wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) (Deubiquitinating enzyme 14) (Ubiquitin thioesterase 14) (Ubiquitin-specific-processing protease 14) (P54578)
Organism: Homo sapiens (Human)
Function: Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs) (By similarity). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19106094}. Cell membrane {ECO:0000269|PubMed:19106094}; Peripheral membrane protein {ECO:0000269|PubMed:19106094}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome regulatory subunit 4
- 26S proteasome regulatory subunit 10B
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 6
- Ubiquitin carboxyl-terminal hydrolase isozyme L5
Sequence:
MPLYSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGNIKIKNGMTLLMMGSADALPEEPSAKTVFVEDMTEEQLASAMELPCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQYLQQDANECWIQMMRVLQQKLEAIEDDSVKETDSSSASAATPSKKKSLIDQFFGVEFETTMKCTESEEEEVTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVLKDVKFPLMLDMYELCTPELQEKMVSFRSKFKDLEDKKVNQQPNTSDKKSSPQKEVKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ
Protein: Scinderin like a (A0JMJ1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MVFHKEFQNAGKEPGLQIWRIEKMDLKLVPKQLHGNFFTGDAYVVLFTSPAPSYNVHMWLGNECSQDESGAAAIFAMQLDDHLGGAPVQYREVQNNESVTFLGYFKTGIKYKQGGVSSGFNHVVSNEMNTKRVLHIKGRRAIRATEVNMSWASFNHGDCFILDLGKDIYQWCGSKCNRFERLKASEVSIGIRDNERNGRATLHIVEDGSEPDVFSNTLGPKPSIPEGSPDDETTDRNNQKKASLHMVSDAAGSMKTSEVKQNSPFKQELLNPSDCYILDNGLDSKIFVWKGPRANTEERKSAMKVAEQFIKEKNYPKNTQIQVMPGGGETTLFKQFFSNWKDKDQSTGPGQAYSIGRIARVSQVPFDASSLHSNKVMAAQHGMVDDGSGKVQVWRVEGNDRVPVDPSSFGQFFGGDCYLILYTYLNGGREQHIIYTWQGLKCTQDELTASAFLTVKLDDSMGGAPVQVRVTQGQEPAHLMSLFKGKPMIIHLGGTSRKGGQSRVGTTRLFHIRQSSTRATRAVEVEPCASKLNTNDVFVLKFPEGMFLWKGVGASEEEIAAAKYVCSILGGSATEISEGKEPAAFWSSLGGKKDYQTSKNLQKTVKLPRLFGCSNKTGRLIAEEVPGDLTQSDLATDDVMLLDTWDQIFLWIGNDANVEEKIGSAKIAKDYVDSDPSKRQGIPIITIKQGFEPPSFTGWFQAWDSKMWDTDPMDRIRGRY
Protein: Stromal interaction molecule 2 (A0A8I6A6S4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MNAAGCRAPRAAGEGSGLAPGGSLLPRRRGPGQLAASECPAAPVSAPPAAAPGRALGRPSRRRWAAMLLFGLLVAGVADGCDLVPRHLRGRRASGSAGAAASPSAAAAGERQALLTDPCMSLSPPCFTEEDRFSLEALQTIHKQMDDDKDGGIEVDESDEFIREDMKYKDATNKHSHLHREDKHITVEDLWKQWKTSEVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHETSFMISQLKISDRSHRQKLQLKALDVVLFGPLTRPPHNWMKDFILTISIVIGVGGCWFAYTQNKTSKEHVAKMMKDLESLQTAEQSLMDLQERLEKAQEENRTVAVEKQNLERKMMDEINYAKEEACRLRELREGAECELSRRQYAEQELEQVRMALKKAEKEFELRSSWSVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEVAASYLMQAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKICGFQIAHNSGLPSLTSSLYSDHSWVVMPRVSIPPYPIAGGVDDLDEDTPPIVSQFPGTVAKPAGSLARSSSLCRSRRSIVPSSPQSQRAQLPAHAPLAAHPRHPHHPQHSLPSPDPDILSVSSCPALYRNEEEEEAIYFTAEKQWEVPDTASECDSLNSSIGRKQSPPSSLEIYQTLSSRKISRDELSLEDSSRGDSPVTADVSRGSPECVGLTETKSMIFSPASRVYNGILEKSCSMHQLSSGIPVPNPRHTSCSLAGSDSKPVQEASSVSRVGSIPHDLCHNGEKSKKPSKIKSLFKKKSK
Protein: HTH-type transcriptional regulator XynR (Regulator of xylonate catabolism) (P77300)
Organism: Escherichia coli (strain K12)
Function: Involved in regulation of xylonate catabolism. Represses the expression of both yagA and yagEF operons. Binds mainly at a single site within the spacer of the bidirectional transcription units yagA and yagEF.
