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Protein

Semaphorin-6A

Gene

Sema6a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell surface receptor for PLXNA2 that plays an important role in cell-cell signaling. Required for normal granule cell migration in the developing cerebellum. Promotes reorganization of the actin cytoskeleton and plays an important role in axon guidance in the developing central nervous system. Can act as repulsive axon guidance cue. Has repulsive action towards migrating granular neurons. May play a role in channeling sympathetic axons into the sympathetic chains and controlling the temporal sequence of sympathetic target innervation.4 Publications

GO - Molecular functioni

  • semaphorin receptor binding Source: MGI
  • transmembrane signaling receptor activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • axon guidance Source: UniProtKB
  • cell surface receptor signaling pathway Source: MGI
  • centrosome localization Source: MGI
  • neuron migration Source: UniProtKB
  • positive regulation of neuron migration Source: UniProtKB
  • semaphorin-plexin signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Semaphorin-6A
Alternative name(s):
Semaphorin Q
Short name:
Sema Q
Semaphorin VIA
Short name:
Sema VIA
Semaphorin-6A-1
Short name:
SEMA6A-1
Gene namesi
Name:Sema6a
Synonyms:Semaq
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1203727. Sema6a.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 649631ExtracellularSequence analysisAdd
BLAST
Transmembranei650 – 67021HelicalSequence analysisAdd
BLAST
Topological domaini671 – 1031361CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • axon Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Mice are viable and fertile, and do not show any major behavioral defects. In developing cerebellum, migration of granule cells is impaired. Granule cells can form normal cell processes, but the movement of the nucleus sems to be impaired.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi191 – 1911L → R: Strongly reduced affinity for PLXNA2. 1 Publication
Mutagenesisi212 – 2121H → N: Strongly reduced affinity for PLXNA2. 1 Publication
Mutagenesisi322 – 3221I → E: Abolishes homodimerization. 1 Publication
Mutagenesisi393 – 3931K → E: Strongly reduced affinity for PLXNA2. 1 Publication
Mutagenesisi415 – 4151M → C: Formation of disulfide-linked homodimer. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 10311013Semaphorin-6APRO_0000032340Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331N-linked (GlcNAc...)Sequence analysis
Glycosylationi49 – 491N-linked (GlcNAc...)Sequence analysis
Glycosylationi65 – 651N-linked (GlcNAc...)1 Publication
Disulfide bondi107 ↔ 117
Disulfide bondi135 ↔ 144
Disulfide bondi258 ↔ 369
Glycosylationi282 – 2821N-linked (GlcNAc...)2 Publications
Disulfide bondi283 ↔ 328
Glycosylationi434 – 4341N-linked (GlcNAc...)2 Publications
Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence analysis
Disulfide bondi477 ↔ 506
Disulfide bondi515 ↔ 533
Disulfide bondi521 ↔ 568
Disulfide bondi525 ↔ 542
Modified residuei698 – 6981PhosphoserineBy similarity
Modified residuei953 – 9531PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO35464.
PaxDbiO35464.
PRIDEiO35464.

PTM databases

PhosphoSiteiO35464.

Expressioni

Tissue specificityi

Particularly high levels in spinal cord, cerebellum, metencephalon, superior and inferior colliculus, diencephalon, olfactory bulb and eye.1 Publication

Developmental stagei

Temporally and spatially regulated during development.

Gene expression databases

BgeeiO35464.
ExpressionAtlasiO35464. baseline and differential.
GenevisibleiO35464. MM.

Interactioni

Subunit structurei

Active as a homodimer or oligomer. The SEMA6A homodimer interacts with a PLXNA2 homodimer, giving rise to a heterotetramer. Interacts with EVL.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Plxna4Q80UG23EBI-8057848,EBI-8057809

GO - Molecular functioni

  • semaphorin receptor binding Source: MGI

Protein-protein interaction databases

DIPiDIP-59220N.
IntActiO35464. 1 interaction.
MINTiMINT-7996710.
STRINGi10090.ENSMUSP00000019791.

