wanglab/gogpt-training-data huggingface dataset:
Protein: Protein 4.1 (Band 4.1) (Erythrocyte membrane protein band 4.1) (Q8JG61)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Glycophorin C
- Anion exchange protein
- Adducin 3
- Adducin 2
- Alpha-adducin
- Adducin 3
- Contactin-associated protein 1
- Actin alpha 1, skeletal muscle b.
- Spectrin beta chain
Sequence:
MLQCRVNFLDDTLFTWELERDSLGQDLFNKVCEHLNLLERDYFGLVMWDSPTNRVWLDCAKEIRKQIKSPVAEFFFSIKFYPPDPSILAEDITRYFLCLHLRKDILIGRLPCPSDILALLGSYTVQSTLGDYDPNLHKNNYVRKIVLAPNQSKELEEKVMELHATYRFMSPAQADLLFLENVMGLPMYGVDLHPAKDASGEDVMLGVCSEGLIVYEDGVKTNSFFWPRVLKISHKRNTFLLKMRPSEEDASEGNLSFSLANYRACKQLWKCSVEHHSFFRNRLQDTKAKRLLTLGSRFRYHGRKQSECVEASSNITRAPPRFTRYSIKRKANEEILDVLKLPVRAEVDDWFLVYGPEKWHIYTSDDVMLESQKLQEYKHHADDWCVLLDGSPFSLSGVQQLLQTEEQREDLETSKEKLTDEFEIKQSYQVQVVHERSDVLEKELPDYEIMRNLNEELLEVGGERIQRVVMTKEWTQTQDNGEKRVERVERRVIVTNEKMVGSGDTSESLEIMEQRLEKVEAIGRKLVEVEELRVGLQEVESLEQRLQQAEKEGLQLMKKDDWYIFLDCRPLTIIETLRERPGVVRDELQQIVYVPKPIKKEDDWFILFDVHPQTTEISQLLSDVSSSIPEGAQAEEVKREVEKIELVLPEKPKTLMREETIQSRVTTEEIQKEHQEQVTVNHGRSQTAILEQRATEPQSNQEDDWFVVLDGSPKTSASTVKSTSVEFHEETREEVIQRTEQKLQVTVQDRRPQPITVEKRTTQAGDVEDDWFIIFDVSPKETVRGPAVEVFVESREQEIQSRVRKEERVIEVMTVSTREQITVPETKRISVTQIPQFPVEPRDIDDDWFQLFDKVLYEEESFPSVRGSAVEVFVESREQEIQSRVRKEERVIEVTTVSTREQITVPETKRISVTQIPQFPVESRDIDDDWFQLFDKVLYEEESFPSVQGPAVEVFVESREQEIQSRVRKEERVIEVMTVGTREQITVPETKRISVTQIPQFPVEPRDIDDDWFQLFDKVPYEEESFPSVQGPAVFVESREQQIESRVRKEERVIKVMTVSTREQITVTKRISVTQIPQFPVEPRDIDDDWFQLFDKVPYEKESFPSDIRSREFELRESKDQRVQRVVEEQFREKRLIAEERRVSIDERRKAAEVLPQMIPVEVREVDNDWFELLDQTSYQKRSVPSVSVVSEERRIKEQEDRRVRQQQMRGREEEEERRLRKPEKPKQELEARRAQPSITVATHSQPQIEDDWFILFDVLPKETVVADVLKVERMAEEQKGRVEERKWILEEERRKLEEERRLLEKERRRREEEMWRREEEKRIQIKAEERLKRAAVSEERAVQLQTEVEDDWYMLMGITLKDYIPSAPSTPVISPVSLPKLRPQIPVDQPLTSTPTAQSASITKTYKERTKDILDITVESEAETESSLMRRTWTKKTEGESIYVRHSILMLEDLDVSQEMIMKHHASVTELKRVFMEVKDDFGPTEWDRRLSSYSPTLKPQLPHANGEILVKMGLMDENGKTILLRTQEEIFA
Protein: Bacterioferritin (BFR) (EC 1.16.3.1) (Cytochrome b-1) (Cytochrome b-557) (P0ABD3)
Organism: Escherichia coli (strain K12)
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.
