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Protein

Nectin-1

Gene

NECTIN1

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

Functioni

Promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between NECTIN1 and NECTIN3 and between NECTIN1 and NECTIN4. Has some neurite outgrowth-promoting activity.1 Publication
(Microbial infection) Acts as a receptor for herpes simplex virus 1/HHV-1, herpes simplex virus 2/HHV-2, and pseudorabies virus/PRV.2 Publications

GO - Molecular functioni

  • carbohydrate binding Source: Ensembl
  • cell adhesion molecule binding Source: BHF-UCL
  • coreceptor activity Source: ProtInc
  • protein homodimerization activity Source: HGNC
  • receptor binding Source: GO_Central
  • virion binding Source: Ensembl
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Receptor

Keywords - Biological processi

Cell adhesion, Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:ENSG00000110400-MONOMER.
ReactomeiR-HSA-418990. Adherens junctions interactions.
R-HSA-420597. Nectin/Necl trans heterodimerization.

Names & Taxonomyi

Protein namesi
Recommended name:
Nectin-1
Alternative name(s):
Herpes virus entry mediator C
Short name:
Herpesvirus entry mediator C
Short name:
HveC
Herpesvirus Ig-like receptor
Short name:
HIgR
Nectin cell adhesion molecule 1Imported
Poliovirus receptor-related protein 1
CD_antigen: CD111
Gene namesi
Name:NECTIN1Imported
Synonyms:HVEC, PRR1, PVRL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:9706. NECTIN1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini31 – 355ExtracellularSequence analysisAdd BLAST325
Transmembranei356 – 376HelicalSequence analysisAdd BLAST21
Topological domaini377 – 517CytoplasmicSequence analysisAdd BLAST141

GO - Cellular componenti

  • adherens junction Source: UniProtKB
  • apical junction complex Source: Ensembl
  • axon Source: Ensembl
  • catenin complex Source: Ensembl
  • cell-cell adherens junction Source: BHF-UCL
  • cell-cell contact zone Source: Ensembl
  • extracellular region Source: UniProtKB-SubCell
  • growth cone membrane Source: Ensembl
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: GO_Central
  • intracellular membrane-bounded organelle Source: Ensembl
  • membrane Source: ProtInc
  • plasma membrane Source: Reactome
  • presynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted, Synapse

Pathology & Biotechi

Involvement in diseasei

Ectodermal dysplasia, Margarita Island type (EDMI)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. It is a syndrome characterized by the association of cleft lip/palate, ectodermal dysplasia (sparse short and dry scalp hair, sparse eyebrows and eyelashes), and partial syndactyly of the fingers and/or toes. Two thirds of the patients do not manifest oral cleft but present with abnormal teeth and nails.
See also OMIM:225060
Non-syndromic orofacial cleft 7 (OFC7)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum.
See also OMIM:225060

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi82N → Y: Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus. 1 Publication1
Mutagenesisi84S → Y: Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus. 1 Publication1
Mutagenesisi129F → A or S: Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus. 1 Publication1

Keywords - Diseasei

Ectodermal dysplasia

Organism-specific databases

DisGeNETi5818.
MalaCardsiPVRL1.
MIMi225060. phenotype.
OpenTargetsiENSG00000110400.
Orphaneti1991. Cleft lip with or without cleft palate.
3253. Zlotogora-Ogur syndrome.
PharmGKBiPA34051.

Polymorphism and mutation databases

BioMutaiPVRL1.
DMDMi18202503.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000001513331 – 517Nectin-1Add BLAST487

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi36N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi51 ↔ 1241 Publication2 Publications
Glycosylationi72N-linked (GlcNAc...)1 Publication1
Glycosylationi139N-linked (GlcNAc...)1 Publication1
Disulfide bondi172 ↔ 2261 Publication2 Publications
Glycosylationi202N-linked (GlcNAc...) (complex)4 Publications1
Disulfide bondi269 ↔ 3161 Publication2 Publications
Glycosylationi286N-linked (GlcNAc...)Sequence analysis1
Glycosylationi297N-linked (GlcNAc...)Sequence analysis1
Glycosylationi307N-linked (GlcNAc...)Sequence analysis1
Glycosylationi332N-linked (GlcNAc...)1 Publication1
Modified residuei422PhosphoserineCombined sources1
Modified residuei434PhosphoserineCombined sources1
Modified residuei435PhosphoserineBy similarity1
Modified residuei436PhosphotyrosineBy similarity1
Modified residuei511PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ15223.
MaxQBiQ15223.
PaxDbiQ15223.
PeptideAtlasiQ15223.
PRIDEiQ15223.

