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Protein

Dihydropyrimidinase-related protein 1

Gene

CRMP1

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

Functioni

Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. May participate in cytokinesis.2 Publications

GO - Molecular functioni

GO - Biological processi

  • axon guidance Source: Reactome
  • microtubule cytoskeleton organization Source: InterPro
  • nervous system development Source: ProtInc
  • nucleobase-containing compound metabolic process Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_19199. CRMPs in Sema3A signaling.

Protein family/group databases

MEROPSiM38.974.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropyrimidinase-related protein 1
Short name:
DRP-1
Alternative name(s):
Collapsin response mediator protein 1
Short name:
CRMP-1
Unc-33-like phosphoprotein 3
Short name:
ULIP-3
Gene namesi
Name:CRMP1
Synonyms:DPYSL1, ULIP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:2365. CRMP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1022TT → AA: 2.5-fold increase in cells with a defect of cytokinesis. 1 Publication

Organism-specific databases

PharmGKBiPA26885.

Polymorphism and mutation databases

BioMutaiCRMP1.
DMDMi3122031.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572Dihydropyrimidinase-related protein 1PRO_0000165909Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321PhosphotyrosineBy similarity
Modified residuei101 – 1011Phosphothreonine; by AURKA1 Publication
Modified residuei102 – 1021Phosphothreonine; by AURKA1 Publication
Modified residuei258 – 2581N6-succinyllysineBy similarity
Modified residuei259 – 2591PhosphoserineBy similarity
Modified residuei316 – 3161Nitrated tyrosineBy similarity
Modified residuei431 – 4311PhosphotyrosineBy similarity
Modified residuei499 – 4991PhosphotyrosineBy similarity
Modified residuei504 – 5041PhosphotyrosineBy similarity
Modified residuei509 – 5091PhosphothreonineBy similarity
Modified residuei514 – 5141PhosphothreonineBy similarity
Modified residuei518 – 5181PhosphoserineBy similarity
Modified residuei522 – 5221PhosphoserineBy similarity

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

MaxQBiQ14194.
PaxDbiQ14194.
PRIDEiQ14194.

PTM databases

PhosphoSiteiQ14194.

Expressioni

Tissue specificityi

Brain.

Gene expression databases

BgeeiQ14194.
CleanExiHS_CRMP1.
ExpressionAtlasiQ14194. baseline and differential.
GenevisibleiQ14194. HS.

Organism-specific databases

HPAiCAB037313.
HPA035640.

Interactioni

Subunit structurei

Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4 or DPYSL5. Interacts with PLXNA1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
AP3M1Q9Y2T23EBI-473101,EBI-2371151
AXIN1O151692EBI-473101,EBI-710484
DPYSL3Q14195-23EBI-473101,EBI-10232496
HTTP428582EBI-473101,EBI-466029
VIMP086703EBI-473101,EBI-353844

Protein-protein interaction databases

BioGridi107790. 94 interactions.
IntActiQ14194. 73 interactions.
MINTiMINT-1423114.
STRINGi9606.ENSP00000321606.