Interaction partners:
Sequence:
MPIIQSVERALQILDLFNEQATELKITDISKLMGLSKSTLHSLLKTLQLHGYIDQNPENGKYRLGMKLVERGHFVVGSIDIRQKAKGWLTELSRRTGQTTHLGILDGREGVYIEKIEGKLAAIAYSRIGRRLPVHATAIGKVLIAWLGEAELNALLEGYQYTTFTPATLASREALMSALAQTREQGYALDSEENEQGVRCVAVPVWNHESRVIAALSLSTLTSRVDDAELANFREQLQQAGLALSRALGYPA
Protein: Transmembrane protein (Q382P5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MESKTWFGSQEVDGSDHGLAASDGASLVEHVRDILMDSDDDVVSVSCVNLFVKTETTSRAVIENEEYLARHSTGRDFRRGATIFSARSSSHSMSRFTTAGTFSSGSKEIEYGVLSMQPSVCVGVDRDVPLKEKVDSFHCGCVGVVSAVTDVRRSVSGLRSSKLVATGDRCVADCGDQEPLLGAGRGPFGGNGDSSILERTYGTLDGLHSVTAERFVDEPLVAAGRWDSYCSEEFPVFVDGDVFRCLFCGSEVHLIQGSPSDVFVPEALVSESNSSFGLRRAVVHVFAVFIISMLMLHHESYNVFKTNPFVDNLLGGKCMMLKLMSFHAIAVSSLLVVFCFRGVWEVPHVVLLVSTAMLVVDDFRLLYGVLLNVTTSFVVRELVQAASFVGSFASLLLFTCADVGYVAGPPFLALSVCLAWLMSRLVAFGVLPAFATTAAAGYTAIIHTVLALVSFSLAIGICLLLPPSMLQPGPCSCGKSHYVTNFLSCLGRLDPSFFIRSVACGCLVAVVSLLTVDSELVTLPVLDSLHFKATDIPVVDGSGNWPNGIAISPVVVLLLSTLALLLLCLVPSMGPFVRFVELGPATAAMVLIVAFFFDGKQLTATLAAVCAFSFAIAVGGLLRSLGAVFLSRTVVRDNFGKATVRPTAALFTTVLPVLLVTAVCSSCVALILGLTAWLAAVRGNGNDSGDGTADRRGWAVMFVVLVFSSVALALQLLVGMWWWLPRLYKRIAGIV
Protein: Neuropeptide Y receptor Y8a (Neuropeptide Y/peptide YY receptor Yc) (O73734)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEANITNISSGTGQKSWVESNVCPPSVSGTTLLIVAYSTVIAVGLVGNTCLVFIISRQKEMRNVTNILIANLSCSDILMCVVCLPVTVIYTLMDRWILGETLCKVTPFVQCMSVTVSIFSLVLIALERHQLIIHPTGWTPAAGHSYLAVAVTWMVACFISLPFLSFNILTNAPFQNISLPFNPFSDHVICMELWPSERNRLAYTTSLLLFQYCLPLLLILLCYLRIFLRLRRRKDMVEQATEARQRKARGAQRVNAMLVVIVVAFALCWLPLNVFNTIFDWYHQALPACQHDVIFSACHLTAMASTCVNPVVYGFLNTNFQKELKATLQRCNCGWGVPETYESFPLSTVATDVSKVSSMQHGSLIRSEQCAHC
Protein: Insulin-like growth factor binding protein 2 (C9E9W3)
Organism: Bos taurus (Bovine)
Interaction partners:
Sequence:
MQPRLGGPALLLLPPLLLLLLLGAGGGDCGARAEVLFRCPPCTPESLAACKPPPGAAAGPAGDARVPCKLVREPGCGCCSVCARLEGERCGVYTPRCGQGLRCYPNPGSELPLRALVHGEGTCEKHGDAEYSASPEQVA
Protein: Nuclear pore complex protein Nup85 (85 kDa nucleoporin) (Nucleoporin Nup85) (Pericentrin-1) (Q4QQS8)
Organism: Rattus norvegicus (Rat)
Function: Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP96/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2-activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol 3-kinase-Rac-lammellipodium protrusion cascade. Involved in nephrogenesis.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}. Note=During mitosis, localizes to the kinetochores and spindle poles. Upon CCl2 stimulation translocates from the cytoplasm to the membrane and colocalizes with CCR2 at the front of migrating cells. {ECO:0000250|UniProtKB:Q9BW27}.
