQLGAFVDSLTSKTLTDSEGNEFATAFDINLNNGKATLVGAFEDAEAADVQKWVESKGYAYVGSYKKLTGTVDFTGIKTADTASVDVQIERILVTETTTTTTTTTDDGSTTTTTTDDGSTTTTTTDDGSTTTTTSTTDDGSTTSTTSTTDDGSTTSTTSTTDDGSTTSTTSTTDDGSTTSTTSTTDDGSTTSTTSTTDDGSTTSTTSTTDDGSTTSTTSTTGDGSTTTTTTTTNTVTSAVKTQYVEIESVDGFYFNTEDKFDTAQIKKAVLHTVYNEGYTGDDGVAVVLREYESEPVDITAELTFGDATPANTYKAVENKFDYEIPVYYNNATLKDAEGNDATVTVYIGLKGDTDLNNIVDGRDATATLTYYAATSTDGKDATTVALSPSTLVGGNPESVYDDFSAFLSDVKVDAGKELTRFAKKAERLIDGRDASSILTFYTKSSVDQYKDMAANEPNKLWDIVTGDAEEE
Protein: Proline--tRNA ligase (EC 6.1.1.15) (Global RNA synthesis factor) (Prolyl-tRNA synthetase) (ProRS) (P16659)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). Misacylated Cys-tRNA(Pro) is not edited by ProRS, but instead may be edited in trans by YbaK.
Subcellular location: Cytoplasm.
Interaction partners:
- Isoleucine--tRNA ligase
- Arginine--tRNA ligase
- Leucine--tRNA ligase
- Methionine--tRNA ligase
- Glutamine--tRNA ligase
- Glutamate--tRNA ligase
- Lysine--tRNA ligase
- Lysine--tRNA ligase, heat inducible
- Tyrosine--tRNA ligase
- Asparagine--tRNA ligase
Sequence:
MRTSQYLLSTLKETPADAEVISHQLMLRAGMIRKLASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQYGPELLRFVDRGERPFVLGPTHEEVITDLIRNELSSYKQLPLNFYQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHTSQESLQETYDAMYAAYSKIFSRMGLDFRAVQADTGSIGGSASHEFQVLAQSGEDDVVFSDTSDYAANIELAEAIAPKEPRAAATQEMTLVDTPNAKTIAELVEQFNLPIEKTVKTLLVKAVEGSSFPQVALLVRGDHELNEVKAEKLPQVASPLTFATEEEIRAVVKAGPGSLGPVNMPIPVVIDRTVAAMSDFAAGANIDGKHYFGINWDRDVATPEVADIRNVVAGDPSPDGQGRLLIKRGIEVGHIFQLGTKYSEALKASVQGEDGRNQILTMGCYGIGVTRVVAAAIEQNYDERGIVWPDAIAPFQVAILPMNMHKSFRVQELAEKLYSELRAQGIEVLLDDRKERPGVMFADMELIGIPHTIVLGDRNLDNDDIEYKYRRNGEKQLIKTGDIVEYLVKQIKG
Protein: Vitellogenin receptor Yl (Protein yolkless) (Yl) (P98163)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in uptake of vitellogenin by endocytosis.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:10679010}. Cytoplasm, cell cortex {ECO:0000269|PubMed:10679010}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:10679010}; Single-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:10679010}; Single-pass membrane protein {ECO:0000255}. Endosome, multivesicular body lumen {ECO:0000269|PubMed:10679010}. Note=Distributed throughout the oocyte during oogenesis (PubMed:10679010). At the start of vitellogenesis during stage 8 of oogenesis redistributes to the oocyte cell cortex (PubMed:10679010). Associated with multivesicular structures that mature into yolk granules (PubMed:10679010). {ECO:0000269|PubMed:10679010}.