Interaction partners:
- Bacterioferritin-associated ferredoxin
- Ferrochelatase
- Bacterial non-heme ferritin
Sequence:
MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIGEDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
Protein: LD07444p (Q8T0E8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCTLHPEEEAHLMAMASGGQPTRTASPRPLVTASIAAPRSLFDVCWDDVLIPQVAVYLSLKDLFNLRCCSRTAQRFVEAALEKRQELHLSGNNTKNIDVAFRVLARCCQRLEVLHLACCRWLTDELLLPLLANNKKRLWAVNLNECVNITALSLQPIIVECKELRVLKLSKCQWLTTGAVDALTLHQSKLVEFDISYCGAIGERCLIIFFRKLNKLTVLSLANTPSVTHQVLIQIGNYCRELEHINVIGCAAISDYGVHALTVHCLRLRTLLIRRCPRVTELSLAPLRQRRLYIDRPQPDVGLNAYNLNDFYPSDFLVY
Protein: Metal transporter NRAT1 (Protein NRAMP ALUMINUM TRANSPORTER 1) (Q6ZG85)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Metal transporter that transports the trivalent cation aluminum (Al(3+)), but does not seem to transport divalent cations such as iron (Fe(2+)), manganese (Mg(2+)) or Cadmium (Cd(2+)). Involved in Al tolerance by taking up Al in root cells, where it is detoxified by chelation with organic acid anions and sequestration into the vacuoles.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20937890}; Multi-pass membrane protein {ECO:0000269|PubMed:20937890}.
Interaction partners:
Sequence:
MEGTGEMREVGRETLHGGVVQSVSETDEYKEKTIDSEKDGQFRVQPRWRKFLAHVGPGALVAIGFLDPSNLETDMQAGADFKYELLWVILVGMVFALLIQTLAANLGVKTGRHLAELCREEYPHYVNIFLWIIAELAVISDDIPEVLGTAFAFNILLKIPVWAGVILTVFSTLLLLGVQRFGARKLEFIIAAFMFTMAACFFGELSYLRPSAGEVVKGMFVPSLQGKGAAANAIALFGAIITPYNLFLHSALVLSRKTPRSDKSIRAACRYFLIECSLAFIVAFLINVSVVVVAGSICNANNLSPADANTCGDLTLQSTPLLLRNVLGRSSSVVYAVALLASGQSTTISCTFAGQVIMQGFLDMKMKNWVRNLITRVIAIAPSLIVSIVSGPSGAGKLIILSSMILSFELPFALIPLLKFCNSSKKVGPLKESIYTVVIAWILSFALIVVNTYFLVWTYVDWLVHNNLPKYANGLISVVVFALMAAYLVAVVYLTFRKDTVATYVPVPERAQAQVEAGGTPVVDASAADEDQPAPYRKDLADASM
Protein: EFF-1B (Protein kinase domain-containing protein) (G5EBM0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MEPPFEWSPQFILLLLAVTTYGFPLEEKFDGLFRAEPPHCSKTPIVRAQTSQNAMSSIARGMQMQFSIGLHTAVCFRLYEDTQLASQEINDDENAGNQTSLLHTIRLEKLEHHHPITQRYTFGIPEVHASCICECDATSSTCTAESHQFTACPESDKSDETSSCYRTFFPNQTPIGCSEDDIPKLCCDVRFKPYKNMTFLAVKLEQPTTYATFVYAAYDFVNGYWVEKDKTKIRSQLDGGTQDRHLDQKRRISLAVTAGGRASHQLETGMYFSRTSNGGETEELRMQPLNEITDNNFDRLGWYRMDDSGHFHVNNGVVKMDDIHKAKVKNCKEQTYKSILSANHYMPGHFNLTRPLEVIKPWIQSARIFDSSLRQAVVTHAEGTNLQISIHLDDEVESQNLVFFHNASRIRDFSGSIIVDSKSNRLFNLTVYEASGKIDGSVKMSTGFGSDTIHTFTAYVSDLHASNRSMIIPLPAIVGQGARAICLRADSMADIDKICHVIEYFESPLEIDLVEGKWHEMIGTCPTCNQINFNGMMKFLNPAHWIKGISSIGDGVMIATDIVVYLGVLCILYLLITKIIVPLGQICLRIRRWCKK