Interaction partners:
- LOC683983 protein
- Nucleoporin 160
- Nuclear pore complex protein Nup133
- Nuclear pore complex protein Nup98-Nup96
- Protein SEC13 homolog
- Nuclear pore complex protein Nup107
- Nucleoporin Nup37
- Nucleoporin 205
- Nuclear pore complex protein Nup155
- Nuclear pore complex protein Nup93
Sequence:
MEELDCEPAVTWIPGVNSKKKQMCFDWGPGEMLLCETSFNKTDKSEKVPSCPFIYIIRKDVDVYSQILRKLFNESHGIFVGLQRLEEELSGKSRKAQLVRVSKNYRSVIRACMEEMHQVAIAAKDPASGRQFSSQVSILSAMELIWNLCEILFIEVAPAGPLLLHLLDWVRLHVCEVDSLSADVLGSDHPSKHESFWNLVTVLVLQGRLDEARQMLSKEADASPSSAGMCRVLGDLMRTMPILSPGNTQTLTELELKWQHWREECERHLQDNTFAANPHLESLCKIMLGDEATLLEQKELMSNWYHFLVTRLLYSNPTVKPTDLHLYAQSSLDMFLGGESSPEPLDNILMAAFEFDIHQVIKECSIALSNWWFVAHLTDLLDHCRLLQSHNLYFGSNMREFLLLEYASGLFAHHSLWQLGVDYFDYCPELGRVSLELHIERIPLNTEQKALKVLRICEQRQMTEQVGSICKILAMKAVRNNRLGSALSWSIRAKDAAFATLVSDRFLRDYCERGCFSDLDLIDNLGPAMMLSDRLTFLGKYREFHRLYGEKRFGDAASLLLSLMTSQIAPRSFWMTLLTDALPLLEQKQVIFSAEQTYELMRCLEDLASRRPECGEPDAQRLQDDDIETTKVEMLRLALARNLARAIIREGSLEGS
Protein: Protein COFACTOR ASSEMBLY OF COMPLEX C SUBUNIT B CCB2, chloroplastic (Protein HIGH CHLOROPHYLL FLUORESCENCE 208) (Q9FJ81)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the biogenesis and accumulation of native cytochrome b6 in the thylakoid membrane. Controls the conversion of apocytochrome b6 to holocytochrome b6. Required for covalent binding of the c-type heme to cytochrome b6.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305|PubMed:18593701}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Photosystem II stability/assembly factor HCF136
- Protein HIGH CHLOROPHYLL FLUORESCENCE PHENOTYPE 173
- Protein high chlorophyll fluorescent 107
- Cytochrome b
- Rho-N domain-containing protein 1
- Cytochrome b
Sequence:
MSIQICNFPFHPKFALQPRAQRSTRIFARTENDSPQSKTSDQQLNLSVLRFTFGIPGFDESYLPRWIGYGFGSLLLLNHFSASAPISESQMRSEALGLSLAAFSIALPYIGKFLKGSVVEQRSLPEEGEQVFVISSNIGDSLKEDLAWATYVLLRNTSTIAVLISVQGELCVRGYWNCPDQMSKAQLHDWFKKKVDEIGLADVKETLYFPQYAGSALSLDILPDGTRSLFVQPLVQNTNEPQKVNGFLLVASTAGYAYSDKDRAWIGAMAEKFRG
Protein: L-cystine-binding protein TcyJ (CBP) (Protein FliY) (Sulfate starvation-induced protein 7) (SSI7) (P0AEM9)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex TcyJLN involved in L-cystine import. This high affinity cystine transporter is involved in resistance to oxidative stress by forming a L-cysteine/L-cystine shuttle system with the EamA transporter, which exports L-cysteine as reducing equivalents to the periplasm to prevent the cells from oxidative stress. Exported L-cysteine can reduce the periplasmic hydrogen peroxide to water, and then generated L-cystine is imported back into the cytoplasm via the TcyJLN complex. Functions at low cystine concentrations. The system can also transport L-cysteine, diaminopimelic acid (DAP), djenkolate, lanthionine, D-cystine, homocystine, and it mediates accumulation of the toxic compounds L-selenaproline (SCA) and L-selenocystine (SeCys). Binds cystine and DAP.
