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Protein

Ras and Rab interactor 3

Gene

RIN3

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

Functioni

Ras effector protein that functions as a guanine nucleotide exchange (GEF) for RAB5B and RAB31, by exchanging bound GDP for free GTP. Required for normal RAB31 function.2 Publications

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB-KW
  • Rab GTPase binding Source: UniProtKB
  • Rab guanyl-nucleotide exchange factor activity Source: UniProtKB

GO - Biological processi

  • endocytosis Source: UniProtKB
  • positive regulation of GTPase activity Source: GOC
  • signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Ras and Rab interactor 3
Alternative name(s):
Ras interaction/interference protein 3
Gene namesi
Name:RIN3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:18751. RIN3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  • cytoplasmic vesicle Source: UniProtKB
  • early endosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi825 – 8251Y → A: Strongly reduced guanine nucleotide exchange factor activity toward RAB31; when associated with A-828. 1 Publication
Mutagenesisi828 – 8281T → A: Strongly reduced guanine nucleotide exchange factor activity toward RAB31; when associated with A-825. 1 Publication

Organism-specific databases

PharmGKBiPA38673.

Polymorphism and mutation databases

BioMutaiRIN3.
DMDMi209572780.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 985985Ras and Rab interactor 3PRO_0000191322Add
BLAST

Proteomic databases

PaxDbiQ8TB24.
PRIDEiQ8TB24.

PTM databases

PhosphoSiteiQ8TB24.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ8TB24.
CleanExiHS_RIN3.
ExpressionAtlasiQ8TB24. baseline and differential.
GenevestigatoriQ8TB24.

Organism-specific databases

HPAiHPA039836.

Interactioni

Subunit structurei

Interacts with CD2AP, RAB5B, RAB31 and BIN1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CRKP461082EBI-1570523,EBI-886
NCK1P163332EBI-1570523,EBI-389883
PLCG1P191743EBI-1570523,EBI-79387

Protein-protein interaction databases

BioGridi122974. 7 interactions.
IntActiQ8TB24. 46 interactions.
MINTiMINT-273957.
STRINGi9606.ENSP00000216487.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U23X-ray1.11B452-467[»]
ProteinModelPortaliQ8TB24.
SMRiQ8TB24. Positions 738-846.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 15896SH2PROSITE-ProRule annotationAdd
BLAST
Domaini703 – 846144VPS9PROSITE-ProRule annotationAdd
BLAST
Domaini877 – 96387Ras-associatingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni587 – 732146Interaction with RAB5BAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi24 – 296Poly-Glu
Compositional biasi248 – 514267Pro-richAdd
BLAST
Compositional biasi722 – 7254Poly-Thr
Compositional biasi965 – 9728Poly-Gly

Sequence similaritiesi

Contains 1 Ras-associating domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 VPS9 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiNOG295439.
GeneTreeiENSGT00530000063053.
HOVERGENiHBG038998.
InParanoidiQ8TB24.
OMAiYTIKEEK.
OrthoDBiEOG7PZRWP.
PhylomeDBiQ8TB24.
TreeFamiTF331067.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000159. Ras-assoc.
IPR000980. SH2.
IPR003123. VPS9.
[Graphical view]
PfamiPF02204. VPS9. 1 hit.
[Graphical view]
SMARTiSM00314. RA. 1 hit.
SM00252. SH2. 1 hit.
SM00167. VPS9. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
PROSITEiPS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
PS51205. VPS9. 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: Q8TB24-1) [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
MIRHAGAPAR GDPTGPVPVV GKGEEEEEED GMRLCLPANP KNCLPHRRGI
60 70 80 90 100
SILEKLIKTC PVWLQLSLGQ AEVARILHRV VAGMFLVRRD SSSKQLVLCV
110 120 130 140 150
HFPSLNESSA EVLEYTIKEE KSILYLEGSA LVFEDIFRLI AFYCVSRDLL
160 170 180 190 200
PFTLRLPQAI LEASSFTDLE TIANLGLGFW DSSLNPPQER GKPAEPPRDR
210 220 230 240 250
APGFPLVSSL RPTAHDANCA CEIELSVGND RLWFVNPIFI EDCSSALPTD
260 270 280 290 300
QPPLGNCPAR PLPPTSDATS PTSRWAPRRP PPPPPVLPLQ PCSPAQPPVL
310 320 330 340 350
PALAPAPACP LPTSPPVPAP HVTPHAPGPP DHPNQPPMMT CERLPCPTAG
360 370 380 390 400
LGPLREEAMK PGAASSPLQQ VPAPPLPAKK NLPTAPPRRR VSERVSLEDQ
410 420 430 440 450
SPGMAAEGDQ LSLPPQGTSD GPEDTPREST EQGQDTEVKA SDPHSMPELP
460 470 480 490 500
RTAKQPPVPP PRKKRISRQL ASTLPAPLEN AELCTQAMAL ETPTPGPPRE
510 520 530 540 550
GQSPASQAGT QHPPAQATAH SQSSPEFKGS LASLSDSLGV SVMATDQDSY
560 570 580 590 600
STSSTEEELE QFSSPSVKKK PSMILGKARH RLSFASFSSM FHAFLSNNRK
610 620 630 640 650
LYKKVVELAQ DKGSYFGSLV QDYKVYSLEM MARQTSSTEM LQEIRTMMTQ
660 670 680 690 700
LKSYLLQSTE LKALVDPALH SEEELEAIVE SALYKCVLKP LKEAINSCLH
710 720 730 740 750
QIHSKDGSLQ QLKENQLVIL ATTTTDLGVT TSVPEVPMME KILQKFTSMH
760 770 780 790 800
KAYSPEKKIS ILLKTCKLIY DSMALGNPGK PYGADDFLPV LMYVLARSNL
810 820 830 840 850
TEMLLNVEYM MELMDPALQL GEGSYYLTTT YGALEHIKSY DKITVTRQLS
860 870 880 890 900
VEVQDSIHRW ERRRTLNKAR ASRSSVQDFI CVSYLEPEQQ ARTLASRADT
910 920 930 940 950
QAQALCAQCA EKFAVERPQA HRLFVLVDGR CFQLADDALP HCIKGYLLRS
960 970 980
EPKRDFHFVY RPLDGGGGGG GGSPPCLVVR EPNFL
Length:985
Mass (Da):107,854
Last modified:October 14, 2008 - v4
Checksum:iA8949EA0D61570BB
GO
Isoform 4 (identifier: Q8TB24-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     878-903: DFICVSYLEPEQQARTLASRADTQAQ → VRPESGRGPVGPCPRHHPCCLLAKEP
     904-985: Missing.