Protein: Uncharacterized protein (Q586J3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTMKPEMDELVPVPDSLMHCFQLESYLRNMRSHISRRLNELQQSVNIVWDEVRRNATPCSDGHQLRSATSQPRSFPSRTQRDVEQTTPTPVLNRTSSALTSSACSLPQTDNRMLPTEQFSWDTSGTNVMSTFGREYGDDARDESALDSQTSVSERPGTKASTIAASEGSMDTAQVVDEMIKNAVDMLQNTSDMLRNNEEILKKAGEMPKSTEETLKMNEEVLKKDEEVLKQNVDVLTSYEETPRDKEEILKSGVEMLKCNVDMLKSNLSMLRHNADMLTNVEETLRGRDEVPNDDKKEEEESLVVEETPKQQKDDGDDVPKIHEERLTPEVGMIKYFHQDTDARRSSDGSLRSSEGIGKGRRAIKKDRSVVVGKRLCKGLKDLPVRIGAAHKQTVEFPQKDGSSLDMEGEGSGKVEEVPKETDEDEDEDDKEPKEVAFKETVDVLKVSEDVPEDKDDVKPATVEADITREGAEETKQSEDIPKGNAREDSEEDKKTYPLREEVLEDAGNKGITVNDAVGGSKSLLEIDEERFRRNEEMHQKNEKLHQKNEEMQQKNEEMQRKNEDMQRKNEDMLRRNEEILQRNEEMLRRNEELLKKKMRALKNREMRKATEIQKVIKAPRGDYKTTRLRQSPHPPRATSRLSSTGEIEGRVGREDPTMIFPSPPRARSVETAAILVDMRKMLREEIAVSLDEACSTITTKAREAAASVRQEILTELRDGCGEASTATYSVVRPGSTPKFAADEGEGQQAFATESETMQQEFHSTQETALEKKLMEHIYDLQERLALYEAERTEFRNIIRVLVQAHTKNSGSPNAALDCTAASSGPEPPSFVTEVAAVDPRKLYKLKNEPISLSSQIPTLHHPLRCDRVSTGTETTLGSRLMRQKLQADTHDQQPWSQRGLGLSRAETGRGIQNNLRQGPSRVQGGLPKLKNNVVETETVRYNTSLDYTPSRYNRRQVESFPPLPYERTRPSGTHTGS
Protein: Voltage-dependent calcium channel subunit alpha-2/delta-1 (Voltage-gated calcium channel subunit alpha-2/delta-1) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-1; Voltage-dependent calcium channel subunit delta-1] (P54289)
Organism: Homo sapiens (Human)
Function: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Plays an important role in excitation-contraction coupling (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:35293990}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit beta-1
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent L-type calcium channel subunit beta-2
- Voltage-dependent L-type calcium channel subunit beta-3
- Voltage-dependent N-type calcium channel subunit alpha-1B
- Voltage-dependent R-type calcium channel subunit alpha-1E
- Voltage-dependent L-type calcium channel subunit alpha-1F
Sequence:
MAAGCLLALTLTLFQSLLIGPSSEEPFPSAVTIKSWVDKMQEDLVTLAKTASGVNQLVDIYEKYQDLYTVEPNNARQLVEIAARDIEKLLSNRSKALVRLALEAEKVQAAHQWREDFASNEVVYYNAKDDLDPEKNDSEPGSQRIKPVFIEDANFGRQISYQHAAVHIPTDIYEGSTIVLNELNWTSALDEVFKKNREEDPSLLWQVFGSATGLARYYPASPWVDNSRTPNKIDLYDVRRRPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVSCFQHLVQANVRNKKVLKDAVNNITAKGITDYKKGFSFAFEQLLNYNVSRANCNKIIMLFTDGGEERAQEIFNKYNKDKKVRVFTFSVGQHNYDRGPIQWMACENKGYYYEIPSIGAIRINTQEYLDVLGRPMVLAGDKAKQVQWTNVYLDALELGLVITGTLPVFNITGQFENKTNLKNQLILGVMGVDVSLEDIKRLTPRFTLCPNGYYFAIDPNGYVLLHPNLQPKPIGVGIPTINLRKRRPNIQNPKSQEPVTLDFLDAELENDIKVEIRNKMIDGESGEKTFRTLVKSQDERYIDKGNRTYTWTPVNGTDYSLALVLPTYSFYYIKAKLEETITQARYSETLKPDNFEESGYTFIAPRDYCNDLKISDNNTEFLLNFNEFIDRKTPNNPSCNADLINRVLLDAGFTNELVQNYWSKQKNIKGVKARFVVTDGGITRVYPKEAGENWQENPETYEDSFYKRSLDNDNYVFTAPYFNKSGPGAYESGIMVSKAVEIYIQGKLLKPAVVGIKIDVNSWIENFTKTSIRDPCAGPVCDCKRNSDVMDCVILDDGGFLLMANHDDYTNQIGRFFGEIDPSLMRHLVNISVYAFNKSYDYQSVCEPGAAPKQGAGHRSAYVPSVADILQIGWWATAAAWSILQQFLLSLTFPRLLEAVEMEDDDFTASLSKQSCITEQTQYFFDNDSKSFSGVLDCGNCSRIFHGEKLMNTNLIFIMVESKGTCPCDTRLLIQAEQTSDGPNPCDMVKQPRYRKGPDVCFDNNVLEDYTDCGGVSGLNPSLWYIIGIQFLLLWLVSGSTHRLL
Protein: Probable methyltransferase PMT14 (EC 2.1.1.-) (Q94EJ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Probable galacturonosyltransferase 7
- Polygalacturonate 4-alpha-galacturonosyltransferase
- Probable galacturonosyltransferase 5
- Probable galacturonosyltransferase 6
- Probable galacturonosyltransferase 15
- Galacturonosyltransferase
Sequence:
MGSKHNPPGNNRSRSTLSLLVVVGLCCFFYLLGAWQKSGFGKGDSIAMEITKQAQCTDIVTDLDFEPHHNTVKIPHKADPKPVSFKPCDVKLKDYTPCQEQDRAMKFPRENMIYRERHCPPDNEKLRCLVPAPKGYMTPFPWPKSRDYVHYANAPFKSLTVEKAGQNWVQFQGNVFKFPGGGTMFPQGADAYIEELASVIPIKDGSVRTALDTGCGVASWGAYMLKRNVLTMSFAPRDNHEAQVQFALERGVPAIIAVLGSILLPYPARAFDMAQCSRCLIPWTANEGTYLMEVDRVLRPGGYWVLSGPPINWKTWHKTWNRTKAELNAEQKRIEGIAESLCWEKKYEKGDIAIFRKKINDRSCDRSTPVDTCKRKDTDDVWYKEIETCVTPFPKVSNEEEVAGGKLKKFPERLFAVPPSISKGLINGVDEESYQEDINLWKKRVTGYKRINRLIGSTRYRNVMDMNAGLGGFAAALESPKSWVMNVIPTINKNTLSVVYERGLIGIYHDWCEGFSTYPRTYDFIHASGVFSLYQHSCKLEDILLETDRILRPEGIVIFRDEVDVLNDVRKIVDGMRWDTKLMDHEDGPLVPEKILVATKQYWVAGDDGNNSPSSSNSEEE
Protein: Proliferating cell nuclear antigen (PCNA) (Cyclin) (P12004)
Organism: Homo sapiens (Human)
Function: Auxiliary protein of DNA polymerase delta and epsilon, is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways. Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion.