Structurei

Secondary structure

1
1031
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 304Combined sources
Helixi32 – 354Combined sources
Beta strandi60 – 645Combined sources
Beta strandi67 – 715Combined sources
Beta strandi73 – 808Combined sources
Helixi81 – 833Combined sources
Beta strandi86 – 894Combined sources
Beta strandi93 – 964Combined sources
Helixi101 – 1099Combined sources
Turni114 – 1163Combined sources
Beta strandi120 – 1289Combined sources
Beta strandi131 – 1366Combined sources
Turni138 – 1403Combined sources
Beta strandi143 – 1486Combined sources
Turni149 – 1513Combined sources
Beta strandi154 – 1607Combined sources
Turni162 – 1643Combined sources
Beta strandi174 – 1785Combined sources
Beta strandi181 – 1899Combined sources
Beta strandi195 – 2006Combined sources
Turni214 – 2163Combined sources
Beta strandi221 – 2288Combined sources
Beta strandi231 – 2399Combined sources
Helixi241 – 2433Combined sources
Beta strandi244 – 2474Combined sources
Beta strandi250 – 2589Combined sources
Beta strandi266 – 2694Combined sources
Beta strandi277 – 2815Combined sources
Beta strandi287 – 2893Combined sources
Beta strandi295 – 2995Combined sources
Beta strandi303 – 3053Combined sources
Beta strandi308 – 3169Combined sources
Beta strandi319 – 3224Combined sources
Beta strandi325 – 3317Combined sources
Helixi332 – 3387Combined sources
Beta strandi343 – 3486Combined sources
Beta strandi353 – 3553Combined sources
Helixi358 – 3603Combined sources
Turni374 – 3774Combined sources
Helixi381 – 3833Combined sources
Helixi386 – 3949Combined sources
Beta strandi397 – 4004Combined sources
Helixi405 – 4073Combined sources
Beta strandi410 – 4134Combined sources
Beta strandi415 – 4184Combined sources
Beta strandi420 – 42910Combined sources
Turni430 – 4334Combined sources
Beta strandi435 – 4428Combined sources
Beta strandi445 – 4528Combined sources
Helixi455 – 4573Combined sources
Beta strandi464 – 4707Combined sources
Helixi474 – 4774Combined sources
Beta strandi489 – 4935Combined sources
Helixi494 – 4963Combined sources
Beta strandi498 – 5025Combined sources
Beta strandi507 – 5126Combined sources
Helixi516 – 5183Combined sources
Helixi522 – 5276Combined sources
Beta strandi533 – 5364Combined sources
Turni537 – 5404Combined sources
Beta strandi541 – 5444Combined sources
Beta strandi557 – 5593Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AFCX-ray2.50A/B19-570[»]
3AL8X-ray3.60A19-570[»]
3OKWX-ray2.30A/B19-571[»]
3OKYX-ray2.20B19-571[»]
ProteinModelPortaliO35464.
SMRiO35464. Positions 19-568.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35464.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 512489SemaPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi792 – 81928Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the semaphorin family.Curated
Contains 1 Sema domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3611. Eukaryota.
ENOG410XQZC. LUCA.
GeneTreeiENSGT00760000119134.
HOGENOMiHOG000232047.
HOVERGENiHBG072910.
InParanoidiO35464.
KOiK06842.
OrthoDBiEOG7SV0TJ.
PhylomeDBiO35464.
TreeFamiTF316102.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR016201. Plexin-like_fold.
IPR002165. Plexin_repeat.
IPR001627. Semap_dom.
IPR027231. Semaphorin.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERiPTHR11036. PTHR11036. 2 hits.
PfamiPF01437. PSI. 1 hit.
PF01403. Sema. 1 hit.
[Graphical view]
SMARTiSM00630. Sema. 1 hit.
[Graphical view]
SUPFAMiSSF101912. SSF101912. 1 hit.
SSF103575. SSF103575. 1 hit.
PROSITEiPS51004. SEMA. 1 hit.
[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 1 (identifier: O35464-1) [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
MRPAALLLCL TLLHCAGAGF PEDSEPISIS HGNYTKQYPV FVGHKPGRNT
60 70 80 90 100
TQRHRLDIQM IMIMNRTLYV AARDHIYTVD IDTSHTEEIY CSKKLTWKSR
110 120 130 140 150
QADVDTCRMK GKHKDECHNF IKVLLKKNDD TLFVCGTNAF NPSCRNYRVD
160 170 180 190 200
TLETFGDEFS GMARCPYDAK HANIALFADG KLYSATVTDF LAIDAVIYRS
210 220 230 240 250
LGDSPTLRTV KHDSKWLKEP YFVQAVDYGD YIYFFFREIA VEYNTMGKVV
260 270 280 290 300
FPRVAQVCKN DMGGSQRVLE KQWTSFLKAR LNCSVPGDSH FYFNILQAVT
310 320 330 340 350
DVIRINGRDV VLATFSTPYN SIPGSAVCAY DMLDIANVFT GRFKEQKSPD
360 370 380 390 400
STWTPVPDER VPKPRPGCCA GSSSLEKYAT SNEFPDDTLN FIKTHPLMDE
410 420 430 440 450
AVPSIINRPW FLRTMVRYRL TKIAVDNAAG PYQNHTVVFL GSEKGIILKF
460 470 480 490 500
LARIGSSGFL NGSLFLEEMN VYNPEKCSYD GVEDKRIMGM QLDRASGSLY
510 520 530 540 550
VAFSTCVIKV PLGRCERHGK CKKTCIASRD PYCGWVRESG SCAHLSPLSR
560 570 580 590 600
LTFEQDIERG NTDGLGDCHN SFVALNGHAS SLYPSTTTSD SASRDGYESR
610 620 630 640 650
GGMLDWNDLL EAPGSTDPLG AVSSHNHQDK KGVIRESYLK SNDQLVPVTL
660 670 680 690 700
LAIAVILAFV MGAVFSGIIV YCVCDHRRKD VAVVQRKEKE LTHSRRGSMS
710 720 730 740 750
SVTKLSGLFG DTQSKDPKPE AILTPLMHNG KLATPSNTAK MLIKADQHHL
760 770 780 790 800
DLTALPTPES TPTLQQKRKP NRGSREWERN QNIINACTKD MPPMGSPVIP
810 820 830 840 850
TDLPLRASPS HIPSVVVLPI TQQGYQHEYV DQPKMSEVVA QMALEDQAAT
860 870 880 890 900
LEYKTIKEHL SSKSPNHGVN LVENLDSLPP KVPQREASLG PPGTSLSQTG
910 920 930 940 950
LSKRLEMQHS SSYGLEYKRS YPTNSLTRSH QTTTLKRNNT NSSNSSHLSR
960 970 980 990 1000
NQSFGRGDNP PPAPQRVDSI QVHSSQPSGQ AVTVSRQPSL NAYNSLTRSG
1010 1020 1030
LKRTPSLKPD VPPKPSFAPL STSMKPNDAC T
Length:1,031
Mass (Da):114,433
Last modified:December 7, 2004 - v2
Checksum:i38565A81A4DA3BDB
GO
Isoform 2 (identifier: O35464-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     439-464: Missing.

