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Protein

Rab GTPase-binding effector protein 1

Gene

Rabep1

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

Functioni

Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Involved in KCNH1 channels trafficking to and from the cell membrane. Stimulates RABGEF1 mediated nucleotide exchange on RAB5A.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis, Endocytosis, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Rab GTPase-binding effector protein 1
Alternative name(s):
Rabaptin-5
Rabaptin-5alpha
Gene namesi
Name:Rabep1
Synonyms:Rab5ep, Rabpt5, Rabpt5a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1860236. Rabep1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 862861Rab GTPase-binding effector protein 1PRO_0000187557Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei282 – 2821N6-acetyllysineBy similarity
Modified residuei374 – 3741PhosphoserineBy similarity
Modified residuei377 – 3771PhosphoserineBy similarity
Modified residuei407 – 4071PhosphoserineCombined sources
Modified residuei408 – 4081PhosphothreonineCombined sources
Modified residuei410 – 4101PhosphoserineCombined sources

Post-translational modificationi

Proteolytic cleavage by caspases in apoptotic cells causes loss of endosome fusion activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO35551.
MaxQBiO35551.
PaxDbiO35551.
PeptideAtlasiO35551.
PRIDEiO35551.

PTM databases

iPTMnetiO35551.
PhosphoSiteiO35551.

Expressioni

Gene expression databases

BgeeiO35551.
CleanExiMM_RABEP1.
ExpressionAtlasiO35551. baseline and differential.
GenevisibleiO35551. MM.

Interactioni

Subunit structurei

Heterodimer with RABGEF1. The heterodimer binds RAB4A and RAB5A that have been activated by GTP-binding. Binds TSC2, GGA1, GGA2, GGA3, AP1G1 and AP1G2 (By similarity). Interacts with ECM29 (By similarity). Interacts with KCNH1 (PubMed:22841712).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207592. 3 interactions.
IntActiO35551. 4 interactions.
MINTiMINT-4131497.
STRINGi10090.ENSMUSP00000075619.

Structurei

3D structure databases

ProteinModelPortaliO35551.
SMRiO35551. Positions 553-640, 802-854.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili11 – 345335Sequence analysisAdd
BLAST
Coiled coili534 – 816283Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the rabaptin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0993. Eukaryota.
ENOG410XSZ1. LUCA.
GeneTreeiENSGT00530000063743.
HOVERGENiHBG055335.
InParanoidiO35551.
KOiK12480.
OMAiQKEVHNA.
OrthoDBiEOG7WHH8T.
TreeFamiTF329365.

Family and domain databases

InterProiIPR003914. Rabaptin.
IPR029880. Rabaptin-5.
IPR018514. Rabaptin_coiled-coil.
IPR015390. Rabaptin_Rab5-bd_dom.
[Graphical view]
PANTHERiPTHR31179:SF5. PTHR31179:SF5. 2 hits.
PfamiPF09311. Rab5-bind. 1 hit.
PF03528. Rabaptin. 1 hit.
[Graphical view]
PRINTSiPR01432. RABAPTIN.

Sequences (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O35551-1) [UniParc]FASTAAdd to basket

