wanglab/gogpt-training-data huggingface dataset:
Protein: Autophagy-related protein 13 homolog (Q9VHR6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Autophagy factor required for autophagosome formation. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of Atg13 and Atg1. The Atg1-Atg13 complex functions at multiple levels to mediate and adjust nutrient-dependent autophagic signaling. Involved in the autophagic degradation of dBruce which controls DNA fragmentation in nurse cells.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Preautophagosomal structure {ECO:0000250}. Note=Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome. {ECO:0000250}.
Interaction partners:
- RB1-inducible coiled-coil protein 1
- Autophagy-related protein 101
- Autophagy-related 1, isoform B
- Autophagy-related 14
- Autophagy-related protein 9
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Raptor, isoform B
- Autophagy-related 8a, isoform A
- non-specific serine/threonine protein kinase
- Autophagy protein 5
Sequence:
MSAQRLNAAERDLEKFIKFLVLKSTQVVVQSRLGEKMQTQCNPLAGSDWFNIAVQDHPEVLDETKRALNLKTGESILQRLPLCVEISLKTTEGDQMVLEVWSLDLLQPQNGASPATNDLNPEGQTLKAAHAIYNRMGIMLKSLISLTRTTPAYKLSRRQCPDSYGIFYRIYVDRPQVHTLGEGHKHVKIGQLSTIVGSLVMSVAYRTKLTISPTAAQSESNTIMLKSDHFRPATDANTPGNQQQTQNGTVVAKKLGLGALNPAQGTADRRFIDIEKPLRPGAFTDMGKLKQYTEDDFVLPETPPFEWLLRGRGSVESLNRLDNNSVASVNISNNNNSTQDSKFNQISNLNNNSAGFKSFEKNSENSVSPIKSLLIPASATATYRHHSEPSLQPPPDDDNLLKELHFPFASPTSHVNDLAKFYRECYHAPPLKGLNELQAEISSISSTPPASSGSGGVAACGPTAAATAIATSSADASAMDDLSRQLEQFETSLEDYDKLVSQFGLTGSSSTGSRSSGGLQMSN
Protein: Endopolygalacturonase B (EC 3.2.1.15) (Pectinase B) (Polygalacturonase B) (Q5B508)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Exopolygalacturonase X-2
- Exopolygalacturonase X-1
- Probable exopolygalacturonase Bgalacturonohydrolase B)
- Probable endopolygalacturonase D
- Endopolygalacturonase AN8327
- Pectinesterase A
- NAD binding Rossmann fold oxidoreductase, putative
- Exo-1,4-beta-xylosidase xlnD
- Exo-1,4-beta-xylosidase bxlB
- Alpha-L-arabinofuranosidase B
Sequence:
MHFLQNSLIAAAMGAALVAAAPAADLDARSSCTFTSASAAKSGASKCSTVTLKSIQVPAGETLDLTGLKSGATVIFEGETTFGYKEWKGPLISMSGDKITVKQASGAKINCDGARWWDTKGSNGGKTKPKFFSAHKLNNSKIQGLKIYNTPVQGFSIQSDHLTISDVTIDNSAGTSKGHNTDAFDIGSSTYITIDGATVYNQDDCIAINSGEHITFTNGYCSGGHGLSIGSVGGRSDNTVKSVTISNSKVVDSQNGVRIKTVYKATGSVTDVTFQDIELSGITKYGLIVEQDYENGSPTGTPTNGVEVEDITFKKITGSVDSSATRVNILCGSGSCKDWTWSGVDITGGKKSSKCKNVPSGASC
Protein: Proteasome subunit beta (A0A140VJS6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU004203}. Nucleus {ECO:0000256|RuleBase:RU004203}.
Interaction partners:
Sequence:
MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS
Protein: Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 (EC 2.7.4.24) (Diphosphoinositol pentakisphosphate kinase 1) (Histidine acid phosphatase domain-containing protein 2A) (InsP6 and PP-IP5 kinase 1) (VIP1 homolog) (P0C644)
Organism: Rattus norvegicus (Rat)
Function: Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated when cells are exposed to hyperosmotic stress.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6PFW1}. Cell membrane {ECO:0000250|UniProtKB:Q6PFW1}. Note=Relocalizes to the plasma membrane upon activation of the PtdIns 3-kinase pathway. {ECO:0000250|UniProtKB:Q6PFW1}.