PTM databases

iPTMnetiQ15223.
PhosphoSitePlusiQ15223.

Miscellaneous databases

PMAP-CutDBQ15223.

Expressioni

Gene expression databases

BgeeiENSG00000110400.
CleanExiHS_PVRL1.
GenevisibleiQ15223. HS.

Organism-specific databases

HPAiCAB016135.
HPA026846.

Interactioni

Subunit structurei

Interacts (via Ig-like C2-type domain 2) with FGFR1, FGFR2 and FGFR3 (By similarity). Cis- and trans-homodimer. Can form trans-heterodimers with NECTIN3 and with NECTIN4. Interaction between NECTIN1 and NECTIN3 on the pre- and postsynaptic sites, respectively, initiates the formation of puncta adherentia junctions between axons and dendrites. Interacts (via cytoplasmic domain) with AFDN (via PDZ domain); this interaction recruits NECTIN1 to cadherin-based adherens junctions and provides a connection with the actin cytoskeleton. Interacts with integrin alphaV/beta3.By similarity4 Publications
(Microbial infection) Interacts with herpes simplex virus 1/HHV-1, herpes simplex virus 2/HHV-2, and pseudorabies virus/PRV envelope glycoprotein D (PubMed:21980294, PubMed:22146396, PubMed:9696799, PubMed:9657005).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NECTIN3Q9NQS32EBI-1771314,EBI-2826725
NECTIN4Q96NY82EBI-1771314,EBI-4314784
SDCBPO005608EBI-1771314,EBI-727004

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • protein homodimerization activity Source: HGNC
  • receptor binding Source: GO_Central

Protein-protein interaction databases

BioGridi111776. 5 interactors.
DIPiDIP-40302N.
IntActiQ15223. 7 interactors.
MINTiMINT-90873.
STRINGi9606.ENSP00000264025.

Structurei

Secondary structure

1517
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 42Combined sources6
Beta strandi47 – 49Combined sources3
Beta strandi61 – 71Combined sources11
Beta strandi74 – 82Combined sources9
Turni83 – 85Combined sources3
Beta strandi86 – 89Combined sources4
Turni94 – 96Combined sources3
Beta strandi97 – 101Combined sources5
Beta strandi103 – 106Combined sources4
Beta strandi109 – 111Combined sources3
Helixi116 – 118Combined sources3
Beta strandi120 – 129Combined sources10
Beta strandi132 – 144Combined sources13
Beta strandi147 – 152Combined sources6
Beta strandi157 – 159Combined sources3
Beta strandi167 – 179Combined sources13
Beta strandi182 – 189Combined sources8
Beta strandi192 – 199Combined sources8
Beta strandi205 – 213Combined sources9
Helixi217 – 219Combined sources3
Beta strandi223 – 230Combined sources8
Beta strandi233 – 240Combined sources8
Beta strandi243 – 252Combined sources10
Beta strandi265 – 275Combined sources11
Beta strandi279 – 284Combined sources6
Beta strandi293 – 296Combined sources4
Beta strandi299 – 302Combined sources4
Helixi308 – 310Combined sources3
Beta strandi312 – 320Combined sources9
Beta strandi323 – 331Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ALPX-ray2.80A/B30-335[»]
3SKUX-ray4.00D/E/F31-345[»]
3U82X-ray3.16B30-335[»]
3U83X-ray2.50A30-335[»]
4FMFX-ray3.20A/B/C/D31-337[»]
4MYWX-ray3.19B/D30-335[»]
ProteinModelPortaliQ15223.
SMRiQ15223.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15223.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 141Ig-like V-typeAdd BLAST111
Domaini149 – 238Ig-like C2-type 1Add BLAST90
Domaini247 – 334Ig-like C2-type 2Add BLAST88

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni282 – 299Interaction with FGFRBy similarityAdd BLAST18

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi437 – 444Poly-Glu8
Compositional biasi445 – 449Poly-Gly5

Domaini

Ig-like C2-type 2 mediates neurite outgrowth through binding, induction of phosphorylation, and activation of FGFR.By similarity