Show »
Length:1,005
Mass (Da):111,726
Checksum:i5C282E0436E9AA38
GO
Isoform 3 (identifier: O35464-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     577-631: Missing.

Note: No experimental confirmation available.
Show »
Length:976
Mass (Da):108,646
Checksum:i4EB77AD756326289
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1721A → V in AAG29494 (PubMed:10993894).Curated
Sequence conflicti201 – 2011L → P in AAG29494 (PubMed:10993894).Curated
Sequence conflicti337 – 3371N → D in AAG29494 (PubMed:10993894).Curated
Sequence conflicti585 – 5851S → N in AAG29494 (PubMed:10993894).Curated
Sequence conflicti685 – 6851Q → R in AAG29494 (PubMed:10993894).Curated
Sequence conflicti703 – 7042TK → SE in AAG29494 (PubMed:10993894).Curated
Sequence conflicti735 – 7351P → S in AAG29494 (PubMed:10993894).Curated
Sequence conflicti766 – 7661Q → E in AAB86408 (PubMed:9204478).Curated
Sequence conflicti856 – 8561I → T in AAG29494 (PubMed:10993894).Curated
Sequence conflicti863 – 88826KSPNH…QREAS → ESSPYVLKQFSEAFNRQGII LSVAVE in AAB86408 (PubMed:9204478).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei439 – 46426Missing in isoform 2. 1 PublicationVSP_012097Add
BLAST
Alternative sequencei577 – 63155Missing in isoform 3. 1 PublicationVSP_012098Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF288666 mRNA. Translation: AAG29494.1.
BC059238 mRNA. Translation: AAH59238.1.
BC062979 mRNA. Translation: AAH62979.1.
AF030430 mRNA. Translation: AAB86408.1.
CCDSiCCDS37813.1. [O35464-1]
CCDS79642.1. [O35464-3]
RefSeqiNP_001298026.1. NM_001311097.1. [O35464-3]
NP_061214.2. NM_018744.2. [O35464-1]
UniGeneiMm.40909.