Interaction partners:
- Inositol hexakisphosphate kinase 1
- Kinase
- Inositol hexakisphosphate kinase 2
- Inositol-pentakisphosphate 2-kinase
- Pituitary adenylate cyclase-activating polypeptide
- Small nuclear ribonucleoprotein Sm D3
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16
- Splicing factor 3A subunit 1
- U6 snRNA-associated Sm-like protein LSm4
- NHP2-like protein 1
Sequence:
MWSLTANEDEDESATAHFFLGAGDEGLGTCGIGMRTGESDSELLEDEEDEVPPEPQIIVGICAMTKKSKSKPMTQILERLCRFDYLTVVILGEDVILNEPVENWPPCHCLISFHSKGFPLDKAVAYSKLRNPFLINDLTMQYYIQDRREVYRILQEEGIDLPRYAVLNRDPACPEECNLIEGEDQVEVNGAVFPKPFVEKPVSAEDHNVYIYYPSSAGGGSQRLFRKIGSRSSVYSPESSVRKTGSYIYEEFMPTDGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEVRYPVMLTAMEKLVARKVCVAFKQTVCGFDLLRANGHSFVCDVNGFSFVKNSMKYYDDCAKILGNTIMRELAPQFQIPWSIPTEAEDIPIVPTTSGTMMELRCVIAIIRHGDRTPKQKMKMEVTHPRFFALFEKHGGYKTGKLKLKRPEQLQEVLDITRLLLAELEKEPGAEIEEKTGKLEQLKSVLEMYGHFSGINRKVQLTYYPHGVKASSEGQDLQREPPAPSLLLVLKWGGELTPDGRVQAEELGRAFRCMYPGGQGDYAGFPGCGLLRLHSTFRHDLKIYASDEGRVQMTAAAFAKGLLALEGELTPILVQMVKSANMNGLLDSDSDSLSSCQHRVKARLHHILQQDAPFGPEDYDQLAPTGSTSLLNSMSVIQNPVKVCDQVFALIENLTHQIRERMQDPSSVDLQLYHSETLELMLQRWSKLERDFRQKSGRYDISKIPDIYDCVKYDVQHNGSLGLQGTAELLRLSKALADVVIPQEYGISREEKVEIAVGFCLPLLRKILLDLQRTHEDESVNKLHPLYSRGVLSPGRHVRTRLYFTSESHVHSLLSVFRYGGLLDETKDAQWQRALAYLSAISELNYMTQIVIMLYEDNTRDPLSEERFHVELHFSPGVKGVEEGSAPAGCGFRPASSENEEMKTDPGSIENLCPAKPSDEPDRALQTSPQPVEGTGLPRRSPLIRNRKAGSMEVLSETSSSRPGGYRLFSSSRPPTEMKQSGLGSQCTGLFSTTVLGGSSSAPNLQDYARTHGKKLPPAGLKHRDELLFVPAVKRFSVSFAKHPTNGFEGCSMVPTIYPLETLHNALSLRQVSEFLTKVCQRHTDAHAQASAALFDSMHNHQASDNPFSPPRTLHSPPLQLRHRSEKPPWYSSGPSSTVSSAGPSSPTTVDGNSHFGFSDQSSVNTQMIEEKQGLGLLQETPGDGTPEFHIELAESTQSPQEPPVEISPPGSQDDTEVNQTCQEVPDTIQPCHDILEEIGQPNQEVPDISQLLLKNHDTATNTCQPCQASQLSKKVYEEICQLCQDNPEESNQLCQEVSVELGRMVHRFPVSIGSTTQETLMEIGRPTQEIPEEPCQEFSEKVGMLTQKASAISELSQDILETDNPSQELSEETDLQAQEVSEEIDQEPEVVDELSNEDIS
Protein: IF rod domain-containing protein (A0A060XL43)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- IF rod domain-containing protein
- BAF nuclear assembly factor 1
- Barrier-to-autointegration factor-like protein
- BAF nuclear assembly factor 1
- Uncharacterized protein
- Uncharacterized protein
- Caspase 7, apoptosis-related cysteine peptidase
- Elongation factor 1-alpha
Sequence:
MNRTTSRQTTSSSSYKRMFGGEGRPSVGMARSTLSSRHVSSAPPSIYASKNVRLRSSAPMPRLSSDTVDFALSDAINSEFKANRTNEKAEMQHLNDRFASYIDKVRFLEQQNKILLAELEQLKGKGASRIGDLYEDEMRDLRRQVDQLTNEKAHVEVDRDNMGEDIERLREKLQDEMIQKEEAEHNLQSFRQDVDNASLARLDLERKVESLQEEIIFLRKLHDEEVAELQAQIQDQHVQIDMDVAKPDLTAALRDVRVQYETLASRNLQDSEDWYKSKFADLSEAANRNTDAIRQAKQEANEYRRQVQALTCEVDSLKGTNESMERQMRELEESFGCEANNFQDTISRLEDDIRNMKDEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRITTPMPNFSSFNLRESMLEARPMIDNLSKKVVIKTIETRDGHVINESTQNHDDLE
Protein: Actin-related protein 2/3 complex subunit 4 (Q641G7)
Organism: Xenopus laevis (African clawed frog)
Function: Actin-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (Probable). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17178911}. Cell projection {ECO:0000269|PubMed:17178911}. Nucleus {ECO:0000269|PubMed:29925947}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 5-A
- Actin-related protein 2/3 complex subunit 3-B
- Actin-related protein 3-A
- Actin-related protein 2/3 complex subunit 2-B
- Actin-related protein 2/3 complex subunit 1A-A
