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Protein

Spectrin alpha chain, non-erythrocytic 1

Gene

Sptan1

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

Functioni

Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi2336 – 23471PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi2379 – 23902PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: MGI
  • calcium ion binding Source: InterPro
  • protein heterodimerization activity Source: MGI
  • spectrin binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding, Calcium, Calmodulin-binding, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-MMU-375165. NCAM signaling for neurite out-growth.
R-MMU-445095. Interaction between L1 and Ankyrins.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-6807878. COPI-mediated anterograde transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin alpha chain, non-erythrocytic 1
Alternative name(s):
Alpha-II spectrin
Fodrin alpha chain
Gene namesi
Name:Sptan1
Synonyms:Spna2, Spta2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:98386. Sptan1.

Subcellular locationi

  • Cytoplasmcytoskeleton
  • Cytoplasmcell cortex

  • Note: Expressed along the cell membrane in podocytes and presumptive tubule cells during glomerulogenesis and is expressed along lateral cell margins in tubule cells.By similarity

GO - Cellular componenti

  • cell-cell adherens junction Source: MGI
  • cortical cytoskeleton Source: MGI
  • cuticular plate Source: MGI
  • extracellular exosome Source: MGI
  • extracellular vesicle Source: MGI
  • fascia adherens Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • lateral plasma membrane Source: MGI
  • membrane Source: MGI
  • microtubule cytoskeleton Source: MGI
  • myelin sheath Source: UniProtKB
  • paranode region of axon Source: BHF-UCL
  • Z disc Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000734561 – 2472Spectrin alpha chain, non-erythrocytic 1Add BLAST2472

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei587PhosphoserineCombined sources1
Modified residuei637N6-acetyllysineBy similarity1
Modified residuei803N6-acetyllysineCombined sources1
Modified residuei924PhosphoserineBy similarity1
Modified residuei982PhosphoserineBy similarity1
Modified residuei999PhosphoserineBy similarity1
Modified residuei1029PhosphoserineCombined sources1
Modified residuei1031PhosphoserineCombined sources1
Modified residuei1041PhosphoserineBy similarity1
Modified residuei1176PhosphotyrosineBy similarity1
Modified residuei1190PhosphoserineCombined sources1
Modified residuei1207PhosphoserineBy similarity1
Modified residuei1217PhosphoserineCombined sources1
Modified residuei1291PhosphoserineCombined sources1
Modified residuei1306PhosphoserineBy similarity1
Modified residuei1323PhosphoserineCombined sources1
Modified residuei1338PhosphoserineBy similarity1
Modified residuei1519N6-acetyllysineBy similarity1
Modified residuei1550PhosphoserineCombined sources1
Modified residuei1557PhosphoserineBy similarity1
Modified residuei1578PhosphoserineBy similarity1
Modified residuei1615PhosphoserineBy similarity1
Modified residuei1647PhosphoserineBy similarity1
Modified residuei2020PhosphothreonineBy similarity1
Modified residuei2052N6-acetyllysineBy similarity1
Modified residuei2066PhosphothreonineCombined sources1
Modified residuei2421N6-acetyllysineBy similarity1

Post-translational modificationi

Phosphorylation of Tyr-1176 decreases sensitivity to cleavage by calpain in vitro.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1176 – 1177Cleavage; by mu-calpainBy similarity2

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP16546.
MaxQBiP16546.
PaxDbiP16546.
PeptideAtlasiP16546.
PRIDEiP16546.

2D gel databases

UCD-2DPAGEP16546.

PTM databases

iPTMnetiP16546.
PhosphoSitePlusiP16546.
SwissPalmiP16546.

Expressioni

Gene expression databases

BgeeiENSMUSG00000057738.
CleanExiMM_SPNA2.
ExpressionAtlasiP16546. baseline and differential.
GenevisibleiP16546. MM.