Subcellular location: Nucleus {ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:24115439, ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:38459011}. Note=Colocalizes with CREBBP, EP300 and POLD1 to sites of DNA damage (PubMed:24939902). Forms nuclear foci representing sites of ongoing DNA replication and vary in morphology and number during S phase (PubMed:15543136). Co-localizes with SMARCA5/SNF2H and BAZ1B/WSTF at replication foci during S phase (PubMed:15543136). Together with APEX2, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents. {ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:24939902}.
Interaction partners:
- DNA polymerase eta
- DNA polymerase delta catalytic subunit
- Flap endonuclease 1
- Cyclin-dependent kinase inhibitor 1
- Replication factor C subunit 3
- Replication factor C subunit 2
- Replication factor C subunit 4
- DNA ligase 1
- Replication factor C subunit 5
- Replication factor C subunit 1
Sequence:
MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDEEGS
Protein: PslF (Q9I1N3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PslE
- PslG
- PslJ
- PslH
- PslD
- PslI
- Alginate biosynthesis protein AlgA
- dTDP-Rha:alpha-D-Gal-diphosphoundecaprenol alpha-1,3-rhamnosyltransferase
- PslA
- PslL
Sequence:
MRIALLAPLPPEKNGIADYASHFRNALQGLGIEVATPLAGVAADSANIASRLDSVDWNAFDLVHAELGGGRLGEFIALRELRKRFPRLPLSATVHDPERMVWRRERLPWPLNLLERLPSPLPQAAVVLADPLTLREERAVAQGLTRLVTLTGLGGECLARRMRLPPGRVEVINHGNLEIATVPLPSLDTLRLLYFGFIYRGKGIEDLLEALADLFASAPEMRQRVRLTLAGGTAAEMAFGAGGNYLYQLKAQIAELGLADAIDWNLNLAAADIPRTIQAHHVMVLPYRESKKLGLLGQQRGTSGALSWAAACGRGAITSDARAFAEEVASGNGAIYPQGDVAALSEQLLNLAREPRLAQAWAERAGAIGHARTWPRTALRFQALFNDMVGTVHGT
Protein: Curli assembly protein CsgC (P0A1Z9)
Organism: Salmonella enteritidis
Function: Plays a role in the extracellular assembly of CsgA (also known as AgfA, AC P0A1E7) into thin aggregative fimbriae (Tafi) fibers. Assembly may also require CsgE (AgfE). Tafi are thought to be assembled via an extracellular nucleation-precipitation (ENP) pathway, and possibly also via an intracellular non-CsgC-dependent pathway.
Subcellular location: Periplasm {ECO:0000269|PubMed:17379722}. Note=Upon overexpression; a small amount is also seen in the cytoplasm.