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 5-B
- Actin-related protein 2/3 complex subunit 2-A
- Actin-related protein 2
- Actin-related protein 3-B
Sequence:
MTATLRPYLNAVRATLQAALCLENFSSQVVERHNKPEVEVRSSKELLLQPVVISRNEKEKVLIEGSINSVRVSIAVKQADEIEKILCHKFMRFMMMRAENFFILRRKPVEGYDISFLITNFHTEQMYKHKLVDFVIHFMEEIDKEISEMKLSVNARARIVAEEFLKNF
Protein: Transcription initiation factor IIA subunit 2 (General transcription factor IIA subunit 2) (TFIIA p12 subunit) (TFIIA-12) (TFIIAS) (Transcription initiation factor IIA gamma chain) (TFIIA-gamma) (P52657)
Organism: Homo sapiens (Human)
Function: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity.
Subcellular location: Nucleus.
Interaction partners:
- Transcription initiation factor IIA subunit 1
- TATA-box-binding protein
- Transcription initiation factor IIB
- General transcription factor IIE subunit 1
- Transcription initiation factor IIE subunit beta
- TFIIA-alpha and beta-like factor
- General transcription factor IIF subunit 1
- Transcription initiation factor TFIID subunit 9
- General transcription factor IIH subunit 3
- DNA-directed RNA polymerase II subunit RPB1
Sequence:
MAYQLYRNTTLGNSLQESLDELIQSQQITPQLALQVLLQFDKAINAALAQRVRNRVNFRGSLNTYRFCDNVWTFVLNDVEFREVTELIKVDKVKIVACDGKNTGSNTTE
Protein: Superoxide dismutase 1 copper chaperone (P40202)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Copper chaperone for apo superoxide dismutase 1 (SOD1). Binds copper ions and delivers them specifically to apo-SOD1.
Subcellular location: Cytoplasm. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}. Note=A small percentage (around 1-5 percent) localizes to the mitochondrial intermembrane space.
Interaction partners:
- Superoxide dismutase
- Copper-transporting ATPase
- P-type cation-transporting ATPase
- Mitochondrial intermembrane space import and assembly protein 40
- Copper chaperone ATX1
- Cytochrome c oxidase copper chaperone
- Mitochondrial FAD-linked sulfhydryl oxidase ERV1
- Copper transport protein CTR1
- Multifunctional tryptophan biosynthesis protein
- Copper transport protein CTR2
Sequence:
MTTNDTYEATYAIPMHCENCVNDIKACLKNVPGINSLNFDIEQQIMSVESSVAPSTIINTLRNCGKDAIIRGAGKPNSSAVAILETFQKYTIDQKKDTAVRGLARIVQVGENKTLFDITVNGVPEAGNYHASIHEKGDVSKGVESTGKVWHKFDEPIECFNESDLGKNLYSGKTFLSAPLPTWQLIGRSFVISKSLNHPENEPSSVKDYSFLGVIARSAGVWENNKQVCACTGKTVWEERKDALANNIK
Protein: VPS35 endosomal protein-sorting factor-like (Esophageal cancer-associated protein) (Q7Z3J2)
Organism: Homo sapiens (Human)
Function: Acts as component of the retriever complex. The retriever complex is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrin alpha-5/beta-1 (ITGA5:ITGB1). The recruitment of the retriever complex to the endosomal membrane involves CCC and WASH complexes. In the endosomes, drives the retrieval and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply and cell signaling. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association with the CCC complex and cooperation with the WASH complex on early endosomes. Seems not to be required for CCC complex stability.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Endosome {ECO:0000269|PubMed:25355947, ECO:0000269|PubMed:28892079}. Note=Endosome location is dependent of the association with the CCC and WASH complexes. {ECO:0000269|PubMed:28892079}.