Interaction partners:
- Deubiquitinase otu
- LD29322p
- LD24340p
- Tubulin alpha-4 chain
- Chorion peroxidase
- Mitosis initiation protein fs
- Maternal effect protein oskar
- Female sterile
- Poly
- Protein matrimony
Sequence:
MCQAEHQVHPSEQRIRVESPKMTASRRGFNLTSQTRAHPSSGGSTSSRYGNCQRTHLIINGRHVAISLLLLVGLCGGTAAGTPGSADTRCDAGQFQCRDGGCILQAKMCDGRGDCKDSSDELDCDYRLCRPPHWFPCAQPHGACLAAELMCNGIDNCPGGEDELNCPVRPGFRFGDTAHRMRSCSKYEFMCQQDRTCIPIDFMCDGRPDCTDKSDEVAGCKQAEITCPGEGHLCANGRCLRRKQWVCDGVDDCGDGSDERGCLNLCEPQKGKFLCRNRETCLTLSEVCDGHSDCSDGSDETDLCHSKPDCDAKKCALGAKCHMMPASGAECFCPKGFRLAKFEDKCEDVDECKEQDDLCSQGCENTSGGYRCVCDAGYLLDKDNRTCRAVVYGSKEQQPLLLYTTQMTIMGMHLREDNVRNHVYQVAGNLSKVIGVAYDGSHIYWTNIQNEAESIVKANGDGSNAEILLTSGLDAPEDLAVDWLTQNIYFSDNIMRHIAVCSNDGLNCAVLVTQDVHQPRSLAVWPQKGLMFWTDWGEKPMIGRASMDGSRSRPIVSDNIEWPNGIALDMHQQRIYWVDAKLGSVQTVRPDGTGRRTVLDGMLKHPYGLAIFEDQLYWSDWATKSVHACHKFSGKDHRILAKDRTIYAVHIYHPAKQPNSPHGCENATCSHLCLLAEPEIGGHSCACPDGMRLAPDHRRCMLMEKRQRLFIGLGQVLLEIEHTAFGRHQVSKSYTLPCLINEMVYNRINGSLIIADNDQRLILEFQPESHESNVLVRSNLGNVSALAFDHLSRNLYWADTERAVIEVLSLQTRHRALIRFFPGQEVPIGLTVMPAEGYLYVVLKAKRHSHIDKIPLSGKGEQVHVFEDDLGDDDIKLVTDYETQTIFWSDSDLGRISYSNYRVPHSQIFRGKLRRPYSLAMVHHDLFWNELGTPRIYWTHKSNMGPRKVIDIMEKDDPAAIMPYVPVATPNGIPLAASSPVGQESHPCQQQNGGCSHICVGEGPYHSICLCPAGFVYRDAGNRTCVEALDCEFRCHSGECLTMNHRCNGRRDCVDNSDEMNCDEEHRRKPKVLCSPNQFACHSGEQCVDKERRCDNRKDCHDHSDEQHCEKFDKSKKCHVHQHGCDNGKCVDSSLVCDGTNDCGDNSDELLCEATSRCEPGMFQCGSGSCIAGSWECDGRIDCSDGSDEHDKCVHRSCPPDMQRCLLGQCLDRSLVCDGHNDCGDKSDELNCGTDSSTMNISCAEDQYQCTSNLKICLPSTVRCNGTTECPRGEDEADCGDVCSIYEFKCRSGRECIRREFRCDGQKDCGDGSDELSCELEKGHHNQSQIQPWSTSSRSCRPHLFDCQDGECVDLSRVCNNFPDCTNGHDEGPKCATACRSASGRQVCQHKCRATPAGAVCSCFDGYRLDADQKSCLDIDECQEQQPCAQLCENTLGGYQCQCHADFMLRQDRVSCKSLQSGATLLFSSFNEVRNLSEQPVMLNVAWSANDSRITGFDLAMHRQMGYFSAEDEGIVYQIDLQTKVIVRALGLPAPTKLSVDWVTGNVYVLSGAQEIQACSFVGRMCGRIVHVKSPRHVKHLAVDGYHARIFYIVIRTEGYGQTSSEIHMARLDGSRRDMLLQRSESFMTALTTDPHQQLLYFVDQHMRTLERISYRLKTGPMRRPEIMLQKSNALMHPSGLSVYENNAFIVNLGSVEAVQCALYGSRICHKISINVLNAQDIVVAGRSRQPQKASHPCAHAHCHGLCLQADYGYECMCGNRLVAEGERCPHGSGNEVAVLGAVNSLELEHEHEQNGHFHWLMALFVLAAGSLIAGLGYMYYQYRQRGHTDLNINMHFQNPLATLGGTKAFLEHERAEAGVGFTTETGTVSSRGSNDTFTTTSATSSFAAQQFSVPNALQRLLRPRQSASGDPMAQELLLESPSRESKLHALDGGGAGGDGDGGRGVGRQVPDILVADMDDDAAKSAGQFGGNYAGNDANARFVS
Protein: Putative ABC-transporter permease protein (Q607F2)