Also known as: Rabaptin-5

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
MAQPGPAPQP DVSLQQRVAE LEKINAEFLR AQQQLEQEFN QKRAKFKELY
60 70 80 90 100
LAKEEDLKRQ NAVLQAAQDD LGHLRTQLWE AQAEMENIKA IATVSENTKQ
110 120 130 140 150
EAIDEVKRQW REEVASLQAI MKETVRDYEH QFHLRLEQER AQWAQYRESA
160 170 180 190 200
EREIADLRRR LSEGQEEENL ENEMKKAQED AEKLRSVVMP MEKEIAALKD
210 220 230 240 250
KLTEAEDKIK ELEASKVKEL NHYLEAEKSC RTDLEMYVAV LNTQKSVLQE
260 270 280 290 300
DAEKLRKELH EVCHLLEQER QQHNQLKHTW QKANDQFLES QRLLMRDMQR
310 320 330 340 350
MEIVLTSEQL RQVEELKKKD QEEDEQQRVN KRKDNKKTDT EEEVKIPVVC
360 370 380 390 400
ALTQEESSTP LSNEEEHLDS THGSVHSLDA DLMLPSGDPF SKSDNDMFKD
410 420 430 440 450
GLRRAQSTDS LGTSSSLQSK ALGYNYKAKS AGNLDESDFG PLVGADSVSE
460 470 480 490 500
NFDTVSLGSL QMPSGFMLTK DQERAIKAMT PEQEETASLL SSVTQGMESA
510 520 530 540 550
YVSPSGYRLV SETEWNLLQK EVHNAGNKLG RRCDMCSNYE KQLQGIQIQE
560 570 580 590 600
AETRDQVKKL QLMLRQANDQ LEKTMKEKQE LEDFLKQSAE DSSHQISALV
610 620 630 640 650
LRAQASEVLL EELQQSFSQA KRDVQEQMAV LMQSREQVSE ELVRLQKDND
660 670 680 690 700
SLQGKHSLHV SLQLAEDFIL PDTVEVLREL VLKYRENIVH VRTAADHMEE
710 720 730 740 750
KLKAEILFLK EQIQAEQCLK ENLEETLQLE IENCKEEIAS ISSLKAELER
760 770 780 790 800
IKVEKGQLES TLREKSQQLE SLQEMKVNLE EQLKKETAAK ATVEQLMFEE
810 820 830 840 850
KNKAQRLQTE LDVSEQVQRD FVKLSQTLQV QLERIRQADS LERIRAILND
860
TKLTDINQLP ET
Length:862
Mass (Da):99,524
Last modified:July 27, 2011 - v2
Checksum:i5796514BB94E7CE5
GO
Isoform 2 (identifier: O35551-2) [UniParc]FASTAAdd to basket

Also known as: Rabaptin-5gamma

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: MAQPGPAPQPDVSLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKE → MAQPGPAPQPD

Show »
Length:819
Mass (Da):94,348
Checksum:i1EC46FAA8E3FDFF1
GO
Isoform 3 (identifier: O35551-3) [UniParc]FASTAAdd to basket

Also known as: Rabaptin-5delta

The sequence of this isoform differs from the canonical sequence as follows:
     176-215: Missing.

Show »
Length:822
Mass (Da):95,026
Checksum:iAC228D687E2D717B
GO
Isoform 4 (identifier: O35551-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     366-367: EH → VK
     368-862: Missing.

Note: No experimental confirmation available.
Show »
Length:367
Mass (Da):43,381
Checksum:iDEB9F977AE99823E
GO
Isoform 5 (identifier: O35551-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     522-556: Missing.
     831-862: QLERIRQADSLERIRAILNDTKLTDINQLPET → RCLGNHHGPSVGGGTNVAGGLGSPLSLPQIFA

Note: May be due to an intron retention. No experimental confirmation available.
Show »
Length:827
Mass (Da):94,815
Checksum:iE47F1ACCA58C0134
GO
Isoform 6 (identifier: O35551-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     738-738: I → IVL

Note: No experimental confirmation available.
Show »
Length:864
Mass (Da):99,736
Checksum:i844089C4DF072AC4
GO

