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Protein

RalA-binding protein 1

Gene

RALBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin.3 Publications

GO - Molecular functioni

  1. ATPase activity Source: UniProtKB
  2. ATPase activity, coupled to movement of substances Source: UniProtKB
  3. GTPase activator activity Source: UniProtKB
  4. Rac GTPase binding Source: UniProtKB
  5. Ral GTPase binding Source: UniProtKB

GO - Biological processi

  1. chemotaxis Source: ProtInc
  2. metabolic process Source: GOC
  3. positive regulation of GTPase activity Source: UniProtKB
  4. regulation of GTPase activity Source: UniProtKB
  5. regulation of small GTPase mediated signal transduction Source: Reactome
  6. signal transduction Source: ProtInc
  7. small GTPase mediated signal transduction Source: UniProtKB
  8. transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
SignaLinkiQ15311.

Protein family/group databases

TCDBi9.A.1.1.1. the non abc multidrug exporter (n-mde) family.

Names & Taxonomyi

Protein namesi
Recommended name:
RalA-binding protein 1
Short name:
RalBP1
Alternative name(s):
76 kDa Ral-interacting protein
Dinitrophenyl S-glutathione ATPase
Short name:
DNP-SG ATPase
Ral-interacting protein 1
Gene namesi
Name:RALBP1
Synonyms:RLIP1, RLIP76
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:9841. RALBP1.

Subcellular locationi

  1. Membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34199.

Chemistry

DrugBankiDB00564. Carbamazepine.
DB00997. Doxorubicin.
DB00398. Sorafenib.
DB00541. Vincristine.

Polymorphism and mutation databases

BioMutaiRALBP1.
DMDMi34098413.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 655654RalA-binding protein 1PRO_0000056733Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Modified residuei29 – 291PhosphoserineBy similarity
Modified residuei44 – 441Phosphothreonine1 Publication
Modified residuei48 – 481Phosphoserine1 Publication
Modified residuei62 – 621Phosphoserine2 Publications
Modified residuei92 – 921Phosphoserine3 Publications
Modified residuei93 – 931Phosphoserine3 Publications
Modified residuei463 – 4631Phosphoserine2 Publications
Modified residuei645 – 6451Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15311.
PaxDbiQ15311.
PeptideAtlasiQ15311.
PRIDEiQ15311.

PTM databases

PhosphoSiteiQ15311.

Expressioni

Tissue specificityi

Expressed ubiquitously but at low levels. Shows a strong expression in the erythrocytes.1 Publication

Gene expression databases

BgeeiQ15311.
CleanExiHS_RALBP1.
ExpressionAtlasiQ15311. baseline and differential.
GenevestigatoriQ15311.

Organism-specific databases

HPAiCAB046010.
HPA046651.
HPA054654.
HPA055606.

Interactioni

Subunit structurei

Interacts with the GTP-bound form of RALA, RALB, CDC42 and RAC1. Interacts with REPS1 and REPS2 and this does not affect the Ral-binding activity. Interacts with DAB2IP. Interacts with catalytically active CCNB1 and CDK1 during mitosis. Interacts with EPN1, NUMB and TFAP2A during interphase and mitosis.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9H6F03EBI-749285,EBI-10307481
AMOTL2Q9Y2J4-43EBI-749285,EBI-10187270
C1orf216Q8TAB53EBI-749285,EBI-747505
CCL20P785562EBI-749285,EBI-3913209
CEP57Q86XR84EBI-749285,EBI-308614
GPS2Q132275EBI-749285,EBI-713355
PPLO604373EBI-749285,EBI-368321
SMARCE1Q969G33EBI-749285,EBI-455078
TAX1BP1Q86VP13EBI-749285,EBI-529518
TBRG1Q05BL03EBI-749285,EBI-10223693
TFPTG5E9B55EBI-749285,EBI-10178002
TNIP1Q150253EBI-749285,EBI-357849
ZNF707Q96C283EBI-749285,EBI-748111

Protein-protein interaction databases

BioGridi116131. 40 interactions.
IntActiQ15311. 24 interactions.
MINTiMINT-140436.
STRINGi9606.ENSP00000019317.