Organism: Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- ABC transporter, ATP-binding protein
- RND efflux pump membrane fusion protein barrel-sandwich domain-containing protein
- ABC transporter, ATP-binding family protein
- ABC transporter, ATP-binding family protein
- Lipoprotein-releasing system ATP-binding protein LolD
- Putative ABC transporter, permease protein
- Putative ABC transporter, permease protein
- Heat shock protein 15
- Transcriptional regulator, TetR family
Sequence:
MGLTFASLIMTQQPAIFVGLMMRSYSFVTDVGLPDIWVMDPKVQFVDDIKPLQDTKLFRVRGVSGVDWAMPMYKGMIKARLADGTFQTCNVIGLDDATLIGGPPVMLEGRLEDLRRADSVIVDIDGARDKLARPSKDPAGKPVPLKVGDTLELNDRRAVVVGIAKTTRTFQSQPVVYTTYSRATLYAPRERKLLSFVLVKARPGQEVHALTRRIRETTGLAAYTQAEFEELTVNYFLKNTGIPINFGMSVTLGFIVGAAIAGQTFYNFTLENIRQFGVLKAMGAGNGTLLGMILLQATLVGMVGYGLGVGLTSLFGWSMRNTILAFKFPWQLLVFSGLGVTLICVFSALLSIRKVIKLEPAIVFKG
Protein: Mediator of RNA polymerase II transcription subunit 19 (Hypoxic gene repressor protein 3) (Mediator complex subunit 19) (Negative regulator of URS2 protein 3) (SNF1 suppressor protein 7) (P25046)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16630888}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 16
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 9
- Mediator of RNA polymerase II transcription subunit 18
Sequence:
MASRVDETTVPSYYYYVDPETTYTYQQPNPLQDLISVYGLDDISRQVARTNLDGTKAVKLRKSYKNQIADLSGKFSTIPTRENGKGGQIAHILFQNNPDMMIQPPQQGQNMSEQQWREQLRNRDIALFQPPNFDWDLCSSVLSQFERSYPSEFANQNQGGAQAPFDIDDLAFDLDGTGKSQSGSNSGNNSKKRKNKSSGSSMATPTHSDSHEDMKRRRLE
Protein: Stac-like, isoform M (A8DYE8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MRVIVLKKNRPNKRGTPTAAAATSSREPPKKSPYAKKDLFVSKVEPTSPRNERKFSAATAPSMKTKWLKAFKSLKPAGSGSAQQADRRNGASSTASEPLRPNLDGSHHLQEYTYKKITACDVCSQILRGHTRQGLRCRICKLNAHGDCAPNLPRCQPKQKLLRRQKSTSELENRVDIEEETSANPKSETTRPFGEPLMLLKSTESNPDESKGNRRVR
Protein: Hha toxicity modulator TomB (Toxin overexpression modulator in biofilms) (P0AAR0)
Organism: Escherichia coli (strain K12)
Function: Attenuates Hha toxicity and regulates biofilm formation. Binds to various coding and intergenic regions of genomic DNA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Hemolysin expression-modulating protein Hha
- Antitoxin YefM
- UPF0125 protein RatB
- Toxin YoeB
Sequence:
MDEYSPKRHDIAQLKFLCETLYHDCLANLEESNHGWVNDPTSAINLQLNELIEHIATFALNYKIKYNEDNKLIEQIDEYLDDTFMLFSSYGINMQDLQKWRKSGNRLFRCFVNATKENPASLSC