Subcellular location: Periplasm {ECO:0000305|PubMed:20351115}.
Interaction partners:
- L-cystine transport system ATP-binding protein TcyN
- L-cystine transport system permease protein TcyL
- Glutamine transport system permease protein GlnP
- Glutamate/aspartate import permease protein GltK
- Arginine ABC transporter permease protein ArtQ
- Arginine ABC transporter permease protein ArtM
- Histidine/lysine/arginine/ornithine transport system permease protein HisM
- Inner membrane amino-acid ABC transporter permease protein YhdY
- Histidine/lysine/arginine/ornithine transport system permease protein HisQ
- Glutamate/aspartate import permease protein GltJ
Sequence:
MKLAHLGRQALMGVMAVALVAGMSVKSFADEGLLNKVKERGTLLVGLEGTYPPFSFQGDDGKLTGFEVEFAQQLAKHLGVEASLKPTKWDGMLASLDSKRIDVVINQVTISDERKKKYDFSTPYTISGIQALVKKGNEGTIKTADDLKGKKVGVGLGTNYEEWLRQNVQGVDVRTYDDDPTKYQDLRVGRIDAILVDRLAALDLVKKTNDTLAVTGEAFSRQESGVALRKGNEDLLKAVNDAIAEMQKDGTLQALSEKWFGADVTK
Protein: Isovaleryl-CoA dehydrogenase, mitochondrial (IVD) (EC 1.3.8.4) (Butyryl-CoA dehydrogenase) (EC 1.3.8.1) (P26440)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of isovaleryl-CoA/3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA as an intermediate step in the leucine (Leu) catabolic pathway. To a lesser extent, is also able to catalyze the oxidation of other saturated short-chain acyl-CoA thioesters as pentanoyl-CoA, hexenoyl-CoA and butenoyl-CoA.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P12007}.
Interaction partners:
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Peroxisomal bifunctional enzyme
- Trifunctional enzyme subunit alpha, mitochondrial
- Enoyl-CoA delta isomerase 2
- Electron transfer flavoprotein subunit beta
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
Sequence:
MAEMATATRLLGWRVASWRLRPPLAGFVSQRAHSLLPVDDAINGLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNADFH
Protein: Unconventional myosin-Va (Dilute myosin heavy chain, non-muscle) (Q9QYF3)
Organism: Rattus norvegicus (Rat)
Function: Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation.
Interaction partners:
- Melanophilin
- Ras-related protein Rab-27A
- RILP-like protein 2
- Rab effector MyRIP
- Ras-related protein Rab-11A
- Ras-related protein Rab-3A
- Glutamate receptor 1
- Calmodulin-1
- Spire-type actin nucleation factor 2
- Dynein light chain 2, cytoplasmic
Sequence:
MAASELYTKFARVWIPDPEEVWKSAELLKDYKPGDKVLLLHLEEGKDLEYRLDPKTSELPHLRNPDILVGENDLTALSYLHEPAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLIIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVGHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTRVPVKPTKGRPGQTAKEHKKTVGLQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLGDRKQTCQNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGWLLRKRYLCMQRAAITVQRYVRGYQARCYAKFLRRTKAATTIQKYWRMYVVRRKYKIRRAATIVLQSYLRGYLARNRYRKILREHKAVIIQKRVRGWLARTHYKRTMKAIIYLQCCFRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETEQLVSNLKEENTLLKQEKETLNHLMVEQAKEMTETMERKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMLNVPKPGHKRTDSTHSSNESEYTFSSEFAETEDIAPRTEEPTEKKVPLDMSLFLKLQKRVTELGQEKQLMQDELDRKEEQVLRSKAKGGERPQIRGAELGYESLKRQELESENKKLKNELNELRKALSEKSAPEVNAPGAPAYRVLMEQLTAVSEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENISPGQIIDEPIRPVNIPRKGKDFQGMLEYKREDEQKLVKNLILELKPRGVAVNLISGLPAYILFMCVRHADYLDDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFIRTIQVRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFIARV
Protein: Kinesin light chain (E9PQ02)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|RuleBase:RU367020}.
