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Protein

Ras and Rab interactor 2

Gene

RIN2

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

Functioni

Ras effector protein. May function as an upstream activator and/or downstream effector for RAB5B in endocytic pathway. May function as a guanine nucleotide exchange (GEF) of RAB5B, required for activating the RAB5 proteins by exchanging bound GDP for free GTP.1 Publication

GO - Molecular functioni

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

GO - Biological processi

  • endocytosis Source: UniProtKB-KW
  • positive regulation of GTPase activity Source: GOC
  • regulation of catalytic activity Source: GOC
  • small GTPase mediated signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Endocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Ras and Rab interactor 2
Alternative name(s):
Ras association domain family 4
Ras inhibitor JC265
Ras interaction/interference protein 2
Gene namesi
Name:RIN2
Synonyms:RASSF4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:18750. RIN2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

MACS syndrome (MACS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA complex disorder of elastic tissue characterized by sagging skin and occasionally by life-threatening visceral complications.
See also OMIM:613075

Organism-specific databases

MalaCardsiRIN2.
MIMi613075. phenotype.
Orphaneti217335. MACS syndrome.
PharmGKBiPA38672.

Polymorphism and mutation databases

BioMutaiRIN2.
DMDMi28201876.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 895895Ras and Rab interactor 2PRO_0000191320Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei366 – 3661PhosphoserineBy similarity
Modified residuei501 – 5011PhosphoserineBy similarity
Modified residuei509 – 5091PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8WYP3.
PaxDbiQ8WYP3.
PRIDEiQ8WYP3.

PTM databases

iPTMnetiQ8WYP3.
PhosphoSiteiQ8WYP3.

Expressioni

Tissue specificityi

Widely expressed. Expressed in heart, kidney, lung placenta. Expressed at low level in skeletal muscle, spleen and peripheral blood.1 Publication

Gene expression databases

BgeeiQ8WYP3.
CleanExiHS_RASSF4.
HS_RIN2.
ExpressionAtlasiQ8WYP3. baseline and differential.
GenevisibleiQ8WYP3. HS.

Organism-specific databases

HPAiHPA034641.

Interactioni

Subunit structurei

Homotetramer; probably composed of anti-parallel linkage of two parallel dimers. Interacts with Ras. Interacts with RAB5B, with a much higher affinity for GTP-bound activated RAB5B. Does not interact with other members of the Rab family.2 Publications

Protein-protein interaction databases

BioGridi119960. 9 interactions.
IntActiQ8WYP3. 3 interactions.
MINTiMINT-1493616.
STRINGi9606.ENSP00000255006.

Structurei

3D structure databases

ProteinModelPortaliQ8WYP3.
SMRiQ8WYP3. Positions 577-750.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini97 – 19094SH2PROSITE-ProRule annotationAdd
BLAST
Domaini618 – 757140VPS9PROSITE-ProRule annotationAdd
BLAST
Domaini787 – 87892Ras-associatingPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi307 – 3148Poly-Pro