Protein: Elongation factor G 1 (EF-G 1) (O30913)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL11
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein uL18
Sequence:
MDYNKLRNIGISAHIDSGKTTLTERILFYCNKIHAIHEVKGKDGVGATMDSMELERERGITIASAATHVEWKDFPINIIDTPGHVDFTIEVERSLRVLDGAILVLDSVAGVQSQSITVDRQLKRYSVPRLAFVNKCDKTGANPYNVKDQLRSKLDLNSVLMQIPIGLEDKHIGVIDLVLMKAYYFEGKDGTEIIEKEIPSDLLEEAKSKREIMLDTLADFNDELMELHMEGKEVPTEIIYNATRTGTLALKLCPVFMGSAYKNKGVQLLLDAVTRFLPSPHDIKNTALDLNNNEKEIDLKIDNELPTVALAFKLEDGQYGQLTYVRIYQGILKKGQELINSRTSKKFKVGRLIRMHANNTEDIEFGGSGDIVALFGIECASGDTFCDPSINYSMTSMFIPDPVISLSVKPKDKKSADNMAKALGRFTKEDPTFKTYVDIESNETIIQGMGELHLEVYIERMKREFKAEVETGMPQVAYRETITRKAEFNYTHKKQSGGAGQFGRVAGFMEPLDKEGETYEFVNLIKGGVIPTEYIPSCDKGFQKAMERGTLIGFPIVDIKITINDGQYHIVDSSDIAFQLAAIGAFREAYEKAKPTILEPIMKVTLEGPTEFQGNMFGLLNQRRGIITGSLEDGSFSKVEAEVPLSEMFGFSTVLRSSTQGKAEFSMEFLRYGKVPSTIFDELRKKFNDQNKS
Protein: CSD domain-containing protein (Q4GYD7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQKTPRLTTRNLFDEVFATIPADVVLNTGPASLREKYALMESIQAENEEQNTDGITFTTEEGGDNGSAADDPGPNGNLTEEGILDFSAVMRHAAKRTEEQQHGDQEQGGEVHRTIDLQLDAEDEAVQEAMKYASLFDDVEQPQRQQSVGVDADGNEGGDGIVNNTGDGGPGVGASSKGTAGGMFTSSHGTRHHTMQHQHQHQQTSGSAQNAPRRQLTAEEQIALMCPGDGRRHTGRCVLFRQNKNFGFIAPDIGNPDVYFTRESIEFTFTRRVLEAFFGMPVSANAQHREGGRDDGVDSRQSHRRQRRHGSETVSNTSGTNNCNNEGSGNEAVLDGFAIAERNIESSCTGEVIREEQPALPVAETNAGGEVSLEQPPDSDTVTSRGDKKGNGVKAMTTVGVSEIVQTEEVKEKPDDGSAGSGDNGGTVANAEANDMIQRAAALLTPEAARLLALFLQVGQPVLLVGEPLTFTVRWNTSVNRTNRRLRADNIGGLPINHHALAIEQSWFSFVFNPGAERGRDGRGNRNQGVPTEGSPSASAGESVPEEKKGGAEEKVSVPGKEGGPETGDAVQKQGGNGLMEGGDSGGVTVKENEGGKKEKRRERDKGGTGSERPVCSVLRRYRGVIYVYDADEHRGHIRPEVNGSSTVQFSSDAFLWASWMEAGRRRPAEGLVVNYSLGGTNKGGKHIATLITATDDTALSDTNLVWETKVANERALNIGRTASGNGSRVENGDGDRRNGGAGGATGAGGNRDEGAKGRKRGRDEELPLLEEDDYGIM
Protein: Serpentine Receptor, class I (O62308)
Organism: Caenorhabditis elegans
Interaction partners:
- Serpentine receptor class r-10
- Seven TM Receptor
- G-protein coupled receptors family 1 profile domain-containing protein
- Serpentine receptor class r-10
- Serpentine receptor class r-10
- Serpentine receptor class alpha-17
- Serpentine Receptor, class J
- Serpentine Receptor, class J
- Serpentine Receptor, class T
- Serpentine receptor class alpha-13
Sequence:
MPAGPPCPSSIPTYYLLTLHIIGGISIPINLIGFYLVWFQSPKMQGYKYCLCYLQLVSFIAEIEMIFICPAFYFFPLIGGFNVGADIIANNISSHHTMTLYVFVFTFELPSTLLCFIFRHNAAGKVDQKCFSSKYLKKFSLVLAHFLPFVTAFCFWNSRLTAKERMDLVMNNWPQCAHWLKFPAFEVYDYHLNPWLAVVGIGAFFVLFMVFSYCIFLGVQTLLILQQHRKSMSRQTYQAHKNALFRLVMQIVLPGVFIVVPLCICMFVVVQGDVHLQEFATDTMFFVSSHSMCSCIIMIISNPKYRSVLRKKILRILGISAKSKSNRRRGNTVLPSQPRIQ
Protein: Protein atz-1 (Abnormal transition zone 1) (Q19872)
Organism: Caenorhabditis elegans
Function: Plays a role in meiosis, germline development and oocyte morphogenesis. May play a role in DNA replication. In the germline, involved in the maintenance of transition zone nuclei and in chromosome structure and organization, but not required for mitotic proliferation.
Subcellular location: Nucleus {ECO:0000269|PubMed:28696027}.
Interaction partners:
- SET domain-containing protein
- Myosin-1
- Meiotic recombination protein rec-8
Sequence:
MASIELRNVQTELAAKNLQFKVLTEKFLEQRKELFDAKKTDSNVEYVECLSEKLRVATERISDLEKETKEGKQVANEEIGRLEKLLREAQQKRDAKIDESYQTFLRIELLVANLGESTDPENEKRIKNLMPAAKTGIPPEGVLRLTINALDSAARESKKKTMAIESLTKQVDDANKLTEVYMKRLEELEDKHRFEEALTLKIQAMMIETTGQLEAQKKIIADLQKKNDDLMKEEEGEEDYEEEENYEVEEDFEDEEEYDEEGEEEDYE
Protein: Asialoglycoprotein receptor 1 (ASGP-R 1) (ASGPR 1) (C-type lectin domain family 4 member H1) (Hepatic lectin H1) (HL-1) (P07306)
Organism: Homo sapiens (Human)
Function: Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.
Subcellular location: [Isoform H1a]: Membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Isoform H1b]: Secreted {ECO:0000269|PubMed:20886072}.
Interaction partners:
- Asialoglycoprotein receptor 2
- Thyroglobulin
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
- Ceramide synthase 2
- von Willebrand factor
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- Albumin
- Sodium/potassium-transporting ATPase subunit beta-2
- Solute carrier family 22 member 1
- Proton-activated chloride channel
Sequence:
MTKEYQDLQHLDNEESDHHQLRKGPPPPQPLLQRLCSGPRLLLLSLGLSLLLLVVVCVIGSQNSQLQEELRGLRETFSNFTASTEAQVKGLSTQGGNVGRKMKSLESQLEKQQKDLSEDHSSLLLHVKQFVSDLRSLSCQMAALQGNGSERTCCPVNWVEHERSCYWFSRSGKAWADADNYCRLEDAHLVVVTSWEEQKFVQHHIGPVNTWMGLHDQNGPWKWVDGTDYETGFKNWRPEQPDDWYGHGLGGGEDCAHFTDDGRWNDDVCQRPYRWVCETELDKASQEPPLL
Protein: Guanine nucleotide-binding protein G(s) subunit alpha (Adenylate cyclase-stimulating G alpha protein) (V6CL61)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU369121}.