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 26C
- Coiled-coil domain-containing protein 22
- Coiled-coil domain-containing protein 93
- COMM domain-containing protein 1
- COMM domain-containing protein 6
- DENN domain-containing protein 10
- COMM domain-containing protein 2
- COMM domain-containing protein 3
- COMM domain-containing protein 4
Sequence:
MAVFPWHSRNRNYKAEFASCRLEAVPLEFGDYHPLKPITVTESKTKKVNRKGSTSSTSSSSSSSVVDPLSSVLDGTDPLSMFAATADPAALAAAMDSSRRKRDRDDNSVVGSDFEPWTNKRGEILARYTTTEKLSINLFMGSEKGKAGTATLAMSEKVRTRLEELDDFEEGSQKELLNLTQQDYVNRIEELNQSLKDAWASDQKVKALKIVIQCSKLLSDTSVIQFYPSKFVLITDILDTFGKLVYERIFSMCVDSRSVLPDHFSPENANDTAKETCLNWFFKIASIRELIPRFYVEASILKCNKFLSKTGISECLPRLTCMIRGIGDPLVSVYARAYLCRVGMEVAPHLKETLNKNFFDFLLTFKQIHGDTVQNQLVVQGVELPSYLPLYPPAMDWIFQCISYHAPEALLTEMMERCKKLGNNALLLNSVMSAFRAEFIATRSMDFIGMIKECDESGFPKHLLFRSLGLNLALADPPESDRLQILNEAWKVITKLKNPQDYINCAEVWVEYTCKHFTKREVNTVLADVIKHMTPDRAFEDSYPQLQLIIKKVIAHFHDFSVLFSVEKFLPFLDMFQKESVRVEVCKCIMDAFIKHQQEPTKDPVILNALLHVCKTMHDSVNALTLEDEKRMLSYLINGFIKMVSFGRDFEQQLSFYVESRSMFCNLEPVLVQLIHSVNRLAMETRKVMKGNHSRKTAAFVRACVAYCFITIPSLAGIFTRLNLYLHSGQVALANQCLSQADAFFKAAISLVPEVPKMINIDGKMRPSESFLLEFLCNFFSTLLIVPDHPEHGVLFLVRELLNVIQDYTWEDNSDEKIRIYTCVLHLLSAMSQETYLYHIDKVDSNDSLYGGDSKFLAENNKLCETVMAQILEHLKTLAKDEALKRQSSLGLSFFNSILAHGDLRNNKLNQLSVNLWHLAQRHGCADTRTMVKTLEYIKKQSKQPDMTHLTELALRLPLQTRT
Protein: Small nuclear ribonucleoprotein F (snRNP-F) (Sm protein F) (Sm-F) (SmF) (P62306)
Organism: Homo sapiens (Human)
Function: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. Is also a component of the minor U12 spliceosome. As part of the U7 snRNP it is involved in histone 3'-end processing.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18984161}. Nucleus {ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000305}.