Interactioni

Subunit structurei

Like erythrocyte spectrin, the spectrin-like proteins are capable of forming dimers which can further associate to tetramers. Interacts (via C-terminal spectrin repeats) with TRPC4. Interacts with CALM and EMD. Interacts with isoform 1 of ACP1. Identified in a complex with ACTN4, CASK, IQGAP1, MAGI2, NPHS1 and SPTBN1. Interacts with SHANK3 (via ANK repeats) (By similarity).By similarity

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: MGI
  • protein heterodimerization activity Source: MGI
  • spectrin binding Source: MGI

Protein-protein interaction databases

DIPiDIP-37712N.
IntActiP16546. 13 interactors.
MINTiMINT-4135256.
STRINGi10090.ENSMUSP00000109348.

Structurei

3D structure databases

ProteinModelPortaliP16546.
SMRiP16546.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati10 – 42Spectrin 1Add BLAST33
Repeati44 – 147Spectrin 2Add BLAST104
Repeati149 – 253Spectrin 3Add BLAST105
Repeati255 – 359Spectrin 4Add BLAST105
Repeati361 – 465Spectrin 5Add BLAST105
Repeati467 – 571Spectrin 6Add BLAST105
Repeati573 – 676Spectrin 7Add BLAST104
Repeati678 – 782Spectrin 8Add BLAST105
Repeati784 – 888Spectrin 9Add BLAST105
Repeati890 – 955Spectrin 10Add BLAST66
Domaini967 – 1026SH3PROSITE-ProRule annotationAdd BLAST60
Repeati1062 – 1089Spectrin 11Add BLAST28
Repeati1091 – 1161Spectrin 12Add BLAST71
Repeati1208 – 1231Spectrin 13Add BLAST24
Repeati1233 – 1337Spectrin 14Add BLAST105
Repeati1339 – 1443Spectrin 15Add BLAST105
Repeati1445 – 1549Spectrin 16Add BLAST105
Repeati1551 – 1656Spectrin 17Add BLAST106
Repeati1658 – 1762Spectrin 18Add BLAST105
Repeati1764 – 1868Spectrin 19Add BLAST105
Repeati1870 – 1974Spectrin 20Add BLAST105
Repeati1976 – 2081Spectrin 21Add BLAST106
Repeati2091 – 2195Spectrin 22Add BLAST105
Repeati2205 – 2310Spectrin 23Add BLAST106
Domaini2323 – 2358EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini2366 – 2401EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini2404 – 2439EF-hand 3PROSITE-ProRule annotationAdd BLAST36

Sequence similaritiesi

Belongs to the spectrin family.Curated
Contains 3 EF-hand domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 23 spectrin repeats.Curated

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000246965.
HOVERGENiHBG059266.
InParanoidiP16546.

