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Protein

Ras-related protein Rab-7L1

Gene

RAB29

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

Functioni

Rab GTPase key regulator in vesicle trafficking. Essential for maintaining the integrity of the endosome-trans-Golgi network structure. Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. Regulates neuronal process morphology in the intact central nervous system (CNS). May play a role in the formation of typhoid toxin transport intermediates during Salmonella enterica serovar Typhi (S.Typhi) epithelial cell infection.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei41 – 422Cleavage; by S.Typhimurium viral protease GtgE

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 218GTPBy similarity
Nucleotide bindingi33 – 397GTPBy similarity
Nucleotide bindingi63 – 675GTPBy similarity
Nucleotide bindingi125 – 1284GTPBy similarity
Nucleotide bindingi156 – 1572GTPBy similarity

GO - Molecular functioni

  1. GDP binding Source: GO_Central
  2. GTPase activity Source: ProtInc
  3. GTP binding Source: GO_Central

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. Golgi organization Source: UniProtKB
  3. GTP catabolic process Source: GOC
  4. melanosome organization Source: GO_Central
  5. positive regulation of intracellular protein transport Source: UniProtKB
  6. protein transport Source: UniProtKB-KW
  7. Rab protein signal transduction Source: GO_Central
  8. retrograde transport, plasma membrane to Golgi Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Differentiation, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-7L1
Alternative name(s):
Rab-7-like protein 1
Ras-related protein Rab-29
Gene namesi
Name:RAB29
Synonyms:RAB7L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9789. RAB29.

Subcellular locationi

Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated. Cytoplasm. Cytoplasmperinuclear region. Golgi apparatus. Golgi apparatustrans-Golgi network. Vacuole. Cytoplasmcytoskeleton
Note: Colocalizes with LRRK2 along tubular structures emerging from Golgi apparatus (By similarity). Colocalizes with GM130 at the Golgi apparatus. Colocalizes with dynamic tubules emerging from and retracting to the Golgi apparatus. Colocalizes with TGN46 at the trans-Golgi network (TGN). In Salmonella enterica serovar Typhi (S.Typhi) infected epithelial cells, is recruited and colocalized with both S.Typhi-containing vacuoles and dynamic tubules as well as those emerging from the vacuole toward the cell periphery.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: UniProtKB
  4. melanosome Source: GO_Central
  5. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  6. plasma membrane Source: UniProtKB-SubCell
  7. trans-Golgi network Source: UniProtKB
  8. vacuole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane, Vacuole

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34151.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203Ras-related protein Rab-7L1PRO_0000121127Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi202 – 2021S-geranylgeranyl cysteineBy similarity
Lipidationi203 – 2031S-geranylgeranyl cysteineBy similarity

Post-translational modificationi

In case of Salmonella enterica serovar Typhimurium (S.Typhimurium) infection, is proteolytically cleaved between Gly-41 and Val-42 by the GtgE viral protease encoded on the Gifsy-2 lysogen bacteriophage, which therefore prevents the recruitment of RAB29 to S.Typhimurium-containing vacuoles. In contrast, no proteolytically cleavage is detected in S.Typhi-infected cells (PubMed:22042847).1 Publication

Keywords - PTMi

Lipoprotein, Prenylation

Proteomic databases

MaxQBiO14966.
PaxDbiO14966.
PRIDEiO14966.

PTM databases

PhosphoSiteiO14966.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiO14966.
CleanExiHS_RAB7L1.
ExpressionAtlasiO14966. baseline and differential.
GenevestigatoriO14966.

Organism-specific databases

HPAiCAB020822.
HPA026303.

Interactioni

Subunit structurei

Interacts with LRRK2.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0077EBI-372165,EBI-5323863

Protein-protein interaction databases

BioGridi114447. 6 interactions.
DIPiDIP-31215N.
IntActiO14966. 5 interactions.
STRINGi9606.ENSP00000235932.