Sequence similaritiesi

Belongs to the nectin family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IF17. Eukaryota.
ENOG410YK75. LUCA.
GeneTreeiENSGT00770000120512.
HOGENOMiHOG000115804.
HOVERGENiHBG100542.
InParanoidiQ15223.
KOiK06081.
OMAiHVFGNGY.
OrthoDBiEOG091G0BLQ.
PhylomeDBiQ15223.
TreeFamiTF331051.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR033314. Nectin1.
[Graphical view]
PANTHERiPTHR23277:SF69. PTHR23277:SF69. 1 hit.
PfamiPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 2 hits.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Delta (identifier: Q15223-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARMGLAGAA GRWWGLALGL TAFFLPGVHS QVVQVNDSMY GFIGTDVVLH
60 70 80 90 100
CSFANPLPSV KITQVTWQKS TNGSKQNVAI YNPSMGVSVL APYRERVEFL
110 120 130 140 150
RPSFTDGTIR LSRLELEDEG VYICEFATFP TGNRESQLNL TVMAKPTNWI
160 170 180 190 200
EGTQAVLRAK KGQDDKVLVA TCTSANGKPP SVVSWETRLK GEAEYQEIRN
210 220 230 240 250
PNGTVTVISR YRLVPSREAH QQSLACIVNY HMDRFKESLT LNVQYEPEVT
260 270 280 290 300
IEGFDGNWYL QRMDVKLTCK ADANPPATEY HWTTLNGSLP KGVEAQNRTL
310 320 330 340 350
FFKGPINYSL AGTYICEATN PIGTRSGQVE VNITEFPYTP SPPEHGRRAG
360 370 380 390 400
PVPTAIIGGV AGSILLVLIV VGGIVVALRR RRHTFKGDYS TKKHVYGNGY
410 420 430 440 450
SKAGIPQHHP PMAQNLQYPD DSDDEKKAGP LGGSSYEEEE EEEEGGGGGE
460 470 480 490 500
RKVGGPHPKY DEDAKRPYFT VDEAEARQDG YGDRTLGYQY DPEQLDLAEN
510
MVSQNDGSFI SKKEWYV
Length:517
Mass (Da):57,158
Last modified:September 26, 2001 - v3
Checksum:iDF34C8AEC893EE6D
GO
Isoform Alpha (identifier: Q15223-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     336-458: FPYTPSPPEH...GERKVGGPHP → KPRPQRGLGS...RTTEPRGECP
     459-517: Missing.

Show »
Length:458
Mass (Da):50,721
Checksum:iAB507515F86D7B45
GO
Isoform Gamma (identifier: Q15223-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     335-352: EFPYTPSPPEHGRRAGPV → AFCQLIYPGKGRTRARMF
     353-517: Missing.

Show »
Length:352
Mass (Da):39,150
Checksum:i2FB60588FA752D99
GO

Sequence cautioni

The sequence CAA53980 differs from that shown. Reason: Erroneous initiation.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002624335 – 352EFPYT…RAGPV → AFCQLIYPGKGRTRARMF in isoform Gamma. 1 PublicationAdd BLAST18
Alternative sequenceiVSP_002626336 – 458FPYTP…GGPHP → KPRPQRGLGSAARLLAGTVA VFLILVAVLTVFFLYNRQQK SPPETDGAGTDQPLSQKPEP SPSRQSSLVPEDIQVVHLDP GRQQQQEEEDLQKLSLQPPY YDLGVSPSYHPSVRTTEPRG ECP in isoform Alpha. CuratedAdd BLAST123
Alternative sequenceiVSP_002625353 – 517Missing in isoform Gamma. 1 PublicationAdd BLAST165
Alternative sequenceiVSP_002627459 – 517Missing in isoform Alpha. CuratedAdd BLAST59

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76400 mRNA. Translation: CAA53980.2. Different initiation.
AF060231 mRNA. Translation: AAC23798.1.
AY029539 mRNA. Translation: AAK33124.1.
BC104948 mRNA. Translation: AAI04949.1.
BC113471 mRNA. Translation: AAI13472.1.
AF252867
, AF196768, AF196769, AF196770, AF196771 Genomic DNA. Translation: AAG16648.1.
AF196774
, AF196768, AF196769, AF196770, AF196771, AF196772, AF196773 Genomic DNA. Translation: AAG16649.1.
CCDSiCCDS8425.1. [Q15223-2]
CCDS8426.1. [Q15223-1]
CCDS8427.1. [Q15223-3]
PIRiJC4024.
RefSeqiNP_002846.3. NM_002855.4. [Q15223-1]
NP_976030.1. NM_203285.1. [Q15223-2]
NP_976031.1. NM_203286.1. [Q15223-3]
UniGeneiHs.334846.

