Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ig heavy chain V-III region KOL

Gene
N/A
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • antigen binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-166663. Initial triggering of complement.
R-HSA-173623. Classical antibody-mediated complement activation.
R-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-2029481. FCGR activation.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-2029485. Role of phospholipids in phagocytosis.
R-HSA-2168880. Scavenging of heme from plasma.
R-HSA-2454202. Fc epsilon receptor (FCERI) signaling.
R-HSA-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-5690714. CD22 mediated BCR regulation.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Names & Taxonomyi

Protein namesi
Recommended name:
Ig heavy chain V-III region KOL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi123851.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›126›126Ig heavy chain V-III region KOLPRO_0000059923Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acid1 Publication
Disulfide bondi22 ↔ 96PROSITE-ProRule annotation1 Publication
Disulfide bondi105 ↔ 110PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PeptideAtlasiP01772.
PRIDEiP01772.

Interactioni

Protein-protein interaction databases

MINTiMINT-1504862.

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Beta strandi18 – 2710Combined sources
Helixi29 – 313Combined sources
Beta strandi34 – 396Combined sources
Beta strandi45 – 517Combined sources
Beta strandi58 – 603Combined sources
Helixi62 – 643Combined sources
Beta strandi68 – 736Combined sources
Turni74 – 774Combined sources
Beta strandi78 – 836Combined sources
Helixi88 – 903Combined sources
Beta strandi92 – 998Combined sources
Beta strandi101 – 1033Combined sources
Beta strandi113 – 1164Combined sources
Beta strandi120 – 1245Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FB4X-ray1.90H2-126[»]
2IG2X-ray3.00H2-126[»]
2RCJX-ray-A/B/E/F/I/J/M/N/Q/R1-126[»]
ProteinModelPortaliP01772.
SMRiP01772. Positions 1-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01772.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 112112Ig-likeAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region

Phylogenomic databases

HOVERGENiHBG018013.
PhylomeDBiP01772.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P01772-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QVQLVESGGG VVQPGRSLRL SCSSSGFIFS SYAMYWVRQA PGKGLEWVAI
60 70 80 90 100
IWDDGSDQHY ADSVKGRFTI SRDNSKNTLF LQMDSLRPED TGVYFCARDG
110 120
GHGFCSSASC FGPDYWGQGT PVTVSS
Length:126
Mass (Da):13,718
Last modified:July 21, 1986 - v1
Checksum:iE4D71B52B16F8776
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei126 – 1261

Sequence databases

PIRiA02055. G1HUKL.

Cross-referencesi

Sequence databases

PIRiA02055. G1HUKL.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FB4X-ray1.90H2-126[»]
2IG2X-ray3.00H2-126[»]
2RCJX-ray-A/B/E/F/I/J/M/N/Q/R1-126[»]
ProteinModelPortaliP01772.
SMRiP01772. Positions 1-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1504862.

Polymorphism and mutation databases

DMDMi123851.

Proteomic databases

PeptideAtlasiP01772.
PRIDEiP01772.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG018013.
PhylomeDBiP01772.

Enzyme and pathway databases

ReactomeiR-HSA-166663. Initial triggering of complement.
R-HSA-173623. Classical antibody-mediated complement activation.
R-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-2029481. FCGR activation.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-2029485. Role of phospholipids in phagocytosis.
R-HSA-2168880. Scavenging of heme from plasma.
R-HSA-2454202. Fc epsilon receptor (FCERI) signaling.
R-HSA-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-5690714. CD22 mediated BCR regulation.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

EvolutionaryTraceiP01772.
NextBioi35537702.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Three-dimensional structure determination of antibodies. Primary structure of crystallized monoclonal immunoglobulin IgG1 KOL, I."
    Schmidt W.E., Jung H.-D., Palm W., Hilschmann N.
    Hoppe-Seyler's Z. Physiol. Chem. 364:713-747(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, DISULFIDE BONDS.
  2. "Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 A and 1.0-A resolution."
    Marquart M., Deisenhofer J., Huber R., Palm W.
    J. Mol. Biol. 141:369-391(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiHV311_HUMAN
AccessioniPrimary (citable) accession number: P01772
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 11, 2016
This is version 100 of the entry and version 1 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.