Interaction partners:
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor RBM22
- Pre-mRNA-processing factor 6
- Small nuclear ribonucleoprotein-associated proteins B and B'
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D3
- U2 small nuclear ribonucleoprotein B''
- U4/U6.U5 tri-snRNP-associated protein 1
- Protein BUD31 homolog
- U7 snRNA-associated Sm-like protein LSm10
Sequence:
MSLPLNPKPFLNGLTGKPVMVKLKWGMEYKGYLVSVDGYMNMQLANTEEYIDGALSGHLGEVLIRCNNVLYIRGVEEEEEDGEMRE
Protein: Calcineurin binding protein 1 (A0A1W2P819)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XFARGEEKNTPKASEKEKACLVDEDSHSSAGTLPGPGASLPSSSGPDRSQDSTAVALSDSSSTQDFFNEPTSLLEGSRKLFPEKRLSGLSAQAGPSGKDLPGPTEERGKTEESLESTEAFRVVEQSVQKPVADSSASAYIPSKPPASTPPLWDGKKRGDSLGEPVAFPQGLPAGAEEQRQFLTEQCISSFC
Protein: Uncharacterized protein Rv3785 (P9WKX1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible dTDP-glucose 4,6-dehydratase
- WAG22 antigen
Sequence:
MVTVARRPVCPVTLTPGDPALASVRDLVDAWSAHDALAELVTMFGGAFPQTDHLEARLASLDKFSTAWDYRARARAARALHGEPVRCQDSGGGARWLIPRLDLPAKKRDAIVGLAQQLGLTLESTPQGTTFDHVLVIGTGRHSNLIRARWARELAKGRQVGHIVLAAASRRLLPSEDDAVAVCAPGARTEFELLAAAARDAFGLDVHPAVRYVRQRDDNPHRDSMVWRFAADTNDLGVPITLLEAPSPEPDSSRATSADTFTFTAHTLGMQDSTCLLVTGQPFVPYQNFDALRTLALPFGIQVETVGFGIDRYDGLGELDQQHPAKLLQEVRSTIRAARALLERIEAGERMATDPRR
Protein: Protein SLOW WALKER 1 (Protein EMBRYO SAC DEVELOPMENT ARREST 13) (Protein EMBRYO SAC DEVELOPMENT ARREST 19) (O82266)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein required for nuclear division and organization during embryo sac development in female gametophyte, probably by promoting rRNA biogenesis essential for the progression of the mitotic division cycles during gametogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:15980260}. Note=Localized in the nucleolus in interphase cells. {ECO:0000269|PubMed:15980260}.
Interaction partners:
- Putative U3 small nucleolar ribonucleoprotein
- M phase phosphoprotein 10
- Ribosomal protein L7Ae/L30e/S12e/Gadd45 family protein
- At4g28200
- Periodic tryptophan protein 2
- KRR1 small subunit processome component
- Putative WD-repeat membrane protein
- At4g22380
- U3 snoRNP-associated protein-like EMB2271
- Bystin
Sequence:
MEEELRVRLNDHQVSKVFPVKPKSTAKPVSESETPESRYWSSFKNHSTPNLVSSVAALAFSPVHPHSLAVAHSATVSLFSSQSLSSSRRFSFRDVVSSVCFRSDGALFAACDLSGVVQVFDIKERMALRTLRSHSAPARFVKYPVQDKLHLVSGGDDGVVKYWDVAGATVISDLLGHKDYVRCGDCSPVNDSMLVTGSYDHTVKVWDARVHTSNWIAEINHGLPVEDVVYLPSGGLIATAGGNSVKVWDLIGGGKMVCSMESHNKTVTSLRVARMESAESRLVSVALDGYMKVFDYGRAKVTYSMRFPAPLMSLGLSPDGSTRVIGGSNGMVFAGKKKVRDVVGGQKKSLNLWSLISDVDESRRRALRPTYFRYFQRGQSEKPSKDDYLVKEKKGLKLTRHDKLLKKFRHKEALVSVLEEKKPANVVAVMEELVARRKLMKCVSNMEEGELGMLLGFLQRYCTVQRYSGLLMGLTKKVLETRAEDIKGKNEFKGLLRNLKREVNQEIRIQQSLLEIQGVIAPLMRIAGRS