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

eggNOGiKOG2320. Eukaryota.
ENOG410ZZW5. LUCA.
GeneTreeiENSGT00530000063053.
HOVERGENiHBG023719.
InParanoidiQ8WYP3.
OMAiESRPPCH.
OrthoDBiEOG7PZRWP.
PhylomeDBiQ8WYP3.
TreeFamiTF331067.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000159. RA_dom.
IPR000980. SH2.
IPR029071. Ubiquitin-rel_dom.
IPR003123. VPS9.
[Graphical view]
PfamiPF00788. RA. 1 hit.
PF02204. VPS9. 1 hit.
[Graphical view]
SMARTiSM00314. RA. 1 hit.
SM00167. VPS9. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF55550. 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: Q8WYP3-1) [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
MTAWTMGARG LDKRGSFFKL IDTIASEIGE LKQEMVRTDV NLENGLEPAE
60 70 80 90 100
THSMVRHKDG GYSEEEDVKT CARDSGYDSL SNRLSILDRL LHTHPIWLQL
110 120 130 140 150
SLSEEEAAEV LQAQPPGIFL VHKSTKMQKK VLSLRLPCEF GAPLKEFAIK
160 170 180 190 200
ESTYTFSLEG SGISFADLFR LIAFYCISRD VLPFTLKLPY AISTAKSEAQ
210 220 230 240 250
LEELAQMGLN FWSSPADSKP PNLPPPHRPL SSDGVCPASL RQLCLINGVH
260 270 280 290 300
SIKTRTPSEL ECSQTNGALC FINPLFLKVH SQDLSGGLKR PSTRTPNANG
310 320 330 340 350
TERTRSPPPR PPPPAINSLH TSPRLARTET QTSMPETVNH NKHGNVALPG
360 370 380 390 400
TKPTPIPPPR LKKQASFLEA EGGAKTLSGG RPGAGPELEL GTAGSPGGAP
410 420 430 440 450
PEAAPGDCTR APPPSSESRP PCHGGRQRLS DMSISTSSSD SLEFDRSMPL
460 470 480 490 500
FGYEADTNSS LEDYEGESDQ ETMAPPIKSK KKRSSSFVLP KLVKSQLQKV
510 520 530 540 550
SGVFSSFMTP EKRMVRRIAE LSRDKCTYFG CLVQDYVSFL QENKECHVSS
560 570 580 590 600
TDMLQTIRQF MTQVKNYLSQ SSELDPPIES LIPEDQIDVV LEKAMHKCIL
610 620 630 640 650
KPLKGHVEAM LKDFHMADGS WKQLKENLQL VRQRNPQELG VFAPTPDFVD
660 670 680 690 700
VEKIKVKFMT MQKMYSPEKK VMLLLRVCKL IYTVMENNSG RMYGADDFLP
710 720 730 740 750
VLTYVIAQCD MLELDTEIEY MMELLDPSLL HGEGGYYLTS AYGALSLIKN
760 770 780 790 800
FQEEQAARLL SSETRDTLRQ WHKRRTTNRT IPSVDDFQNY LRVAFQEVNS
810 820 830 840 850
GCTGKTLLVR PYITTEDVCQ ICAEKFKVGD PEEYSLFLFV DETWQQLAED
860 870 880 890
TYPQKIKAEL HSRPQPHIFH FVYKRIKNDP YGIIFQNGEE DLTTS
Length:895
Mass (Da):100,163
Last modified:March 1, 2002 - v1
Checksum:i0DECDBF8D2629EE4
GO
Isoform 2 (identifier: Q8WYP3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLDSFSQESTLPFREARKRTSFQPVQVWRNFTASQTTESPACSGASLGEM

Note: No experimental confirmation available.
Show »
Length:944
Mass (Da):105,613
Checksum:iEB0C72971CE5BFB6
GO

Sequence cautioni

The sequence CAB66858.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1921I → V in AK094884 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti197 – 1971S → T.1 Publication
Corresponds to variant rs3803981 [ dbSNP | Ensembl ].
VAR_024694
Natural varianti643 – 6431A → T.
Corresponds to variant rs199603 [ dbSNP | Ensembl ].
VAR_052945

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MLDSFSQESTLPFREARKRT SFQPVQVWRNFTASQTTESP ACSGASLGEM in isoform 2. 1 PublicationVSP_015145

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB060339 mRNA. Translation: BAB84317.1.
AL049538, AL132821 Genomic DNA. Translation: CAI19340.1.
AL132821, AL049538 Genomic DNA. Translation: CAI23572.1.
AK094884 mRNA. No translation available.
AL136924 mRNA. Translation: CAB66858.1. Different initiation.
M37190 mRNA. Translation: AAA36553.1.
CCDSiCCDS56182.1. [Q8WYP3-2]
PIRiB38637.
RefSeqiNP_001229510.1. NM_001242581.1. [Q8WYP3-2]
NP_061866.1. NM_018993.3. [Q8WYP3-1]
XP_005260788.1. XM_005260731.2. [Q8WYP3-1]
XP_006723637.1. XM_006723574.2. [Q8WYP3-1]
XP_006723638.1. XM_006723575.2. [Q8WYP3-1]
XP_006723640.1. XM_006723577.2. [Q8WYP3-1]
XP_011527559.1. XM_011529257.1. [Q8WYP3-1]
XP_011527560.1. XM_011529258.1. [Q8WYP3-1]
UniGeneiHs.472270.
Hs.733605.

