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P0CG05

- LAC2_HUMAN

UniProt

P0CG05 - LAC2_HUMAN

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Protein

Ig lambda-2 chain C regions

Gene
IGLC2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. antigen binding Source: UniProtKB-KW

GO - Biological processi

  1. complement activation Source: Reactome
  2. complement activation, classical pathway Source: Reactome
  3. Fc-epsilon receptor signaling pathway Source: Reactome
  4. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  5. innate immune response Source: Reactome
  6. regulation of immune response Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Bence-Jones protein

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_160163. Scavenging of heme from plasma.
REACT_160274. FCGR activation.
REACT_163701. FCERI mediated MAPK activation.
REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_163936. Fc epsilon receptor (FCERI) signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_7956. Classical antibody-mediated complement activation.
REACT_8024. Initial triggering of complement.

Names & Taxonomyi

Protein namesi
Recommended name:
Ig lambda-2 chain C regions
Gene namesi
Name:IGLC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:5856. IGLC2.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: Reactome
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProt
  5. plasma membrane Source: Reactome
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 106›106Ig lambda-2 chain C regionsPRO_0000394665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 871 Publication
Disulfide bondi105 – 105Interchain (with heavy chain)1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP0CG05.

Interactioni

Protein-protein interaction databases

IntActiP0CG05. 1 interaction.

Structurei

Secondary structure

1
106
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125
Helixi16 – 205
Beta strandi24 – 3613
Beta strandi39 – 446
Beta strandi47 – 493
Beta strandi53 – 553
Beta strandi62 – 643
Beta strandi66 – 749
Helixi76 – 816
Beta strandi85 – 917
Beta strandi94 – 1007
Helixi102 – 1043

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JVKX-ray1.94B1-105[»]
1LILX-ray2.65A/B1-106[»]
1ZVOX-ray-A/B2-106[»]
2JB5X-ray2.80L1-104[»]
2JB6X-ray2.85A/L1-104[»]
3C2AX-ray2.10L/M2-105[»]
3TV3X-ray1.29L1-106[»]
3TWCX-ray1.65L1-106[»]
3TYGX-ray3.25L1-106[»]
4EOWX-ray1.97L1-106[»]
4LLDX-ray1.19B1-105[»]
4LLMX-ray1.75B1-105[»]
4LLQX-ray1.42B1-105[»]
4LLUX-ray2.16B/D1-105[»]
4LLWX-ray1.95B/D1-105[»]
4LLYX-ray1.60B/D1-105[»]
4O58X-ray2.75L1-106[»]
4O5IX-ray6.50N/P/R/T/V/X1-106[»]
ProteinModelPortaliP0CG05.
SMRiP0CG05. Positions 2-102.

Miscellaneous databases

EvolutionaryTraceiP0CG05.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 10195Ig-likeAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin C region, Immunoglobulin domain

Phylogenomic databases

PhylomeDBiP0CG05.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]
PfamiPF07654. C1-set. 1 hit.
[Graphical view]
SMARTiSM00407. IGc1. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0CG05-1 [UniParc]FASTAAdd to Basket

« Hide

GQPKAAPSVT LFPPSSEELQ ANKATLVCLI SDFYPGAVTV AWKADSSPVK    50
AGVETTTPSK QSNNKYAASS YLSLTPEQWK SHRSYSCQVT HEGSTVEKTV 100
APTECS 106
Length:106
Mass (Da):11,294
Last modified:June 15, 2010 - v1
Checksum:iE5DB72BBE65F4577
GO

Sequence cautioni

The sequence AAA59107.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA20015.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA20026.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA20028.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAA36049.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAB38569.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence EAW59547.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence EAW59549.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J00253 Genomic DNA. Translation: AAA59107.1. Different initiation.
X51754 Genomic DNA. Translation: CAB38569.1. Different initiation.
X51755 Genomic DNA. Translation: CAA36049.1. Different initiation.
D87017 Genomic DNA. Translation: BAA20015.1. Different initiation.
D87023 Genomic DNA. Translation: BAA20026.1. Different initiation.
D87023 Genomic DNA. Translation: BAA20028.1. Different initiation.
CH471095 Genomic DNA. Translation: EAW59547.1. Different initiation.
CH471095 Genomic DNA. Translation: EAW59549.1. Different initiation.
PIRiA92057. L2HU.

Polymorphism databases

DMDMi298351714.