Genome annotation databases

EnsembliENST00000264025; ENSP00000264025; ENSG00000110400. [Q15223-1]
ENST00000340882; ENSP00000345289; ENSG00000110400. [Q15223-3]
ENST00000341398; ENSP00000344974; ENSG00000110400. [Q15223-2]
GeneIDi5818.
KEGGihsa:5818.
UCSCiuc001pwu.2. human. [Q15223-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76400 mRNA. Translation: CAA53980.2. Different initiation.
AF060231 mRNA. Translation: AAC23798.1.
AY029539 mRNA. Translation: AAK33124.1.
BC104948 mRNA. Translation: AAI04949.1.
BC113471 mRNA. Translation: AAI13472.1.
AF252867
, AF196768, AF196769, AF196770, AF196771 Genomic DNA. Translation: AAG16648.1.
AF196774
, AF196768, AF196769, AF196770, AF196771, AF196772, AF196773 Genomic DNA. Translation: AAG16649.1.
CCDSiCCDS8425.1. [Q15223-2]
CCDS8426.1. [Q15223-1]
CCDS8427.1. [Q15223-3]
PIRiJC4024.
RefSeqiNP_002846.3. NM_002855.4. [Q15223-1]
NP_976030.1. NM_203285.1. [Q15223-2]
NP_976031.1. NM_203286.1. [Q15223-3]
UniGeneiHs.334846.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ALPX-ray2.80A/B30-335[»]
3SKUX-ray4.00D/E/F31-345[»]
3U82X-ray3.16B30-335[»]
3U83X-ray2.50A30-335[»]
4FMFX-ray3.20A/B/C/D31-337[»]
4MYWX-ray3.19B/D30-335[»]
ProteinModelPortaliQ15223.
SMRiQ15223.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111776. 5 interactors.
DIPiDIP-40302N.
IntActiQ15223. 7 interactors.
MINTiMINT-90873.
STRINGi9606.ENSP00000264025.

PTM databases

iPTMnetiQ15223.
PhosphoSitePlusiQ15223.

Polymorphism and mutation databases

BioMutaiPVRL1.
DMDMi18202503.

Proteomic databases

EPDiQ15223.
MaxQBiQ15223.
PaxDbiQ15223.
PeptideAtlasiQ15223.
PRIDEiQ15223.

Protocols and materials databases

DNASUi5818.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264025; ENSP00000264025; ENSG00000110400. [Q15223-1]
ENST00000340882; ENSP00000345289; ENSG00000110400. [Q15223-3]
ENST00000341398; ENSP00000344974; ENSG00000110400. [Q15223-2]
GeneIDi5818.
KEGGihsa:5818.
UCSCiuc001pwu.2. human. [Q15223-1]

Organism-specific databases

CTDi5818.
DisGeNETi5818.
GeneCardsiPVRL1.
HGNCiHGNC:9706. NECTIN1.
HPAiCAB016135.
HPA026846.
MalaCardsiPVRL1.
MIMi225060. phenotype.
600644. gene.
neXtProtiNX_Q15223.
OpenTargetsiENSG00000110400.
Orphaneti1991. Cleft lip with or without cleft palate.
3253. Zlotogora-Ogur syndrome.
PharmGKBiPA34051.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF17. Eukaryota.
ENOG410YK75. LUCA.
GeneTreeiENSGT00770000120512.
HOGENOMiHOG000115804.
HOVERGENiHBG100542.
InParanoidiQ15223.
KOiK06081.
OMAiHVFGNGY.
OrthoDBiEOG091G0BLQ.
PhylomeDBiQ15223.
TreeFamiTF331051.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000110400-MONOMER.
ReactomeiR-HSA-418990. Adherens junctions interactions.
R-HSA-420597. Nectin/Necl trans heterodimerization.

Miscellaneous databases

ChiTaRSiPVRL1. human.
EvolutionaryTraceiQ15223.
GeneWikiiPVRL1.
GenomeRNAii5818.
PMAP-CutDBQ15223.
PROiQ15223.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000110400.
CleanExiHS_PVRL1.
GenevisibleiQ15223. HS.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR033314. Nectin1.
[Graphical view]
PANTHERiPTHR23277:SF69. PTHR23277:SF69. 1 hit.
PfamiPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 2 hits.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNECT1_HUMAN
AccessioniPrimary (citable) accession number: Q15223
Secondary accession number(s): O75465
, Q2M3D3, Q9HBE6, Q9HBW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: November 30, 2016
This is version 164 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, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.