Protein: Mak10 subunit, NatC N(Alpha)-terminal acetyltransferase (Q582D3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- N-acetyltransferase, putative
- Sm protein B
- Small nuclear ribonucleoprotein E
- N-acetyltransferase B complex
Sequence:
MLCALDDTWADCLDEFKLALSSTGNTWKCESLAGVDKEAMLSAPEVMDAKTDPGCGYAQIRSLNDLLAKGDIPSAATLQGQELLDVMDLILAKELQYLQGFSLTSGCLAFPYFFKMDLLKEQNPVLHAYCRGVVRTVEIVLRAVMTTGIRSDEEFVPWIREMESEENVPDEQILCQLEEAACKADSPAVATRLRWRMDFLSALRLFVVVEGKAAVEEACGICSAAQELLNSDDYARTFEPVQDGRFFRETEVAYWASGFTPTKPMPVAPFCEVVQSYTTTLQQLASLKDLFSLPSIQAILEYIESIGAQKPLLPVRAIAVIALFRSNPSESFLYGPSLSHRVLEDLSTSYGAPLYLGIMEGKEELLEGVVKYRLHKGMDHRKVTPQQTEFLRQHTVDAVRSWAREMEKVYLIHMECMLCNRGLAHRRLMNVLPQLGGLQEMSYSTDINIFLSQTPGLAADLQNEAIKRTSILTMYANQHVLHVMELIFSLTVELDLFTQGELVPALWYMNFIQRLQVENLLNLSPPYGALIPETRINRVTKVPLYNLALSTRTSGNVDTLRVAILETGRQITDALFRAACVMEAKGLIDFKTQGKYSLTTVERVFNNRMKCLGHIRSPTFVPYGYCVSAKPNFSSTNDGDPPKISHYAHEAGVQALNAAERLKHLLAMKGLDGARGRALYEHIKAMEKTARAINASLASFVGVCDDEEALKGYAVEVCRPFHSCMICLTLRKRTTA
Protein: Aquaporin TIP1-3 (Gamma-tonoplast intrinsic protein 3) (Gamma-TIP3) (Tonoplast intrinsic protein 1-3) (AtTIP1;3) (O82598)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Potential aquaporin, which may facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Vacuole membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Tonoplast.
Interaction partners:
- Probable aquaporin SIP1-2
- Protein S-acyltransferase 24
- Aquaporin SIP1-1
- Probable aquaporin SIP2-1
- PAMP-induced secreted peptide 1
- Mitochondrial inner membrane protease ATP23
Sequence:
MPINRIAIGTPGEASRPDAIRAAFAEFFSMVIFVFAGQGSGMAYGKLTGDGPATPAGLVAASLSHAFALFVAVSVGANVSGGHVNPAVTFGAFIGGNITLLRAILYWIAQLLGAVVACLLLKVSTGGMETAAFSLSYGVTPWNAVVFEIVMTFGLVYTVYATAVDPKKGDIGIIAPLAIGLIVGANILVGGAFDGASMNPAVSFGPAVVSWIWTNHWVYWVGPFIGAAIAAIVYDTIFIGSNGHEPLPSNDF
Protein: Uncharacterized mitochondrial protein Mp05 (ORF447) (O21050)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Mitochondrion.
Interaction partners:
Sequence:
MLITKNNKKKIKKISKRGTNKAFLQKLLSVEKLTNLLKKKQRKVSLARKAQKKIYHKGKFKITDIISIPLRGEVIKRIIKPKLQGIDLVVDEMDHNPINDIEILFYTREQEEERRQEEPEDYPLDAWDKDVLGIVSEDEPQYKNPTDFIYHWEFGILHPVASFEEFFEIDFNHVALHKVDSYGDFAFYGNDPYVKTFEYPTEQYYISEEDAGQFEIDYLLHYSTKLERHSQYLLKRKENYNPKQPQILETDSRSEHYLMNYFYYNKLENVLEKKEGIDDAEVYKFIKLDFGEKMELKLEKFYDLNRERRFRVKKLSQSKLYEFEKAALKGIGFDCFMLIVGIIIFLASSPYLFSQLPWRVKYSLHNTWYHNLLEVIDVLFSMPKVINLEWLYLQAMWEGELTVLKIRGGISVLTAIETIMSVMSNYKDLSQTSQIINYLANFSFDIY
Protein: SH2B adapter protein 3 (Lymphocyte adapter protein) (Lymphocyte-specific adapter protein Lnk) (Signal transduction protein Lnk) (Q9UQQ2)
Organism: Homo sapiens (Human)
Function: Links T-cell receptor activation signal to phospholipase C-gamma-1, GRB2 and phosphatidylinositol 3-kinase.