Structurei

Secondary structure

1
655
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi184 – 1874Combined sources
Helixi194 – 2007Combined sources
Helixi211 – 22212Combined sources
Turni223 – 2253Combined sources
Turni228 – 2325Combined sources
Helixi237 – 24812Combined sources
Helixi255 – 2573Combined sources
Helixi260 – 27314Combined sources
Helixi280 – 29112Combined sources
Helixi296 – 30914Combined sources
Helixi312 – 33423Combined sources
Helixi339 – 35012Combined sources
Helixi354 – 36714Combined sources
Beta strandi384 – 3863Combined sources
Helixi395 – 41420Combined sources
Turni417 – 4193Combined sources
Helixi424 – 44421Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KWHNMR-A393-446[»]
2KWINMR-B393-446[»]
2MBGNMR-A184-446[»]
ProteinModelPortaliQ15311.
SMRiQ15311. Positions 183-446.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15311.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini192 – 380189Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni403 – 49997Interacts with RalAAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi164 – 1718Poly-Lys

Sequence similaritiesi

Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG295787.
GeneTreeiENSGT00720000108475.
HOGENOMiHOG000007929.
HOVERGENiHBG044496.
InParanoidiQ15311.
KOiK08773.
OMAiTMMYDGV.
OrthoDBiEOG7V49ZT.
PhylomeDBiQ15311.
TreeFamiTF315411.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q15311-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTECFLPPTS SPSEHRRVEH GSGLTRTPSS EEISPTKFPG LYRTGEPSPP
60 70 80 90 100
HDILHEPPDV VSDDEKDHGK KKGKFKKKEK RTEGYAAFQE DSSGDEAESP
110 120 130 140 150
SKMKRSKGIH VFKKPSFSKK KEKDFKIKEK PKEEKHKEEK HKEEKHKEKK
160 170 180 190 200
SKDLTAADVV KQWKEKKKKK KPIQEPEVPQ IDVPNLKPIF GIPLADAVER
210 220 230 240 250
TMMYDGIRLP AVFRECIDYV EKYGMKCEGI YRVSGIKSKV DELKAAYDRE
260 270 280 290 300
ESTNLEDYEP NTVASLLKQY LRDLPENLLT KELMPRFEEA CGRTTETEKV
310 320 330 340 350
QEFQRLLKEL PECNYLLISW LIVHMDHVIA KELETKMNIQ NISIVLSPTV
360 370 380 390 400
QISNRVLYVF FTHVQELFGN VVLKQVMKPL RWSNMATMPT LPETQAGIKE
410 420 430 440 450
EIRRQEFLLN CLHRDLQGGI KDLSKEERLW EVQRILTALK RKLREAKRQE
460 470 480 490 500
CETKIAQEIA SLSKEDVSKE EMNENEEVIN ILLAQENEIL TEQEELLAME
510 520 530 540 550
QFLRRQIASE KEEIERLRAE IAEIQSRQQH GRSETEEYSS ESESESEDEE
560 570 580 590 600
ELQIILEDLQ RQNEELEIKN NHLNQAIHEE REAIIELRVQ LRLLQMQRAK
610 620 630 640 650
AEQQAQEDEE PEWRGGAVQP PRDGVLEPKA AKEQPKAGKE PAKPSPSRDR

KETSI
Length:655
Mass (Da):76,063
Last modified:January 23, 2007 - v3
Checksum:iEC6F75329FD8D062
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti617 – 6171A → V.
Corresponds to variant rs35867116 [ dbSNP | Ensembl ].
VAR_049147

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42542 mRNA. Translation: AAB00103.1.
CH471113 Genomic DNA. Translation: EAX01601.1.
CH471113 Genomic DNA. Translation: EAX01602.1.
CH471113 Genomic DNA. Translation: EAX01604.1.
CH471113 Genomic DNA. Translation: EAX01605.1.
BC013126 mRNA. Translation: AAH13126.1.
CCDSiCCDS11845.1.
PIRiF59435.
RefSeqiNP_006779.1. NM_006788.3.
UniGeneiHs.528993.

Genome annotation databases

EnsembliENST00000019317; ENSP00000019317; ENSG00000017797.
ENST00000383432; ENSP00000372924; ENSG00000017797.
GeneIDi10928.
KEGGihsa:10928.
UCSCiuc002kob.3. human.

Polymorphism and mutation databases

BioMutaiRALBP1.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42542 mRNA. Translation: AAB00103.1.
CH471113 Genomic DNA. Translation: EAX01601.1.
CH471113 Genomic DNA. Translation: EAX01602.1.
CH471113 Genomic DNA. Translation: EAX01604.1.
CH471113 Genomic DNA. Translation: EAX01605.1.
BC013126 mRNA. Translation: AAH13126.1.
CCDSiCCDS11845.1.
PIRiF59435.
RefSeqiNP_006779.1. NM_006788.3.
UniGeneiHs.528993.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KWHNMR-A393-446[»]
2KWINMR-B393-446[»]
2MBGNMR-A184-446[»]
ProteinModelPortaliQ15311.
SMRiQ15311. Positions 183-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116131. 40 interactions.
IntActiQ15311. 24 interactions.
MINTiMINT-140436.
STRINGi9606.ENSP00000019317.