Structurei

3D structure databases

ProteinModelPortaliO14966.
SMRiO14966. Positions 4-176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi36 – 449Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119125.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiO14966.
KOiK07916.
OMAiGQERFIS.
OrthoDBiEOG78M02X.
PhylomeDBiO14966.
TreeFamiTF324491.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O14966-1) [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
MGSRDHLFKV LVVGDAAVGK TSLVQRYSQD SFSKHYKSTV GVDFALKVLQ
60 70 80 90 100
WSDYEIVRLQ LWDIAGQERF TSMTRLYYRD ASACVIMFDV TNATTFSNSQ
110 120 130 140 150
RWKQDLDSKL TLPNGEPVPC LLLANKCDLS PWAVSRDQID RFSKENGFTG
160 170 180 190 200
WTETSVKENK NINEAMRVLI EKMMRNSTED IMSLSTQGDY INLQTKSSSW

SCC
Length:203
Mass (Da):23,155
Last modified:January 1, 1998 - v1
Checksum:i40E7CAB02446DF97
GO
Isoform 2 (identifier: O14966-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     42-65: Missing.

Note: No experimental confirmation available.

Show »
Length:179
Mass (Da):20,252
Checksum:i977C65E0E5641A2E
GO
Isoform 3 (identifier: O14966-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Note: No experimental confirmation available.

Show »
Length:131
Mass (Da):14,964
Checksum:i2DB0B04E3DC55E38
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7272Missing in isoform 3. 1 PublicationVSP_045078Add
BLAST
Alternative sequencei42 – 6524Missing in isoform 2. 1 PublicationVSP_043391Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84488 mRNA. Translation: BAA22160.1.
AK308359 mRNA. No translation available.
AK303879 mRNA. Translation: BAG64815.1.
AC119673 Genomic DNA. No translation available.
BC002585 mRNA. Translation: AAH02585.1.
CCDSiCCDS1459.1. [O14966-1]
CCDS44301.1. [O14966-2]
CCDS44302.1. [O14966-3]
RefSeqiNP_001129134.1. NM_001135662.1. [O14966-1]
NP_001129135.1. NM_001135663.1. [O14966-2]
NP_001129136.1. NM_001135664.1. [O14966-3]
NP_003920.1. NM_003929.2. [O14966-1]
XP_005245626.1. XM_005245569.1. [O14966-1]
XP_005245627.1. XM_005245570.1. [O14966-1]
XP_005245628.1. XM_005245571.1. [O14966-1]
XP_006711665.1. XM_006711602.1. [O14966-1]
XP_006711666.1. XM_006711603.1. [O14966-1]
XP_006711667.1. XM_006711604.1. [O14966-1]
XP_006711668.1. XM_006711605.1. [O14966-3]
XP_006711669.1. XM_006711606.1. [O14966-3]
UniGeneiHs.115325.

Genome annotation databases

EnsembliENST00000235932; ENSP00000235932; ENSG00000117280. [O14966-1]
ENST00000367139; ENSP00000356107; ENSG00000117280. [O14966-1]
ENST00000414729; ENSP00000402910; ENSG00000117280. [O14966-1]
ENST00000437324; ENSP00000416613; ENSG00000117280. [O14966-3]
ENST00000446390; ENSP00000389899; ENSG00000117280. [O14966-2]
GeneIDi8934.
KEGGihsa:8934.
UCSCiuc001hde.4. human. [O14966-1]
uc010prr.2. human. [O14966-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84488 mRNA. Translation: BAA22160.1.
AK308359 mRNA. No translation available.
AK303879 mRNA. Translation: BAG64815.1.
AC119673 Genomic DNA. No translation available.
BC002585 mRNA. Translation: AAH02585.1.
CCDSiCCDS1459.1. [O14966-1]
CCDS44301.1. [O14966-2]
CCDS44302.1. [O14966-3]
RefSeqiNP_001129134.1. NM_001135662.1. [O14966-1]
NP_001129135.1. NM_001135663.1. [O14966-2]
NP_001129136.1. NM_001135664.1. [O14966-3]
NP_003920.1. NM_003929.2. [O14966-1]
XP_005245626.1. XM_005245569.1. [O14966-1]
XP_005245627.1. XM_005245570.1. [O14966-1]
XP_005245628.1. XM_005245571.1. [O14966-1]
XP_006711665.1. XM_006711602.1. [O14966-1]
XP_006711666.1. XM_006711603.1. [O14966-1]
XP_006711667.1. XM_006711604.1. [O14966-1]
XP_006711668.1. XM_006711605.1. [O14966-3]
XP_006711669.1. XM_006711606.1. [O14966-3]
UniGeneiHs.115325.