Note: No experimental confirmation available.

Show »
Length:903
Mass (Da):98,739
Checksum:i562A82ADCBD13127
GO

Sequence cautioni

The sequence BAB13888.1 differs from that shown.Aberrant splicing.Curated
The sequence BAB15357.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC03432.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti742 – 7421I → F in AAH25248 (PubMed:15489334).Curated
Sequence conflicti965 – 9651Missing in BAB15357 (PubMed:14702039).Curated
Sequence conflicti965 – 9651Missing in AAH25248 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti111 – 1111E → K.
Corresponds to variant rs2274542 [ dbSNP | Ensembl ].
VAR_046645
Natural varianti215 – 2151H → L.
Corresponds to variant rs3829947 [ dbSNP | Ensembl ].
VAR_059960
Natural varianti215 – 2151H → P.
Corresponds to variant rs3829947 [ dbSNP | Ensembl ].
VAR_046646
Natural varianti215 – 2151H → R.
Corresponds to variant rs3829947 [ dbSNP | Ensembl ].
VAR_059961
Natural varianti425 – 4251T → I.
Corresponds to variant rs3742717 [ dbSNP | Ensembl ].
VAR_052946
Natural varianti425 – 4251T → M.1 Publication
Corresponds to variant rs3742717 [ dbSNP | Ensembl ].
VAR_046647
Natural varianti613 – 6131G → A.
Corresponds to variant rs12434929 [ dbSNP | Ensembl ].
VAR_046648

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei878 – 90326DFICV…DTQAQ → VRPESGRGPVGPCPRHHPCC LLAKEP in isoform 4. 1 PublicationVSP_007587Add
BLAST
Alternative sequencei904 – 98582Missing in isoform 4. 1 PublicationVSP_007588Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB081753 mRNA. Translation: BAC16513.1.
AL136332 Genomic DNA. No translation available.
AL159141 Genomic DNA. No translation available.
AK021762 mRNA. Translation: BAB13888.1. Sequence problems.
AK026092 mRNA. Translation: BAB15357.1. Different initiation.
AK074176 mRNA. Translation: BAB85002.1.
AK090451 mRNA. Translation: BAC03432.1. Sequence problems.
BC025248 mRNA. Translation: AAH25248.2.
AB060338 mRNA. Translation: BAB84316.1.
CCDSiCCDS32144.1. [Q8TB24-1]
PIRiT50623.
RefSeqiNP_079108.3. NM_024832.3. [Q8TB24-1]
UniGeneiHs.326822.