Interaction partners:
Sequence:
MHTLLLLAALSNQITFTTTQQGDIYTVIPQVTLNEPCVCQVQILSVRDGVGGQSHTQQKQTLSLPANQPIELSRLSVNISSEDSVKIIVTVSDGQSLHLSQQWPPSAQ
Protein: Csh1p (Q59QH2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Wh11p
- Glyoxalase 3
- 17-beta-hydroxysteroid dehydrogenase-like protein
- Adh5p
Sequence:
MVTRLGKSGLKVNTVAVGTMRLGSSWRGFNGDIDECLKILKFCYDNGFRTFDTADTYSNGKSEELLGLFIKKYNIPRERIVILTKCYFSVKDDAEDSSLEIDPIDYMNGKGLSRKHILAAAEASVKRLGTYIDVLQIHRLDHEVTYEEVMRSLNDVVEQGLARYIGASSMKTWEFVELQNVAKANGWHQFISMQSHYSLLYREDERELNDYCKKNSIGLIPWSPNGGGVLCRPFDSEKTKQFLDNKQWSSLFGLENVRDADKIIVDRVKELSVKYNASMMQVSLAWCISKGVIPIAGVSKFEQAEELVGIFKVNLTEDDIKYLEEPYHAKDLARVAA
Protein: LATS1 protein (Large tumor suppressor kinase 1) (Q6PJG3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKRSEKPEGYRQMRPKTFPASNYTVSSRQMLQEIRESLRNLSKPSDAAKAEHNMSKMSTEDPRQVRNPPKFGTHHKALQEIRNSLLPFANETNSSRSTSEVNPQMLQDLQAAGFDEEDHLSVACSPISLTKPFLI
Protein: Cell division protein DedD (P09549)
Organism: Escherichia coli (strain K12)
Function: Non-essential cell division protein that could be required for efficient cell constriction.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02022, ECO:0000305}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02022}. Note=Localizes at the septal ring. {ECO:0000255|HAMAP-Rule:MF_02022, ECO:0000269|PubMed:19684127, ECO:0000269|PubMed:19880599}.
Interaction partners:
- Dihydrofolate synthase/folylpolyglutamate synthase
- Cell division protein DamX
- Cell division protein FtsN
- Endolytic peptidoglycan transglycosylase RlpA
- Cell division protein ZipA
- Ribonuclease T
- Guanylate kinase
- Cell division protein YtfB
- Colicin V production protein
- Cell division protein FtsQ
Sequence:
MASKFQNRLVGTIVLVALGVIVLPGLLDGQKKHYQDEFAAIPLVPKAGDRDEPDMMPAATQALPTQPPEGAAEEVRAGDAAAPSLDPATIAANNTEFEPEPAPVAPPKPKPVEPPKPKVEAPPAPKPEPKPVVEEKAAPTGKAYVVQLGALKNADKVNEIVGKLRGAGYRVYTSPSTPVQGKITRILVGPDASKDKLKGSLGELKQLSGLSGVVMGYTPN
Protein: Cannabinoid receptor 1 (S5TLS4)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}. Presynapse {ECO:0000256|ARBA:ARBA00034106}.
Interaction partners:
Sequence:
MKSILDGLADTTFRTITTDLLYVGSNDIQYEDIKGDMASKLGYFPQKFPLTSFRGSPFQEKMTAGDNPQLVPADQVNITEFYNKSLSSFKENEENIQCGENFMDIECFMVLNPSQQLAIAVLSLTLGTFTVLENLLVLCVILHSRSLRCRPSYHFIGSLAVADLLGSVIFVYSFIDFHVFHRKDSRNVFLFKLGGVTASFTASVGSLFLTAIDRYISIHRPLAYKRIVTRPKAVVAFCLMWTIAIVIAVLPLLGWNCEKLQSVCSDIFPHIDETYLMFWIGVTSVLLLFIVYAYMYILWKAHSHAVRMIQRGTQKSIIIHTSEDGKVQVTRPDQARMDIRLAKTLVLILVVLIICWGPLLAIMVYDVFGKMNKLIKTVFAFCSMLCLLNSTVNPIIYALRSKDLRHAFRSMFPSCEGTAQPLDNSMGDSDCLHKHANNAASVHRAAESCIKSTVKIAKVTMSVSTDTSAEAL
Protein: Palmitoyl-protein thioesterase 1 (PPT-1) (EC 3.1.2.22) (Palmitoyl-protein hydrolase 1) (P50897)
Organism: Homo sapiens (Human)
Function: Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.
Subcellular location: Lysosome {ECO:0000269|PubMed:19941651}. Secreted {ECO:0000250|UniProtKB:P45478}.