Family and domain databases

CDDicd00051. EFh. 1 hit.
Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR014837. EF-hand_Ca_insen.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR013315. Spectrin_alpha_SH3.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTiSM00054. EFh. 2 hits.
SM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P16546-1) [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
MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ
60 70 80 90 100
RDAEELEKWI QEKLQVASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV
110 120 130 140 150
KLDETGNLMI SEGHFASETI RTRLMELHRQ WELLLEKMRE KGIKLLQAQK
160 170 180 190 200
LVQYLRECED VMDWINDKEA IVTSEELGQD LEHVEVLQKK FEEFQTDLAA
210 220 230 240 250
HEERVNEVSQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL KGLALQRQGK
260 270 280 290 300
LFGAAEVQRF NRDVDETIGW IKEKEQLMAS DDFGRDLASV QALLRKHEGL
310 320 330 340 350
ERDLAALEDK VKALCAEADR LQQSHPLSAS QIQVKREELI TNWEQIRTLA
360 370 380 390 400
AERHARLDDS YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL
410 420 430 440 450
DRHQEHKGEI DAHEDSFKSA DESGQALLAA SHYASDEVRE KLSILSEERT
460 470 480 490 500
ALLELWELRR QQYEQCMDLQ LFYRDTEQVD NWMSKQEAFL LNEDLGDSLD
510 520 530 540 550
SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA MEDVATRRDA
560 570 580 590 600
LLSRRNALHE RAMHRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA
610 620 630 640 650
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKEEVA
660 670 680 690 700
ARMNEVISLW KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH
710 720 730 740 750
LASDDYGKDL TNVQNLQKKH ALLEADVAAH QDRIDGITIQ ARQFQDAGHF
760 770 780 790 800
DAENIKKKQE ALVARYEALK EPMVARKQKL ADSLRLQQLF RDVEDEETWI
810 820 830 840 850
REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI KAVTQKGNAM
860 870 880 890 900
VEEGHFAAED VKAKLSELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN
910 920 930 940 950
EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR
960 970 980 990 1000
EQAQSCRQQV APMDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST
1010 1020 1030 1040 1050
NKDWWKVEVN DRQGFVPAAY VKKLDPAQSA SRENLLEEQG SIALRQGQID
1060 1070 1080 1090 1100
NQTRITKEAG SVSLRMKQVE ELYQSLLELG EKRKGMLEKS CKKFMLFREA
1110 1120 1130 1140 1150
NELQQWITEK EAALTNEEVG ADLEQVEVLQ KKFDDFQKDL KANESRLKDI
1160 1170 1180 1190 1200
NKVAEDLESE GLMAEEVQAV QQQEVYGAMP RDEADSKTAS PWKSARLMVH
1210 1220 1230 1240 1250
TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE
1260 1270 1280 1290 1300
EKNQALNTDN YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAQRLI
1310 1320 1330 1340 1350
QSHPESAEDL KEKCTELNQA WTSLGKRADQ RKAKLGDSHD LQRFLSDFRD
1360 1370 1380 1390 1400
LMSWINGIRG LVSSDELAKD VTGAEALLER HQEHRTEIDA RAGTFQAFEQ
1410 1420 1430 1440 1450
FGQQLLAHGH YASPEIKEKL DILDQERTDL EKAWVQRRMM LDHCLELQLF
1460 1470 1480 1490 1500
HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK
1510 1520 1530 1540 1550
IAALQAFADQ LIAVDHYAKG DIANRRNEVL DRWRRLKAQM IEKRSKLGES
1560 1570 1580 1590 1600
QTLQQFSRDV DEIEAWISEK LQTASDESYK DPTNIQSKHQ KHQAFEAELH
1610 1620 1630 1640 1650
ANADRIRGVI DMGNSLIERG ACAGSEDAVK ARLAALADQW QFLVQKSAEK
1660 1670 1680 1690 1700
SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL LASEDYGKDL ASVNNLLKKH
1710 1720 1730 1740 1750
QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKEKRD TINGRFQKIK
1760 1770 1780 1790 1800
SMATSRRAKL SESHRLHQFF RDMDDEESWI KEKKLLVSSE DYGRDLTGVQ
1810 1820 1830 1840 1850
NLRKKHKRLE AELAAHEPAI QGVLDTGKKL SDDNTIGQEE IQQRLAQFVE
1860 1870 1880 1890 1900
HWKELKQLAA ARGQRLEESL EYQQFVANVE EEEAWINEKM TLVASEDYGD
1910 1920 1930 1940 1950
TLAAIQGLLK KHEAFETDFT VHKDRVNDVC TNGQDLIKKN NHHEENISSK
1960 1970 1980 1990 2000
MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ FNWKADVVES WIGEKENSLK
2010 2020 2030 2040 2050
TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK DQLLAAKHIQ
2060 2070 2080 2090 2100
SKAIEARHAS LMKRWTQLLA NSATRKKKLL EAQSHFRKVE DLFLTFAKKA
2110 2120 2130 2140 2150
SAFNSWFENA EEDLTDPVRC NSLEEIKALR EAHDAFRSSL SSAQADFNQL
2160 2170 2180 2190 2200
AELDRQIKSF RVASNPYTWF TMEALEETWR NLQKIIKERE LELQKEQRRQ
2210 2220 2230 2240 2250
EENDKLRQEF AQHANAFHQW IQETRTYLLD GSCMVEESGT LESQLEATKR
2260 2270 2280 2290 2300
KHQEIRAMRS QLKKIEDLGA AMEEALILDN KYTEHSTVGL AQQWDQLDQL
2310 2320 2330 2340 2350
GMRMQHNLEQ QIQARNTTGV TEEALKEFSM MFKHFDKDKS GRLNHQEFKS
2360 2370 2380 2390 2400
CLRSLGYDLP MVEEGEPDPE FEAILDTVDP NRDGHVSLQE YMAFMISRET
2410 2420 2430 2440 2450
ENVKSSEEIE SAFRALSSEG KPYVTKEELY QNLTREQADY CVSHMKPYVD
2460 2470
GKGRELPTAF DYVEFTRSLF VN
Length:2,472
Mass (Da):284,597
Last modified:January 9, 2007 - v4
Checksum:i7D778AC0B32D0AD6
GO
Isoform 2 (identifier: P16546-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1053-1072: Missing.