Interaction partners:
- Tyrosine-protein kinase JAK2
- Growth factor receptor-bound protein 2
- NT-3 growth factor receptor
- SH2B adapter protein 1
- High affinity nerve growth factor receptor
- BDNF/NT-3 growth factors receptor
- Polycomb group protein ASXL1
- Mast/stem cell growth factor receptor Kit
- Methylcytosine dioxygenase TET2
- T-cell activation Rho GTPase-activating protein
Sequence:
MNGPALQPSSPSSAPSASPAAAPRGWSEFCELHAVAAARELARQYWLFAREHPQHAPLRAELVSLQFTDLFQRYFCREVRDGRAPGRDYRDTGRGPPAKAEASPEPGPGPAAPGLPKARSSEELAPPRPPGPCSFQHFRRSLRHIFRRRSAGELPAAHTAAAPGTPGEAAETPARPGLAKKFLPWSLAREPPPEALKEAVLRYSLADEASMDSGARWQRGRLALRRAPGPDGPDRVLELFDPPKSSRPKLQAACSSIQEVRWCTRLEMPDNLYTFVLKVKDRTDIIFEVGDEQQLNSWMAELSECTGRGLESTEAEMHIPSALEPSTSSSPRGSTDSLNQGASPGGLLDPACQKTDHFLSCYPWFHGPISRVKAAQLVQLQGPDAHGVFLVRQSETRRGEYVLTFNFQGIAKHLRLSLTERGQCRVQHLHFPSVVDMLHHFQRSPIPLECGAACDVRLSSYVVVVSQPPGSCNTVLFPFSLPHWDSESLPHWGSELGLPHLSSSGCPRGLSPEGLPGRSSPPEQIFHLVPSPEELANSLQHLEHEPVNRARDSDYEMDSSSRSHLRAIDNQYTPL
Protein: Fibroblast growth factor (FGF) (Q90696)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
VFMHLFVLCLQAQVTVQSPPNFTQHVREQSLVTDQLSRRLVRTYQLYSRTSGKHVQILDNKKINAMAEDGDVHAKLIVETDTFGSRVRIKGAATGFYICMNKKGKLIGKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRLPKGHQTTEPHRRFEFLNYPFNRRSKRTRNSSARVRP
Protein: Amyloid-beta A4 protein (Q8UUR9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU367156}; Single-pass type I membrane protein {ECO:0000256|RuleBase:RU367156}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MGIDRTVFLLLMLTTLSLAIEVPSDDSVGLLAEPQVAMFCGKLNMHINVQSGKWEPDPTGTKSCISTKEGILKYCQEVYPDLQITNVVEANQPVSIQNWCKMGRRQCRSHTHIVVPYRCLVGEFVSDALLVPDKCKFLHQERMDMCESHLHWHTVAKESCGDRSMNLHDYGMLLPCGIDRFRGVEFVCCPMEEQKDLDSEEQEEANSDVWWGGAETEYTDASVLKEQVTAKPDPAVTEDDEDLNNEEEEVWDNDEDGDGEDDEDEEDDDEDIIDEQDTSEQTSNIAMTTTTTTTTESIEEVVRVPTMAPSPADAVDRYLEAPGDMNEHMRFQKAKESLEAKHREKMSEVMREWEEAERQAKNLPRADKKTIIQRFQEKVESLEKEAAGERQQLVETHMARVEALLNDRRRQALESYLSSLQSDQPRPRQVLNLLKKYIRAEQKDRQHTLKHFEHVREVDPKKASQIRPFVMTHLRVIEERMNQSLGYLYKVPQVANDIQDQVAVLVQRDQAEVTQQLSSLQSKMRVSYGNDALMPDLPDSTTPLDNLPPEQDGLGFIHPESFNQANTDNHVEPVDARPIPERGLPTRPEIPKVRLDIEERHNAGYDVRDKRLMFLAEDMGSNKGAIIGLMVGGVVIATVIVITLVMLRKKQYTSIHHGVIEVDAAVTPEERHLAKMQQNGYENPTYKFFEQMQN
Protein: Extracellular glycoprotein lacritin (Q9GZZ8)
Organism: Homo sapiens (Human)
Function: Modulates secretion by lacrimal acinar cells.
Subcellular location: Secreted.
Interaction partners:
- Chondroitin sulfate proteoglycan 5
- Syndecan-1
- Lipocalin-1
- Nidogen-1
- Fibulin-2
- Lactotransferrin
- Vitronectin
Sequence:
MKFTTLLFLAAVAGALVYAEDASSDSTGADPAQEAGTSKPNEEISGPAEPASPPETTTTAQETSAAAVQGTAKVTSSRQELNPLKSIVEKSILLTEQALAKAGKGMHGGVPGGKQFIENGSEFAQKLLKKFSLLKPWA