Genome annotation databases

EnsembliENST00000255006; ENSP00000255006; ENSG00000132669. [Q8WYP3-2]
GeneIDi54453.
KEGGihsa:54453.
UCSCiuc002wro.3. human. [Q8WYP3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB060339 mRNA. Translation: BAB84317.1.
AL049538, AL132821 Genomic DNA. Translation: CAI19340.1.
AL132821, AL049538 Genomic DNA. Translation: CAI23572.1.
AK094884 mRNA. No translation available.
AL136924 mRNA. Translation: CAB66858.1. Different initiation.
M37190 mRNA. Translation: AAA36553.1.
CCDSiCCDS56182.1. [Q8WYP3-2]
PIRiB38637.
RefSeqiNP_001229510.1. NM_001242581.1. [Q8WYP3-2]
NP_061866.1. NM_018993.3. [Q8WYP3-1]
XP_005260788.1. XM_005260731.2. [Q8WYP3-1]
XP_006723637.1. XM_006723574.2. [Q8WYP3-1]
XP_006723638.1. XM_006723575.2. [Q8WYP3-1]
XP_006723640.1. XM_006723577.2. [Q8WYP3-1]
XP_011527559.1. XM_011529257.1. [Q8WYP3-1]
XP_011527560.1. XM_011529258.1. [Q8WYP3-1]
UniGeneiHs.472270.
Hs.733605.

3D structure databases

ProteinModelPortaliQ8WYP3.
SMRiQ8WYP3. Positions 577-750.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119960. 9 interactions.
IntActiQ8WYP3. 3 interactions.
MINTiMINT-1493616.
STRINGi9606.ENSP00000255006.

PTM databases

iPTMnetiQ8WYP3.
PhosphoSiteiQ8WYP3.

Polymorphism and mutation databases

BioMutaiRIN2.
DMDMi28201876.

Proteomic databases

MaxQBiQ8WYP3.
PaxDbiQ8WYP3.
PRIDEiQ8WYP3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000255006; ENSP00000255006; ENSG00000132669. [Q8WYP3-2]
GeneIDi54453.
KEGGihsa:54453.
UCSCiuc002wro.3. human. [Q8WYP3-1]

Organism-specific databases

CTDi54453.
GeneCardsiRIN2.
HGNCiHGNC:18750. RIN2.
HPAiHPA034641.
MalaCardsiRIN2.
MIMi610222. gene.
613075. phenotype.
neXtProtiNX_Q8WYP3.
Orphaneti217335. MACS syndrome.
PharmGKBiPA38672.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2320. Eukaryota.
ENOG410ZZW5. LUCA.
GeneTreeiENSGT00530000063053.
HOVERGENiHBG023719.
InParanoidiQ8WYP3.
OMAiESRPPCH.
OrthoDBiEOG7PZRWP.
PhylomeDBiQ8WYP3.
TreeFamiTF331067.

Miscellaneous databases

ChiTaRSiRIN2. human.
GenomeRNAii54453.
NextBioi56681.
PROiQ8WYP3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WYP3.
CleanExiHS_RASSF4.
HS_RIN2.
ExpressionAtlasiQ8WYP3. baseline and differential.
GenevisibleiQ8WYP3. HS.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000159. RA_dom.
IPR000980. SH2.
IPR029071. Ubiquitin-rel_dom.
IPR003123. VPS9.
[Graphical view]
PfamiPF00788. RA. 1 hit.
PF02204. VPS9. 1 hit.
[Graphical view]
SMARTiSM00314. RA. 1 hit.
SM00167. VPS9. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
PS51205. VPS9. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH RAB5B.
    Tissue: Leukocyte.
  2. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [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 1-852 (ISOFORM 2), VARIANT THR-197.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-895 (ISOFORMS 1/2).
    Tissue: Uterus.
  5. "Expression of three mammalian cDNAs that interfere with RAS function in Saccharomyces cerevisiae."
    Colicelli J., Nicolette C., Birchmeier C., Rodgers L., Riggs M., Wigler M.
    Proc. Natl. Acad. Sci. U.S.A. 88:2913-2917(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 425-895 (ISOFORMS 1/2), INTERACTION WITH RAS.
    Tissue: Glial cell.
  6. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. Cited for: INVOLVEMENT IN MACS SYNDROME.
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRIN2_HUMAN
AccessioniPrimary (citable) accession number: Q8WYP3
Secondary accession number(s): Q00425
, Q5TFT8, Q9BQL3, Q9H071
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: March 1, 2002
Last modified: May 11, 2016
This is version 117 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 20
    Human chromosome 20: 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. 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.