Chemistry

DrugBankiDB00564. Carbamazepine.
DB00997. Doxorubicin.
DB00398. Sorafenib.
DB00541. Vincristine.

Protein family/group databases

TCDBi9.A.1.1.1. the non abc multidrug exporter (n-mde) family.

PTM databases

PhosphoSiteiQ15311.

Polymorphism and mutation databases

BioMutaiRALBP1.
DMDMi34098413.

Proteomic databases

MaxQBiQ15311.
PaxDbiQ15311.
PeptideAtlasiQ15311.
PRIDEiQ15311.

Protocols and materials databases

DNASUi10928.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000019317; ENSP00000019317; ENSG00000017797.
ENST00000383432; ENSP00000372924; ENSG00000017797.
GeneIDi10928.
KEGGihsa:10928.
UCSCiuc002kob.3. human.

Organism-specific databases

CTDi10928.
GeneCardsiGC18P009465.
HGNCiHGNC:9841. RALBP1.
HPAiCAB046010.
HPA046651.
HPA054654.
HPA055606.
MIMi605801. gene.
neXtProtiNX_Q15311.
PharmGKBiPA34199.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG295787.
GeneTreeiENSGT00720000108475.
HOGENOMiHOG000007929.
HOVERGENiHBG044496.
InParanoidiQ15311.
KOiK08773.
OMAiTMMYDGV.
OrthoDBiEOG7V49ZT.
PhylomeDBiQ15311.
TreeFamiTF315411.

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
SignaLinkiQ15311.

Miscellaneous databases

ChiTaRSiRALBP1. human.
EvolutionaryTraceiQ15311.
GeneWikiiRALBP1.
GenomeRNAii10928.
NextBioi41515.
PROiQ15311.
SOURCEiSearch...

Gene expression databases

BgeeiQ15311.
CleanExiHS_RALBP1.
ExpressionAtlasiQ15311. baseline and differential.
GenevestigatoriQ15311.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity."
    Jullien-Flores V., Dorseuil O., Romero F., Letourneur F., Saragosti S., Berger R., Tavitian A., Gacon G., Camonis J.H.
    J. Biol. Chem. 270:22473-22477(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RALA.
  2. "Novel function of human RLIP76: ATP-dependent transport of glutathione conjugates and doxorubicin."
    Awasthi S., Cheng J., Singhal S.S., Saini M.K., Pandya U., Pikula S., Bandorowicz-Pikula J., Singh S.V., Zimniak P., Awasthi Y.C.
    Biochemistry 39:9327-9334(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, PROTEIN SEQUENCE OF 2-15; 409-438 AND 472-486.
    Tissue: Bone marrow.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  5. "Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral."
    Ikeda M., Ishida O., Hinoi T., Kishida S., Kikuchi A.
    J. Biol. Chem. 273:814-821(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH REPS2.
    Tissue: Brain.
  6. "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis."
    Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.
    J. Biol. Chem. 278:30597-30604(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CCNB1; CDK1; EPN1; NUMB AND TFAP2A.
  7. "RLIP76 is the major ATP-dependent transporter of glutathione-conjugates and doxorubicin in human erythrocytes."
    Sharma R., Singhal S.S., Cheng J., Yang Y., Sharma A., Zimniak P., Awasthi S., Awasthi Y.C.
    Arch. Biochem. Biophys. 391:171-179(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation."
    Zhang H., Zhang R., Luo Y., D'Alessio A., Pober J.S., Min W.
    J. Biol. Chem. 279:44955-44965(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2IP.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44; SER-48; SER-62; SER-92; SER-93; SER-463 AND SER-645, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "The RalB-RLIP76 complex reveals a novel mode of ral-effector interaction."
    Fenwick R.B., Campbell L.J., Rajasekar K., Prasannan S., Nietlispach D., Camonis J., Owen D., Mott H.R.
    Structure 18:985-995(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 393-446 IN COMPLEX WITH RALB, INTERACTION WITH RALB.

Entry informationi

Entry nameiRBP1_HUMAN
AccessioniPrimary (citable) accession number: Q15311
Secondary accession number(s): D3DUI0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.