Sequence cautioni

The sequence AAH03921.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681Q → K in BAB31710 (PubMed:16141072).Curated
Sequence conflicti805 – 8051Q → R in BAA23818 (PubMed:9427343).Curated
Sequence conflicti805 – 8051Q → R in BAA21783 (PubMed:9427343).Curated
Sequence conflicti805 – 8051Q → R in AAF78238 (PubMed:11977240).Curated
Sequence conflicti805 – 8051Q → R in AAG44544 (PubMed:11977240).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5454MAQPG…YLAKE → MAQPGPAPQPD in isoform 2. 1 PublicationVSP_010452Add
BLAST
Alternative sequencei176 – 21540Missing in isoform 3. 1 PublicationVSP_010453Add
BLAST
Alternative sequencei366 – 3672EH → VK in isoform 4. 1 PublicationVSP_010454
Alternative sequencei368 – 862495Missing in isoform 4. 1 PublicationVSP_010455Add
BLAST
Alternative sequencei522 – 55635Missing in isoform 5. 1 PublicationVSP_010456Add
BLAST
Alternative sequencei738 – 7381I → IVL in isoform 6. 1 PublicationVSP_025444
Alternative sequencei831 – 86232QLERI…QLPET → RCLGNHHGPSVGGGTNVAGG LGSPLSLPQIFA in isoform 5. 1 PublicationVSP_010457Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86066 mRNA. Translation: BAA21783.1.
AB001750 mRNA. Translation: BAA23818.1.
AF248489 mRNA. Translation: AAF78238.1.
AF248490 mRNA. Translation: AAG44544.1.
AL596136 Genomic DNA. Translation: CAI26055.1.
CR933735, CR936845 Genomic DNA. Translation: CAM28155.1.
CH466596 Genomic DNA. Translation: EDL12625.1.
BC129854 mRNA. Translation: AAI29855.1.
BC003921 mRNA. Translation: AAH03921.1. Different initiation.
BC060166 mRNA. Translation: AAH60166.1.
BC129853 mRNA. Translation: AAI29854.1.
AK019413 mRNA. Translation: BAB31710.3.
CCDSiCCDS24968.1. [O35551-1]
CCDS70232.1. [O35551-2]
CCDS78984.1. [O35551-3]
RefSeqiNP_001278070.1. NM_001291141.1. [O35551-2]
NP_001278071.1. NM_001291142.1. [O35551-3]
NP_001278072.1. NM_001291143.1.
NP_062273.2. NM_019400.3. [O35551-1]
UniGeneiMm.7087.

Genome annotation databases

EnsembliENSMUST00000076270; ENSMUSP00000075619; ENSMUSG00000020817. [O35551-1]
ENSMUST00000081362; ENSMUSP00000080102; ENSMUSG00000020817. [O35551-3]
ENSMUST00000100928; ENSMUSP00000098488; ENSMUSG00000020817. [O35551-5]
ENSMUST00000108533; ENSMUSP00000104173; ENSMUSG00000020817. [O35551-6]
ENSMUST00000178245; ENSMUSP00000137267; ENSMUSG00000020817. [O35551-2]
GeneIDi54189.
KEGGimmu:54189.
UCSCiuc007jwr.3. mouse. [O35551-1]
uc007jwt.3. mouse. [O35551-2]
uc007jwu.1. mouse. [O35551-5]
uc011xyb.2. mouse. [O35551-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86066 mRNA. Translation: BAA21783.1.
AB001750 mRNA. Translation: BAA23818.1.
AF248489 mRNA. Translation: AAF78238.1.
AF248490 mRNA. Translation: AAG44544.1.
AL596136 Genomic DNA. Translation: CAI26055.1.
CR933735, CR936845 Genomic DNA. Translation: CAM28155.1.
CH466596 Genomic DNA. Translation: EDL12625.1.
BC129854 mRNA. Translation: AAI29855.1.
BC003921 mRNA. Translation: AAH03921.1. Different initiation.
BC060166 mRNA. Translation: AAH60166.1.
BC129853 mRNA. Translation: AAI29854.1.
AK019413 mRNA. Translation: BAB31710.3.
CCDSiCCDS24968.1. [O35551-1]
CCDS70232.1. [O35551-2]
CCDS78984.1. [O35551-3]
RefSeqiNP_001278070.1. NM_001291141.1. [O35551-2]
NP_001278071.1. NM_001291142.1. [O35551-3]
NP_001278072.1. NM_001291143.1.
NP_062273.2. NM_019400.3. [O35551-1]
UniGeneiMm.7087.