Genome annotation databases

EnsembliENSMUST00000019791; ENSMUSP00000019791; ENSMUSG00000019647. [O35464-1]
ENSMUST00000076043; ENSMUSP00000075420; ENSMUSG00000019647. [O35464-3]
ENSMUST00000156422; ENSMUSP00000121442; ENSMUSG00000019647. [O35464-1]
GeneIDi20358.
KEGGimmu:20358.
UCSCiuc008ewa.1. mouse. [O35464-1]
uc008ewb.1. mouse. [O35464-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF288666 mRNA. Translation: AAG29494.1.
BC059238 mRNA. Translation: AAH59238.1.
BC062979 mRNA. Translation: AAH62979.1.
AF030430 mRNA. Translation: AAB86408.1.
CCDSiCCDS37813.1. [O35464-1]
CCDS79642.1. [O35464-3]
RefSeqiNP_001298026.1. NM_001311097.1. [O35464-3]
NP_061214.2. NM_018744.2. [O35464-1]
UniGeneiMm.40909.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AFCX-ray2.50A/B19-570[»]
3AL8X-ray3.60A19-570[»]
3OKWX-ray2.30A/B19-571[»]
3OKYX-ray2.20B19-571[»]
ProteinModelPortaliO35464.
SMRiO35464. Positions 19-568.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59220N.
IntActiO35464. 1 interaction.
MINTiMINT-7996710.
STRINGi10090.ENSMUSP00000019791.

PTM databases

PhosphoSiteiO35464.

Proteomic databases

MaxQBiO35464.
PaxDbiO35464.
PRIDEiO35464.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019791; ENSMUSP00000019791; ENSMUSG00000019647. [O35464-1]
ENSMUST00000076043; ENSMUSP00000075420; ENSMUSG00000019647. [O35464-3]
ENSMUST00000156422; ENSMUSP00000121442; ENSMUSG00000019647. [O35464-1]
GeneIDi20358.
KEGGimmu:20358.
UCSCiuc008ewa.1. mouse. [O35464-1]
uc008ewb.1. mouse. [O35464-3]

Organism-specific databases

CTDi57556.
MGIiMGI:1203727. Sema6a.

Phylogenomic databases

eggNOGiKOG3611. Eukaryota.
ENOG410XQZC. LUCA.
GeneTreeiENSGT00760000119134.
HOGENOMiHOG000232047.
HOVERGENiHBG072910.
InParanoidiO35464.
KOiK06842.
OrthoDBiEOG7SV0TJ.
PhylomeDBiO35464.
TreeFamiTF316102.

Miscellaneous databases

ChiTaRSiSema6a. mouse.
EvolutionaryTraceiO35464.
NextBioi298237.
PROiO35464.
SOURCEiSearch...

Gene expression databases

BgeeiO35464.
ExpressionAtlasiO35464. baseline and differential.
GenevisibleiO35464. MM.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR016201. Plexin-like_fold.
IPR002165. Plexin_repeat.
IPR001627. Semap_dom.
IPR027231. Semaphorin.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERiPTHR11036. PTHR11036. 2 hits.
PfamiPF01437. PSI. 1 hit.
PF01403. Sema. 1 hit.
[Graphical view]
SMARTiSM00630. Sema. 1 hit.
[Graphical view]
SUPFAMiSSF101912. SSF101912. 1 hit.
SSF103575. SSF103575. 1 hit.
PROSITEiPS51004. SEMA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A-1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-like protein (EVL) via a novel carboxyl-terminal zyxin-like domain."
    Klostermann A., Lutz B., Gertler F., Behl C.
    J. Biol. Chem. 275:39647-39653(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH EVL.
    Tissue: Brain.
  2. "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] (ISOFORMS 1 AND 3).
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "Cloning and expression of a novel murine semaphorin with structural similarity to insect semaphorin I."
    Zhou L., White F.A., Lentz S.I., Wright D.E., Fisher D.A., Snider W.D.
    Mol. Cell. Neurosci. 9:26-41(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-888 (ISOFORM 1).
  4. "The transmembrane semaphorin Sema6A controls cerebellar granule cell migration."
    Kerjan G., Dolan J., Haumaitre C., Schneider-Maunoury S., Fujisawa H., Mitchell K.J., Chedotal A.
    Nat. Neurosci. 8:1516-1524(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  5. "Semaphorin-6A controls guidance of corticospinal tract axons at multiple choice points."
    Runker A.E., Little G.E., Suto F., Fujisawa H., Mitchell K.J.
    Neural Dev. 3:34-34(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-571 IN COMPLEX WITH PLXNA2, FUNCTION, SUBUNIT, GLYCOSYLATION AT ASN-65; ASN-282 AND ASN-434, DISULFIDE BONDS, MUTAGENESIS OF LEU-191 AND ILE-322.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 19-570 IN COMPLEX WITH PLXNA2, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-282 AND ASN-434, DISULFIDE BONDS, MUTAGENESIS OF HIS-212; LYS-393 AND MET-415.

Entry informationi

Entry nameiSEM6A_MOUSE
AccessioniPrimary (citable) accession number: O35464
Secondary accession number(s): Q6P5A8, Q6PCN9, Q9EQ71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 7, 2004
Last modified: May 11, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.