Interaction partners:
Sequence:
MDEIVPKVSLDDPSTAISRDYILRITNDPEDNYPSEFYDHILTCWKDKGVMACYERSSEYQLIDCAQYFLDKVDVVRQNNYDPSEQDILRCRVMTTGIFETKFEVDKVRFHMFDVGGQRDERRKWIQCFNDVTAIIFVCASSSYNLVLWEDNTQNRLRESLALFKNIWNNRWLKTISVILFLNKQDLLSEKIKAKRYLLESFFPEFEGYNLPNDAVFDNQEDKDVVRAKYFIRGEFLRISTANSDGRHHCYPHFTCAVDTENIRRVFNDCRDIIQRIHLRQYELL
Protein: Mannose 6-phosphate receptor-like protein 1 (Q06815)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Sorting receptor involved in the transport of vacuolar enzymes from the Golgi complex to the vacuole. Involved in the delivery and maturation of PEP4 (vacuolar proteinase A) and PRB1 (vacuolar proteinase B).
Subcellular location: Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein.
Interaction partners:
- ADP-ribosylation factor-binding protein GGA1
- ADP-ribosylation factor-binding protein GGA2
- Sorting nexin MVP1
- Vacuolar protein sorting/targeting protein VPS10
- Vacuolar protein sorting-associated protein 38
- Uncharacterized transporter YNL095C
Sequence:
MLKRSSLIYLSCVLIITIPILLHVYNGPGLSHEANEHRASHKQKRTLANPDKPKSENDEDLFCAVTNPVTGSYIDLSQLSSTPNKLREGQKQISGNNKHESSKTKWSVRGWGYDTNFTLGICSSPVGEAESQQLSNLTGAFYVDQLNENNLVSIGDFSTRPALVGGSTAKKLTLKYENGSMCPNGKDKKATLLNFVCDKEIQSKAQISYIGNLHNCSYFFEVRSIHACPTSNKKNEVNVLGIFIGIFAIFFLVEFAGRRWIYAKLNRHLKNDDELHDISPSLNEQPHWDLIEDGSRWSKFFNGIIKTTRRFTKSLMRSLVRGRNSRQGGIRLRSSPSASSSSLANREFFRDMEAQNEIIDSLDINSHTTESDHPTLADNSV
Protein: serralysin (EC 3.4.24.40) (E0SC28)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- serralysin
- Alkaline protease secretion ATP-binding protein aprD
- Membrane fusion protein
- Outer membrane exporter of proteases
- Alkaline proteinase inhibitor
Sequence:
MEKNLSSRDDDALHSLSASSSYDSVYDLLHYHERGNGLTINGKPSYSIEDAGEQITRDNVSWNGSNVFGKSANLTFKFLQSARSTPDGDTGFVKFNAAQVAQAKLALQSWADLANITFTEVTGNQSANVTFGNYTRDSSGRLDYGTQAYAYLPGSGSASGTTWYNYNVDNIRSPDKMEYGRQTLTHEIGHALGLNHPGDYNAGEGNPTYSDVTYAEDTRQFSIMSYWSEKNTGGDFKGHYAAGPMLDDIDAIQRLYGANMTTRTGDTVYGFNSNTDRDFYTATSSSKALIFSVWDAGGNDTFDFSGYSNNQRINLNEGSLSDVGGLKGNVSIAHGVTIENAIGGSGNDLLIGNNADNILRGGAGDDILYGGGGADRLYGGSGRDTFVYTAVSDSKVAAPDWILDFQTGVDKIDLSALNTGNNLHFVNQFSGSGGEILLNWDSSASVSNLYLNLDNNTSPEFLVKIVGQVSQTADFVV