Interaction partners:
- Battenin
- Bis
- Ceroid-lipofuscinosis neuronal protein 6
- Protein CLN8
- Tripeptidyl-peptidase 1
- Lysosomal thioesterase PPT2
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- DnaJ homolog subfamily C member 5
- Major facilitator superfamily domain-containing protein 8
- BTB/POZ domain-containing protein KCTD7
Sequence:
MASPGCLWLLAVALLPWTCASRALQHLDPPAPLPLVIWHGMGDSCCNPLSMGAIKKMVEKKIPGIYVLSLEIGKTLMEDVENSFFLNVNSQVTTVCQALAKDPKLQQGYNAMGFSQGGQFLRAVAQRCPSPPMINLISVGGQHQGVFGLPRCPGESSHICDFIRKTLNAGAYSKVVQERLVQAEYWHDPIKEDVYRNHSIFLADINQERGINESYKKNLMALKKFVMVKFLNDSIVDPVDSEWFGFYRSGQAKETIPLQETSLYTQDRLGLKEMDNAGQLVFLATEGDHLQLSEEWFYAHIIPFLG
Protein: Epididymis secretory sperm binding protein (A0A384MDN8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRQLSRARPATVLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDCRVKIDTKAIPLFGNSLKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKNGKQPVGRFFGNTWAEMYRNRYWKEHHFEGIALVEKALQAAYGASAPSMTSATLRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLAAAEEGPLEPAVVDAFNQAWHLVTHECPNYFR
Protein: C-X-C motif chemokine 10 (10 kDa interferon gamma-induced protein) (Gamma-IP10) (IP-10) (C7) (Interferon-gamma induced protein CRG-2) (Small-inducible cytokine B10) (P17515)
Organism: Mus musculus (Mouse)
Function: Pro-inflammatory cytokine that is involved in a wide variety of processes such as chemotaxis, differentiation, and activation of peripheral immune cells, regulation of cell growth, apoptosis and modulation of angiostatic effects (By similarity). Plays thereby an important role during viral infections by stimulating the activation and migration of immune cells to the infected sites. Mechanistically, binding of CXCL10 to the CXCR3 receptor activates G protein-mediated signaling and results in downstream activation of phospholipase C-dependent pathway, an increase in intracellular calcium production and actin reorganization. In turn, recruitment of activated Th1 lymphocytes occurs at sites of inflammation (By similarity). Activation of the CXCL10/CXCR3 axis also plays an important role in neurons in response to brain injury for activating microglia, the resident macrophage population of the central nervous system, and directing them to the lesion site. This recruitment is an essential element for neuronal reorganization.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P02778}.
Interaction partners:
- C-X-C chemokine receptor type 3
- C-X-C motif chemokine 9
- C-C chemokine receptor type 5
- C-C chemokine receptor type 2
- C-C motif chemokine 5
- C-X-C chemokine receptor type 4
- Probable C-C chemokine receptor type 3
- Stromal cell-derived factor 1
- Platelet factor 4
- Chemokine subfamily B Cys-X-Cys
Sequence:
MNPSAAVIFCLILLGLSGTQGIPLARTVRCNCIHIDDGPVRMRAIGKLEIIPASLSCPRVEIIATMKKNDEQRCLNPESKTIKNLMKAFSQKRSKRAP
Protein: UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (EC 2.7.8.15) (GlcNAc-1-P transferase) (G1PT) (GPT) (N-acetylglucosamine-1-phosphate transferase) (Q9H3H5)
Organism: Homo sapiens (Human)
Function: Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P23338}; Multi-pass membrane protein {ECO:0000269|PubMed:29459785, ECO:0000269|PubMed:30388443}.