Interaction partners:
Sequence:
MAMMVFPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLVAPEAGEAEPGSQERCILLRRSLEAIELGLGEAQEEKGDVPKDTLDDLFPNEDEQSPAPSPGGGDVSGQHGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKEAAHLLNDA
Protein: Uncharacterized protein (Q8HCP1)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MSRASSYAAGSSFVVSREAPVKRIVGLAFQYWKLELQIGITTLGFKTTTSASFFAHRGSFVNSPEDHWNRNQYPWPHNSNLPNYSTYIPNHYPPPQNESNPGQGPCNCTSMPNPMWVANYTVQILVSKPMIQGPCHKINSKNIIIRTRFLLIS
Protein: Glutathione hydrolase 1 proenzyme (EC 3.4.19.13) (Gamma-glutamyltransferase 1) (Gamma-glutamyltranspeptidase 1) (GGT 1) (EC 2.3.2.2) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) (CD antigen CD224) [Cleaved into: Glutathione hydrolase 1 heavy chain; Glutathione hydrolase 1 light chain] (P19440)
Organism: Homo sapiens (Human)
Function: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates (such as maresin conjugate (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate, MCTR1) and other gamma-glutamyl compounds (such as leukotriene C4, LTC4). The metabolism of glutathione by GGT1 releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Contributes to cysteine homeostasis, glutathione homeostasis and in the conversion of the leukotriene LTC4 to LTD4.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23682772, ECO:0000269|PubMed:8095045}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P07314}.
Interaction partners:
- Gamma-glutamylcyclotransferase
- Glutathione synthetase
- Glutathione hydrolase 6
- Aminopeptidase N
- Glutamate--cysteine ligase catalytic subunit
- 5-oxoprolinase
- Glutamate--cysteine ligase regulatory subunit
- Glutathione reductase, mitochondrial
- Glutathione hydrolase 7
- Cytosol aminopeptidase
Sequence:
MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCSKIGRDALRDGGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALENKRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKDIQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSRESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISDDTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNEMDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTATALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY
Protein: Uncharacterized protein (Q57W44)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- RNA-binding protein
Sequence:
MDESNRVPTGEAPSDEPPLKVRRHEGGHGELRETSSGDTNPQGATLFIRCTSIHGRGELLNGFISEHREALGVAKWYNVAGDESDGRCVPTLRTDAPFECVYVRSSRKPYFLLEFNEKGDVAKKFVEKLVGLRNTLYKGSPVFVEVAKGGLTVATERLKLEKRDAARRSATAVPLSFSSDKPTGPTAFVPRAVRKR
Protein: DNA replication licensing factor MCM2 (EC 3.6.4.12) (Minichromosome maintenance protein 2) (OsMCM2) (Q2R482)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells. Can complement the fission yeast mcm2 mutant.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM4
- Origin of replication complex subunit 1
- Os05g0173700 protein
- DNA replication licensing factor MCM3
- Cell division control protein 6 homolog
- Probable DNA helicase MCM8
- DNA replication licensing factor MCM6
- Origin of replication complex subunit 2
Sequence:
MDDSENNAPSTPGSPGFSTDRLPPNTTTSRGATDPSSYSDDDDDDVVGAEEAEVDPNVLPEDDGVVAAEEEEDGEDLFNDNYLDDYRRMDEQDQYESVGLDDSIEDERNLDEIMADRRAAEAELDARDVRTGAAPDRKLPRMLHDQDTDEDMSFRRPKRHRANFRPPREPRTPRSDDDGDGATPSSPGRSQRGMYSGGDVPMTDQTDDDPYEDEFDEEDEMNMYRVQGTLREWVTRDEVRRFIAKKFKEFLLTYVNPKNEQGEFEYVRLINEMVLANKCSLEIDYKQFIYIHPNIAIWLADAPQSVLEVMEEVAKNVVFDLHKNYRNIHQKIYVRITNLPVYDQIRNIRQIHLNTMIRIGGVVTRRSGVFPQLQQVKFDCSKCGTVLGPFFQNSYTEVKVGSCPECQSKGPFTINVEQTIYRNYQKLTLQESPGIVPAGRLPRYKEVILLNDLIDCARPGEEIEVTGIYTNNFDLSLNTKNGFPVFATVVEANYVAKKQDLFSAYKLTDEDKAEIEKLAKDPRIGERIVKSIAPSIYGHEDIKTAIALAMFGGQEKNVKGKHRLRGDINVLLLGDPGTAKSQFLKYVEKTGHRAVYTTGKGASAVGLTAAVHKDPVTREWTLEGGALVLADRGICLIDEFDKMNDQDRVSIHEAMEQQSISISKAGIVTSLQARCSVIAAANPIGGRYDSSKTFTQNVELTDPIISRFDVLCVVKDIVDPFTDEMLARFVVDSHARSQPKGANLEDRVPTDVEDDPLAAARQADPDILSQDMLKKYITYAKLNVFPKIHDADLDKISHVYAELRRESSHGQGVPIAVRHIESIIRMSEAHARMHLRSYVSQEDVDMAIRVLLDSFISTQKFGVQKALQKNFRKYMTYKKDYNELLLLLLRTLVKDVLHFEEIVSGPTTRLTHIEVKVEDLKNKAQEYEIYDLRPFFSSAHFRDNNFVLDEGRGIIRHPLAA
Protein: Bifunctional protein PyrR [Includes: Pyrimidine operon regulatory protein; Uracil phosphoribosyltransferase (UPRTase) (EC 2.4.2.9)] (P9WHK3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Regulates the transcription of the pyrimidine nucleotide (pyr) operon in response to exogenous pyrimidines.