Genome annotation databases

EnsembliENST00000216487; ENSP00000216487; ENSG00000100599. [Q8TB24-1]
GeneIDi79890.
KEGGihsa:79890.
UCSCiuc001yap.3. human. [Q8TB24-1]
uc001yas.1. human. [Q8TB24-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB081753 mRNA. Translation: BAC16513.1.
AL136332 Genomic DNA. No translation available.
AL159141 Genomic DNA. No translation available.
AK021762 mRNA. Translation: BAB13888.1. Sequence problems.
AK026092 mRNA. Translation: BAB15357.1. Different initiation.
AK074176 mRNA. Translation: BAB85002.1.
AK090451 mRNA. Translation: BAC03432.1. Sequence problems.
BC025248 mRNA. Translation: AAH25248.2.
AB060338 mRNA. Translation: BAB84316.1.
CCDSiCCDS32144.1. [Q8TB24-1]
PIRiT50623.
RefSeqiNP_079108.3. NM_024832.3. [Q8TB24-1]
UniGeneiHs.326822.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U23X-ray1.11B452-467[»]
ProteinModelPortaliQ8TB24.
SMRiQ8TB24. Positions 738-846.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122974. 7 interactions.
IntActiQ8TB24. 46 interactions.
MINTiMINT-273957.
STRINGi9606.ENSP00000216487.

PTM databases

PhosphoSiteiQ8TB24.

Polymorphism and mutation databases

BioMutaiRIN3.
DMDMi209572780.

Proteomic databases

PaxDbiQ8TB24.
PRIDEiQ8TB24.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216487; ENSP00000216487; ENSG00000100599. [Q8TB24-1]
GeneIDi79890.
KEGGihsa:79890.
UCSCiuc001yap.3. human. [Q8TB24-1]
uc001yas.1. human. [Q8TB24-4]

Organism-specific databases

CTDi79890.
GeneCardsiGC14P092980.
H-InvDBHIX0011904.
HGNCiHGNC:18751. RIN3.
HPAiHPA039836.
MIMi610223. gene.
neXtProtiNX_Q8TB24.
PharmGKBiPA38673.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG295439.
GeneTreeiENSGT00530000063053.
HOVERGENiHBG038998.
InParanoidiQ8TB24.
OMAiYTIKEEK.
OrthoDBiEOG7PZRWP.
PhylomeDBiQ8TB24.
TreeFamiTF331067.

Miscellaneous databases

ChiTaRSiRIN3. human.
GenomeRNAii79890.
NextBioi69706.
PROiQ8TB24.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TB24.
CleanExiHS_RIN3.
ExpressionAtlasiQ8TB24. baseline and differential.
GenevestigatoriQ8TB24.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000159. Ras-assoc.
IPR000980. SH2.
IPR003123. VPS9.
[Graphical view]
PfamiPF02204. VPS9. 1 hit.
[Graphical view]
SMARTiSM00314. RA. 1 hit.
SM00252. SH2. 1 hit.
SM00167. VPS9. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
PROSITEiPS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
PS51205. VPS9. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RIN3: a novel Rab5 GEF interacting with amphiphysin II involved in the early endocytic pathway."
    Kajiho H., Saito K., Tsujita K., Kontani K., Araki Y., Kurosu H., Katada T.
    J. Cell Sci. 116:4159-4168(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH BIN1 AND RAB5B, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] OF 1-167 AND 405-985 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 485-985 (ISOFORM 4), VARIANT MET-425.
    Tissue: Embryo.
  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] OF 328-985 (ISOFORM 1).
    Tissue: Eye.
  5. "A novel binding protein composed of homophilic tetramer exhibits unique properties for the small GTPase Rab5."
    Saito K., Murai J., Kajiho H., Kontani K., Kurosu H., Katada T.
    J. Biol. Chem. 277:3412-3418(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 435-959 (ISOFORM 1).
    Tissue: Leukocyte and Spleen.
  6. "Tyr-phosphorylation signals translocate RIN3, the small GTPase Rab5-GEF, to early endocytic vesicles."
    Yoshikawa M., Kajiho H., Sakurai K., Minoda T., Nakagawa S., Kontani K., Katada T.
    Biochem. Biophys. Res. Commun. 372:168-172(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
  7. "Characterization of RIN3 as a guanine nucleotide exchange factor for the Rab5 subfamily GTPase Rab31."
    Kajiho H., Sakurai K., Minoda T., Yoshikawa M., Nakagawa S., Fukushima S., Kontani K., Katada T.
    J. Biol. Chem. 286:24364-24373(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-825 AND THR-828, INTERACTION WITH RAB31.
  8. "Atomic resolution crystal structure of the 2nd SH3 domain from human CD2AP (CMS) in complex with a proline-rich peptide from human RIN3."
    Structural genomics consortium (SGC)
    Submitted (DEC-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) OF 452-467 IN COMPLEX WITH CD2AP, INTERACTION WITH CD2AP.

Entry informationi

Entry nameiRIN3_HUMAN
AccessioniPrimary (citable) accession number: Q8TB24
Secondary accession number(s): Q76LB3
, Q8NF30, Q8TEE8, Q8WYP4, Q9H6A5, Q9HAG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: October 14, 2008
Last modified: May 27, 2015
This is version 117 of the entry and version 4 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 chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.