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J00253 Genomic DNA. Translation: AAA59107.1 . Different initiation.
X51754 Genomic DNA. Translation: CAB38569.1 . Different initiation.
X51755 Genomic DNA. Translation: CAA36049.1 . Different initiation.
D87017 Genomic DNA. Translation: BAA20015.1 . Different initiation.
D87023 Genomic DNA. Translation: BAA20026.1 . Different initiation.
D87023 Genomic DNA. Translation: BAA20028.1 . Different initiation.
CH471095 Genomic DNA. Translation: EAW59547.1 . Different initiation.
CH471095 Genomic DNA. Translation: EAW59549.1 . Different initiation.
PIRi A92057. L2HU.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JVK X-ray 1.94 B 1-105 [» ]
1LIL X-ray 2.65 A/B 1-106 [» ]
1ZVO X-ray - A/B 2-106 [» ]
2JB5 X-ray 2.80 L 1-104 [» ]
2JB6 X-ray 2.85 A/L 1-104 [» ]
3C2A X-ray 2.10 L/M 2-105 [» ]
3TV3 X-ray 1.29 L 1-106 [» ]
3TWC X-ray 1.65 L 1-106 [» ]
3TYG X-ray 3.25 L 1-106 [» ]
4EOW X-ray 1.97 L 1-106 [» ]
4LLD X-ray 1.19 B 1-105 [» ]
4LLM X-ray 1.75 B 1-105 [» ]
4LLQ X-ray 1.42 B 1-105 [» ]
4LLU X-ray 2.16 B/D 1-105 [» ]
4LLW X-ray 1.95 B/D 1-105 [» ]
4LLY X-ray 1.60 B/D 1-105 [» ]
4O58 X-ray 2.75 L 1-106 [» ]
4O5I X-ray 6.50 N/P/R/T/V/X 1-106 [» ]
ProteinModelPortali P0CG05.
SMRi P0CG05. Positions 2-102.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0CG05. 1 interaction.

Protein family/group databases

IMGTi Search...
Search...
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Search...
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Search...
Search...

Polymorphism databases

DMDMi 298351714.

Proteomic databases

PRIDEi P0CG05.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

GeneCardsi GC22P023243.
H-InvDB HIX0016285.
HIX0197173.
HGNCi HGNC:5856. IGLC2.
neXtProti NX_P0CG05.
GenAtlasi Search...

Phylogenomic databases

PhylomeDBi P0CG05.

Enzyme and pathway databases

Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_160163. Scavenging of heme from plasma.
REACT_160274. FCGR activation.
REACT_163701. FCERI mediated MAPK activation.
REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_163936. Fc epsilon receptor (FCERI) signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_7956. Classical antibody-mediated complement activation.
REACT_8024. Initial triggering of complement.

Miscellaneous databases

EvolutionaryTracei P0CG05.
PROi P0CG05.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view ]
Pfami PF07654. C1-set. 1 hit.
[Graphical view ]
SMARTi SM00407. IGc1. 1 hit.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Immunoglobulin lambda-chains. The complete amino acid sequence of a Bence-Jones protein."
    Milstein C., Clegg J.B., Jarvis J.M.
    Biochem. J. 110:631-652(1968) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN X), DISULFIDE BONDS.
  2. "The amino acid sequence of a lambda type Bence-Jones protein. 3. The complete amino acid sequence and the location of the disulfide bridges."
    Titani K., Wikler M., Shinoda T., Putnam F.W.
    J. Biol. Chem. 245:2171-2176(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN SH).
  3. "Structural rule of antibodies. Primary structure of a monoclonal immunoglobulin-L-chain of the lambda type, subgroup IV (Bence-Jones-protein Kern). V. The complete amino acid sequence and its genetic interpretation."
    Ponstingl H., Hess M., Hilschmann N.
    Hoppe-Seyler's Z. Physiol. Chem. 352:247-266(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN KERN).
  4. "Clustered arrangement of immunoglobulin lambda constant region genes in man."
    Hieter P.A., Hollis G.F., Korsmeyer S.J., Waldmann T.A., Leder P.
    Nature 294:536-540(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Comparative studies on the structure of the light chains of human immunoglobulins. IV. Assignment of a subsubgroup."
    Kametani F., Takayasu T., Suzuki S., Shinoda T., Okuyama T., Shimizu A.
    J. Biochem. 93:421-429(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN NIG-64).
  6. "Structure and expression of the human immunoglobulin lambda genes."
    Vasicek T.J., Leder P.
    J. Exp. Med. 172:609-620(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "One-megabase sequence analysis of the human immunoglobulin lambda gene locus."
    Kawasaki K., Minoshima S., Nakato E., Shibuya K., Shintani A., Schmeits J.L., Wang J., Shimizu N.
    Genome Res. 7:250-261(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "Immunoglobulin lambda (IGL) genes of human and mouse."
    Lefranc M.-P., Lefranc G.
    (In) Honjo T., Alt F.W., Neuberger M. (eds.); Molecular Biology of B Cells, pp.37-59, Elsevier Academic Press, London (2004)
    Cited for: SEROLOGICAL ISOTYPE.

Entry informationi

Entry nameiLAC2_HUMAN
AccessioniPrimary (citable) accession number: P0CG05
Secondary accession number(s): A0M8Q4, P80423
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: September 3, 2014
This is version 38 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

Miscellaneous

Displays the following serological isotype: Mcg-, Kern- and Oz-. The Mcg- isotype marker is characterized by Ala-6, Ser-8 and Thr-57; the Ke- marker by Ser-46 and the Oz- marker by Arg-83.

Keywords - Technical termi

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

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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