Interaction partners:
- Aspartate carbamoyltransferase catalytic subunit
- Orotidine 5'-phosphate decarboxylase
- Dihydroorotase
- Uracil phosphoribosyltransferase
- Carbamoyl phosphate synthase large chain
- Carbamoyl phosphate synthase small chain
- Probable export or membrane protein
- Uridylate kinase
- Thymidine phosphorylase
- Purine nucleoside phosphorylase
Sequence:
MGAAGDAAIGRESRELMSAADVGRTISRIAHQIIEKTALDDPVGPDAPRVVLLGIPTRGVTLANRLAGNITEYSGIHVGHGALDITLYRDDLMIKPPRPLASTSIPAGGIDDALVILVDDVLYSGRSVRSALDALRDVGRPRAVQLAVLVDRGHRELPLRADYVGKNVPTSRSESVHVRLREHDGRDGVVISR
Protein: Organic cation/carnitine transporter 2 (High-affinity sodium-dependent carnitine cotransporter) (Solute carrier family 22 member 5) (O76082)
Organism: Homo sapiens (Human)
Function: Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Relative uptake activity ratio of carnitine to TEA is 11.3. In intestinal epithelia, transports the quorum-sensing pentapeptide CSF (competence and sporulation factor) from Bacillus Subtilis wich induces cytoprotective heat shock proteins contributing to intestinal homeostasis. May also contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (Probable).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10679939, ECO:0000269|PubMed:17509700, ECO:0000269|PubMed:33334877}; Multi-pass membrane protein {ECO:0000269|PubMed:10679939}. Apical cell membrane {ECO:0000269|PubMed:10966938, ECO:0000269|PubMed:20722056}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000269|PubMed:35307651}; Multi-pass membrane protein {ECO:0000255}. Note=In intestinal cells, apical expression is induced by TNF. Localized to the basal membrane of Sertoli cells (PubMed:35307651). {ECO:0000269|PubMed:20722056, ECO:0000269|PubMed:35307651}.; SUBCELLULAR LOCATION: [Isoform 3]: Endoplasmic reticulum {ECO:0000269|PubMed:17509700}.
Interaction partners:
- Nucleotide-binding oligomerization domain-containing protein 2
Sequence:
MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFTGLSSVFLIATPEHRCRVPDAANLSSAWRNHTVPLRLRDGREVPHSCRRYRLATIANFSALGLEPGRDVDLGQLEQESCLDGWEFSQDVYLSTIVTEWNLVCEDDWKAPLTISLFFVGVLLGSFISGQLSDRFGRKNVLFVTMGMQTGFSFLQIFSKNFEMFVVLFVLVGMGQISNYVAAFVLGTEILGKSVRIIFSTLGVCIFYAFGYMVLPLFAYFIRDWRMLLVALTMPGVLCVALWWFIPESPRWLISQGRFEEAEVIIRKAAKANGIVVPSTIFDPSELQDLSSKKQQSHNILDLLRTWNIRMVTIMSIMLWMTISVGYFGLSLDTPNLHGDIFVNCFLSAMVEVPAYVLAWLLLQYLPRRYSMATALFLGGSVLLFMQLVPPDLYYLATVLVMVGKFGVTAAFSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYFVYLGAYDRFLPYILMGSLTILTAILTLFLPESFGTPLPDTIDQMLRVKGMKHRKTPSHTRMLKDGQERPTILKSTAF