Structurei

Secondary structure

1
572
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 2510Combined sources
Beta strandi30 – 389Combined sources
Beta strandi41 – 488Combined sources
Beta strandi53 – 597Combined sources
Beta strandi64 – 674Combined sources
Beta strandi69 – 746Combined sources
Helixi89 – 9911Combined sources
Beta strandi101 – 1088Combined sources
Helixi116 – 13015Combined sources
Beta strandi132 – 1409Combined sources
Helixi148 – 15710Combined sources
Beta strandi163 – 1708Combined sources
Turni171 – 1744Combined sources
Helixi178 – 19013Combined sources
Beta strandi194 – 1985Combined sources
Helixi202 – 21312Combined sources
Turni214 – 2163Combined sources
Helixi221 – 2255Combined sources
Helixi229 – 24618Combined sources
Beta strandi250 – 2556Combined sources
Helixi258 – 27013Combined sources
Beta strandi274 – 2796Combined sources
Helixi280 – 2845Combined sources
Helixi288 – 2914Combined sources
Helixi295 – 3006Combined sources
Helixi313 – 32210Combined sources
Helixi338 – 3414Combined sources
Helixi342 – 3443Combined sources
Helixi348 – 3503Combined sources
Turni358 – 3603Combined sources
Helixi361 – 3699Combined sources
Turni370 – 3734Combined sources
Helixi377 – 3848Combined sources
Helixi386 – 3916Combined sources
Turni395 – 3973Combined sources
Beta strandi409 – 41911Combined sources
Beta strandi426 – 4305Combined sources
Turni433 – 4364Combined sources
Beta strandi438 – 44811Combined sources
Beta strandi451 – 4555Combined sources
Helixi476 – 48914Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B3ZX-ray3.05A/B/C/D1-572[»]
ProteinModelPortaliQ14194.
SMRiQ14194. Positions 15-490.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0044.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiQ14194.
OMAiGINSFQV.
OrthoDBiEOG7SJD48.
PhylomeDBiQ14194.
TreeFamiTF314706.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro_1.
IPR030624. CRMP1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PANTHERiPTHR11647:SF54. PTHR11647:SF54. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q14194-1) [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
MSYQGKKSIP HITSDRLLIK GGRIINDDQS LYADVYLEDG LIKQIGENLI
60 70 80 90 100
VPGGVKTIEA NGRMVIPGGI DVNTYLQKPS QGMTAADDFF QGTRAALVGG
110 120 130 140 150
TTMIIDHVVP EPGSSLLTSF EKWHEAADTK SCCDYSLHVD ITSWYDGVRE
160 170 180 190 200
ELEVLVQDKG VNSFQVYMAY KDVYQMSDSQ LYEAFTFLKG LGAVILVHAE
210 220 230 240 250
NGDLIAQEQK RILEMGITGP EGHALSRPEE LEAEAVFRAI TIAGRINCPV
260 270 280 290 300
YITKVMSKSA ADIIALARKK GPLVFGEPIA ASLGTDGTHY WSKNWAKAAA
310 320 330 340 350
FVTSPPLSPD PTTPDYLTSL LACGDLQVTG SGHCPYSTAQ KAVGKDNFTL
360 370 380 390 400
IPEGVNGIEE RMTVVWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR
410 420 430 440 450
IAVGSDADVV IWDPDKLKTI TAKSHKSAVE YNIFEGMECH GSPLVVISQG
460 470 480 490 500
KIVFEDGNIN VNKGMGRFIP RKAFPEHLYQ RVKIRNKVFG LQGVSRGMYD
510 520 530 540 550
GPVYEVPATP KYATPAPSAK SSPSKHQPPP IRNLHQSNFS LSGAQIDDNN
560 570
PRRTGHRIVA PPGGRSNITS LG
Length:572
Mass (Da):62,184
Last modified:November 1, 1996 - v1
Checksum:iA5385FCC79328A30
GO
Isoform LCRMP-1 (identifier: Q14194-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MSYQGKKSIPHIT → MADRRRAWNT...DLPLGRDNGQ

Show »
Length:686
Mass (Da):74,262
Checksum:i2C897F656E5F34FA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti351 – 37020Missing in AAK55500 (PubMed:10048489).CuratedAdd
BLAST
Sequence conflicti504 – 5041Y → H in AAA93201 (PubMed:7637782).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti461 – 4611V → I.
Corresponds to variant rs34611001 [ dbSNP | Ensembl ].
VAR_037745

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1313MSYQG…IPHIT → MADRRRAWNTEDDLPVYLAR PGSAAQTPRQKYGGMFAAVE GAYENKTIDFDAYSVGRRGS ARTPRSAGRPDAVGLPGPGG SEDTASDVSEPSGSAVSSPG ERDERPPTLRIRRPAPRDLP LGRDNGQ in isoform LCRMP-1. 1 PublicationVSP_042545Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78012 mRNA. Translation: BAA11190.1.
DQ206871 mRNA. Translation: ABB22046.1.
BT006806 mRNA. Translation: AAP35452.1.
AC105915 Genomic DNA. Translation: AAY40959.1.
CH471131 Genomic DNA. Translation: EAW82405.1.
CH471131 Genomic DNA. Translation: EAW82407.1.
BC000252 mRNA. Translation: AAH00252.1.
BC007613 mRNA. Translation: AAH07613.1.
AH010780 Genomic DNA. Translation: AAK55500.1.
U17278 mRNA. Translation: AAA93201.1.
CCDSiCCDS33950.1. [Q14194-2]
CCDS43207.1. [Q14194-1]
PIRiJC5316.
RefSeqiNP_001014809.1. NM_001014809.2. [Q14194-2]
NP_001275590.1. NM_001288661.1.
NP_001275591.1. NM_001288662.1.
NP_001304.1. NM_001313.4. [Q14194-1]
UniGeneiHs.135270.