3D structure databases

ProteinModelPortaliO14966.
SMRiO14966. Positions 4-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114447. 6 interactions.
DIPiDIP-31215N.
IntActiO14966. 5 interactions.
STRINGi9606.ENSP00000235932.

PTM databases

PhosphoSiteiO14966.

Proteomic databases

MaxQBiO14966.
PaxDbiO14966.
PRIDEiO14966.

Protocols and materials databases

DNASUi8934.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000235932; ENSP00000235932; ENSG00000117280. [O14966-1]
ENST00000367139; ENSP00000356107; ENSG00000117280. [O14966-1]
ENST00000414729; ENSP00000402910; ENSG00000117280. [O14966-1]
ENST00000437324; ENSP00000416613; ENSG00000117280. [O14966-3]
ENST00000446390; ENSP00000389899; ENSG00000117280. [O14966-2]
GeneIDi8934.
KEGGihsa:8934.
UCSCiuc001hde.4. human. [O14966-1]
uc010prr.2. human. [O14966-2]

Organism-specific databases

CTDi8934.
GeneCardsiGC01M205738.
HGNCiHGNC:9789. RAB29.
HPAiCAB020822.
HPA026303.
MIMi603949. gene.
neXtProtiNX_O14966.
PharmGKBiPA34151.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119125.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiO14966.
KOiK07916.
OMAiGQERFIS.
OrthoDBiEOG78M02X.
PhylomeDBiO14966.
TreeFamiTF324491.

Miscellaneous databases

ChiTaRSiRAB7L1. human.
GenomeRNAii8934.
NextBioi33592.
PROiO14966.
SOURCEiSearch...

Gene expression databases

BgeeiO14966.
CleanExiHS_RAB7L1.
ExpressionAtlasiO14966. baseline and differential.
GenevestigatoriO14966.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and chromosome assignment to 1q32 of a human cDNA (RAB7L1) encoding a small GTP-binding protein, a member of the RAS superfamily."
    Shimizu F., Katagiri T., Suzuki M., Watanabe T.K., Okuno S., Kuga Y., Nagata M., Fujiwara T., Nakamura Y., Takahashi E.
    Cytogenet. Cell Genet. 77:261-263(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Thymus and Trachea.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1).
    Tissue: Ovary.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Proteolytic targeting of Rab29 by an effector protein distinguishes the intracellular compartments of human-adapted and broad-host Salmonella."
    Spano S., Liu X., Galan J.E.
    Proc. Natl. Acad. Sci. U.S.A. 108:18418-18423(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SALMONELLA INFECTION, CLEAVAGE BY GIFSY-2 BACTERIOPHAGE GTGE, SUBCELLULAR LOCATION.
  8. "A role of rab29 in the integrity of the trans-Golgi network and retrograde trafficking of mannose-6-phosphate receptor."
    Wang S., Ma Z., Xu X., Wang Z., Sun L., Zhou Y., Lin X., Hong W., Wang T.
    PLoS ONE 9:E96242-E96242(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RETROGRADE TRANSPORT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiRAB7L_HUMAN
AccessioniPrimary (citable) accession number: O14966
Secondary accession number(s): B4E1K3, C9JE77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 1, 1998
Last modified: February 4, 2015
This is version 142 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.