Interaction partners:
- UDP-N-acetylglucosamine transferase subunit ALG14
- UDP-N-acetylglucosamine transferase subunit ALG13
- Dolichyl-phosphate beta-glucosyltransferase
- Dolichol kinase
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichyldiphosphatase 1
- Dolichol-phosphate mannosyltransferase subunit 3
- Phosphomannomutase 2
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Dol-P-Man:Man
Sequence:
MWAFSELPMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLNKTSRQQIPESQGVISGAVFLIILFCFIPFPFLNCFVKEQCKAFPHHEFVALIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPKPFRPILGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIPRLNIKTGKLEMSYSKFKTKSLSFLGTFILKVAESLQLVTVHQSETEDGEFTECNNMTLINLLLKVLGPIHERNLTLLLLLLQILGSAITFSIRYQLVRLFYDV
Protein: 1,2-phenylacetyl-CoA epoxidase, subunit B (1,2-phenylacetyl-CoA monooxygenase, subunit B) (P76078)
Organism: Escherichia coli (strain K12)
Function: Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit B may play a regulatory role or be directly involved in electron transport.
Interaction partners:
- Putative 1,2-phenylacetyl-CoA epoxidase, subunit D
- Acyl-coenzyme A thioesterase PaaI
- 1,2-phenylacetyl-CoA epoxidase, subunit A
- 1,2-phenylacetyl-CoA epoxidase, subunit C
- 1,2-phenylacetyl-CoA epoxidase, subunit E
- 1,2-epoxyphenylacetyl-CoA isomerase
- Phenylacetate-coenzyme A ligase
- Bifunctional protein PaaZ
- 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase
- 2,3-dehydroadipyl-CoA hydratase
Sequence:
MSNVYWPLYEVFVRGKQGLSHRHVGSLHAADERMALENARDAYTRRSEGCSIWVVKASEIVASQPEERGEFFDPAESKVYRHPTFYTIPDGIEHM
Protein: Dishevelled binding antagonist of beta catenin 3 (Thymus expressed gene 3-like, isoform CRA_b) (G5E9H6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MIRAFSFPVSPERGRLRGWLEGSLAGLCELHWLRERQEYRVQQALRLAQPGMGGAEAEDEEDADEDEDAAAARRAAAALEEQLEALPGLVWDLGQQLGDLSLESGGLEQESGRSSGFYEDPSSTGGPDSPPSTFCGDSGFSGSSSYGRLGPSEPRGIYASERPKSLGKVGEGGALGPGKGQ
Protein: GTP cyclohydrolase 1 (EC 3.5.4.16) (GTP cyclohydrolase I) (Q9SFV7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: GTP cyclohydrolase 1 is the first enzyme in the biosynthetic pathway leading to folic acid.
Interaction partners:
- Folate synthesis bifunctional protein
- Folate synthesis bifunctional protein
- Probable dihydroneopterin aldolase 3
- Dihydroneopterin aldolase 1
- Dihydroneopterin aldolase 2
- Protein HOMOLOG OF MAMMALIAN LYST-INTERACTING PROTEIN 5
- Folylpolyglutamate synthase
- Dihydrofolate synthetase
- Folylpolyglutamate synthase
- Folylpolyglutamate synthase
Sequence:
MGALDEGCLNLELDIGMKNGCIELAFEHQPETLAIQDAVKLLLQGLHEDVNREGIKKTPFRVAKALREGTRGYKQKVKDYVQSALFPEAGLDEGVGQAGGVGGLVVVRDLDHYSYCESCLLPFHVKCHIGYVPSGQRVLGLSKFSRVTDVFAKRLQDPQRLADDICSALQHWVKPAGVAVVLECSHIHFPSLDLDSLNLSSHRGFVKLLVSSGSGVFEDESSNLWGEFQSFLMFKGVKTQALCRNGSSVKEWCPSVKSSSKLSPEVDPEMVSAVVSILKSLGEDPLRKELIATPTRFLKWMLNFQRTNLEMKLNSFNPAKVNGEVKEKRLHCELNMPFWSMCEHHLLPFYGVVHIGYFCAEGSNPNPVGSSLMKAIVHFYGFKLQVQERMTRQIAETLSPLVGGDVIVVAEAGHTCMISRGIEKFGSSTATIAVLGRFSSDNSARAMFLDKIHTTNALKTESSSPF