3D structure databases

ProteinModelPortaliO35551.
SMRiO35551. Positions 553-640, 802-854.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207592. 3 interactions.
IntActiO35551. 4 interactions.
MINTiMINT-4131497.
STRINGi10090.ENSMUSP00000075619.

PTM databases

iPTMnetiO35551.
PhosphoSiteiO35551.

Proteomic databases

EPDiO35551.
MaxQBiO35551.
PaxDbiO35551.
PeptideAtlasiO35551.
PRIDEiO35551.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000076270; ENSMUSP00000075619; ENSMUSG00000020817. [O35551-1]
ENSMUST00000081362; ENSMUSP00000080102; ENSMUSG00000020817. [O35551-3]
ENSMUST00000100928; ENSMUSP00000098488; ENSMUSG00000020817. [O35551-5]
ENSMUST00000108533; ENSMUSP00000104173; ENSMUSG00000020817. [O35551-6]
ENSMUST00000178245; ENSMUSP00000137267; ENSMUSG00000020817. [O35551-2]
GeneIDi54189.
KEGGimmu:54189.
UCSCiuc007jwr.3. mouse. [O35551-1]
uc007jwt.3. mouse. [O35551-2]
uc007jwu.1. mouse. [O35551-5]
uc011xyb.2. mouse. [O35551-3]

Organism-specific databases

CTDi9135.
MGIiMGI:1860236. Rabep1.

Phylogenomic databases

eggNOGiKOG0993. Eukaryota.
ENOG410XSZ1. LUCA.
GeneTreeiENSGT00530000063743.
HOVERGENiHBG055335.
InParanoidiO35551.
KOiK12480.
OMAiQKEVHNA.
OrthoDBiEOG7WHH8T.
TreeFamiTF329365.

Miscellaneous databases

ChiTaRSiRabep1. mouse.
PROiO35551.
SOURCEiSearch...

Gene expression databases

BgeeiO35551.
CleanExiMM_RABEP1.
ExpressionAtlasiO35551. baseline and differential.
GenevisibleiO35551. MM.

Family and domain databases

InterProiIPR003914. Rabaptin.
IPR029880. Rabaptin-5.
IPR018514. Rabaptin_coiled-coil.
IPR015390. Rabaptin_Rab5-bd_dom.
[Graphical view]
PANTHERiPTHR31179:SF5. PTHR31179:SF5. 2 hits.
PfamiPF09311. Rab5-bind. 1 hit.
PF03528. Rabaptin. 1 hit.
[Graphical view]
PRINTSiPR01432. RABAPTIN.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Neurocrescin: a novel neurite-outgrowth factor secreted by muscle after denervation."
    Nishimune H., Uyeda A., Nogawa M., Fujimori K., Taguchi T.
    NeuroReport 8:3649-3654(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: ICR.
    Tissue: Brain and Muscle.
  2. "Identification of a new alternative-splicing transcript of rabaptin-5 interacting with protein kinase MAK-V."
    Korobko E.V., Smirnova E.V., Kiselev S.L., Georgiev G.P., Korobko I.V.
    Dokl. Biochem. 370:1-3(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
    Strain: CBA/J.
    Tissue: Embryo.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 4; 5 AND 6).
    Strain: C57BL/6J.
    Tissue: Brain and Mammary gland.
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-316 (ISOFORMS 1/4/5).
    Strain: C57BL/6J.
    Tissue: Embryonic head.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407; THR-408 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. "Physical and functional interaction of KV10.1 with Rabaptin-5 impacts ion channel trafficking."
    Ninkovic M., Mitkovski M., Kohl T., Stuhmer W., Pardo L.A.
    FEBS Lett. 586:3077-3084(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNH1.

Entry informationi

Entry nameiRABE1_MOUSE
AccessioniPrimary (citable) accession number: O35551
Secondary accession number(s): A1L322
, Q5QNU3, Q99L08, Q9CRP3, Q9EQF9, Q9JI94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 117 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

Complete proteome, 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.