Show »
Length:2,452
Mass (Da):282,340
Checksum:i589EE26D4A8C4084
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti995T → A in CAA31289 (PubMed:2111175).Curated1
Sequence conflicti1156D → G in CAA31289 (PubMed:2111175).Curated1
Sequence conflicti1204T → S in CAA31289 (PubMed:2111175).Curated1
Sequence conflicti1279E → D in CAA31289 (PubMed:2111175).Curated1
Sequence conflicti1396Q → P in CAA31289 (PubMed:2111175).Curated1
Sequence conflicti1819A → S in BAB27703 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0220931053 – 1072Missing in isoform 2. 2 PublicationsAdd BLAST20

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL928926 Genomic DNA. Translation: CAM46236.1.
AL928926 Genomic DNA. Translation: CAM46238.1.
X12801 mRNA. Translation: CAA31289.1.
BC027791 mRNA. Translation: AAH27791.1.
AK011566 mRNA. Translation: BAB27703.1.
PIRiA43769.
PC7076.
UniGeneiMm.204969.

Genome annotation databases

EnsembliENSMUST00000046257; ENSMUSP00000047792; ENSMUSG00000057738. [P16546-2]
ENSMUST00000095083; ENSMUSP00000092697; ENSMUSG00000057738. [P16546-1]
UCSCiuc008jat.1. mouse. [P16546-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL928926 Genomic DNA. Translation: CAM46236.1.
AL928926 Genomic DNA. Translation: CAM46238.1.
X12801 mRNA. Translation: CAA31289.1.
BC027791 mRNA. Translation: AAH27791.1.
AK011566 mRNA. Translation: BAB27703.1.
PIRiA43769.
PC7076.
UniGeneiMm.204969.

3D structure databases

ProteinModelPortaliP16546.
SMRiP16546.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-37712N.
IntActiP16546. 13 interactors.
MINTiMINT-4135256.
STRINGi10090.ENSMUSP00000109348.

PTM databases

iPTMnetiP16546.
PhosphoSitePlusiP16546.
SwissPalmiP16546.

2D gel databases

UCD-2DPAGEP16546.

Proteomic databases

EPDiP16546.
MaxQBiP16546.
PaxDbiP16546.
PeptideAtlasiP16546.
PRIDEiP16546.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000046257; ENSMUSP00000047792; ENSMUSG00000057738. [P16546-2]
ENSMUST00000095083; ENSMUSP00000092697; ENSMUSG00000057738. [P16546-1]
UCSCiuc008jat.1. mouse. [P16546-1]

Organism-specific databases

MGIiMGI:98386. Sptan1.

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000246965.
HOVERGENiHBG059266.
InParanoidiP16546.

Enzyme and pathway databases

ReactomeiR-MMU-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-MMU-375165. NCAM signaling for neurite out-growth.
R-MMU-445095. Interaction between L1 and Ankyrins.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-6807878. COPI-mediated anterograde transport.

Miscellaneous databases

PROiP16546.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000057738.
CleanExiMM_SPNA2.
ExpressionAtlasiP16546. baseline and differential.
GenevisibleiP16546. MM.

Family and domain databases

CDDicd00051. EFh. 1 hit.
Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR014837. EF-hand_Ca_insen.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR013315. Spectrin_alpha_SH3.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTiSM00054. EFh. 2 hits.
SM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPTN1_MOUSE
AccessioniPrimary (citable) accession number: P16546
Secondary accession number(s): A3KGU6
, A3KGU8, Q8K380, Q9CT05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 9, 2007
Last modified: November 30, 2016
This is version 163 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.