Genome annotation databases

EnsembliENST00000397890; ENSP00000380987; ENSG00000072832.
GeneIDi1400.
KEGGihsa:1400.
UCSCiuc003giq.3. human. [Q14194-1]
uc003gis.3. human. [Q14194-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78012 mRNA. Translation: BAA11190.1.
DQ206871 mRNA. Translation: ABB22046.1.
BT006806 mRNA. Translation: AAP35452.1.
AC105915 Genomic DNA. Translation: AAY40959.1.
CH471131 Genomic DNA. Translation: EAW82405.1.
CH471131 Genomic DNA. Translation: EAW82407.1.
BC000252 mRNA. Translation: AAH00252.1.
BC007613 mRNA. Translation: AAH07613.1.
AH010780 Genomic DNA. Translation: AAK55500.1.
U17278 mRNA. Translation: AAA93201.1.
CCDSiCCDS33950.1. [Q14194-2]
CCDS43207.1. [Q14194-1]
PIRiJC5316.
RefSeqiNP_001014809.1. NM_001014809.2. [Q14194-2]
NP_001275590.1. NM_001288661.1.
NP_001275591.1. NM_001288662.1.
NP_001304.1. NM_001313.4. [Q14194-1]
UniGeneiHs.135270.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B3ZX-ray3.05A/B/C/D1-572[»]
ProteinModelPortaliQ14194.
SMRiQ14194. Positions 15-490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107790. 94 interactions.
IntActiQ14194. 73 interactions.
MINTiMINT-1423114.
STRINGi9606.ENSP00000321606.

Protein family/group databases

MEROPSiM38.974.

PTM databases

PhosphoSiteiQ14194.

Polymorphism and mutation databases

BioMutaiCRMP1.
DMDMi3122031.

Proteomic databases

MaxQBiQ14194.
PaxDbiQ14194.
PRIDEiQ14194.

Protocols and materials databases

DNASUi1400.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000397890; ENSP00000380987; ENSG00000072832.
GeneIDi1400.
KEGGihsa:1400.
UCSCiuc003giq.3. human. [Q14194-1]
uc003gis.3. human. [Q14194-2]

Organism-specific databases

CTDi1400.
GeneCardsiGC04M005815.
HGNCiHGNC:2365. CRMP1.
HPAiCAB037313.
HPA035640.
MIMi602462. gene.
neXtProtiNX_Q14194.
PharmGKBiPA26885.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0044.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiQ14194.
OMAiGINSFQV.
OrthoDBiEOG7SJD48.
PhylomeDBiQ14194.
TreeFamiTF314706.

Enzyme and pathway databases

ReactomeiREACT_19199. CRMPs in Sema3A signaling.

Miscellaneous databases

ChiTaRSiCRMP1. human.
GeneWikiiCRMP1.
GenomeRNAii1400.
NextBioi5731.
PROiQ14194.
SOURCEiSearch...

Gene expression databases

BgeeiQ14194.
CleanExiHS_CRMP1.
ExpressionAtlasiQ14194. baseline and differential.
GenevisibleiQ14194. HS.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro_1.
IPR030624. CRMP1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PANTHERiPTHR11647:SF54. PTHR11647:SF54. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution."
    Hamajima N., Matsuda K., Sakata S., Tamaki N., Sasaki M., Nonaka M.
    Gene 180:157-163(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Long form collapsin response mediator protein-1 (LCRMP-1) expression is associated with clinical outcome and lymph node metastasis in non-small cell lung cancer patients."
    Pan S.-H., Chao Y.-C., Chen H.Y., Hung P.F., Lin P.Y., Lin C.W., Chang Y.L., Wu C.T., Lee Y.C., Yang S.-C., Hong T.-M., Yang P.-C.
    Lung Cancer 67:93-100(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LCRMP-1), ALTERNATIVE SPLICING.
    Tissue: Lung adenocarcinoma.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Eye.
  7. "Genomic organization and localization of the human CRMP-1 gene."
    Torres R., Polymeropoulos M.H.
    DNA Res. 5:393-395(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-572 (ISOFORM 1).
  8. "Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33."
    Goshima Y., Nakamura F., Strittmatter P., Strittmatter S.M.
    Nature 376:509-514(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 64-572 (ISOFORM 1).
    Tissue: Brain.
  9. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 44-56; 190-210; 246-254; 259-268; 346-361; 391-397; 452-463; 472-481; 488-511 AND 533-552, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  10. "Brain CRMP forms heterotetramers similar to liver dihydropyrimidinase."
    Wang L.H., Strittmatter S.M.
    J. Neurochem. 69:2261-2269(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH DPYSL2 AND DPYSL4.
  11. "Collapsin response mediator protein-1 and the invasion and metastasis of cancer cells."
    Shih J.-Y., Yang S.-C., Hong T.-M., Yuan A., Chen J.J.W., Yu C.-J., Chang Y.-L., Lee Y.-C., Peck K., Wu C.-W., Yang P.-C.
    J. Natl. Cancer Inst. 93:1392-1400(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "From midbody protein-protein interaction network construction to novel regulators in cytokinesis."
    Chen T.C., Lee S.A., Hong T.M., Shih J.Y., Lai J.M., Chiou H.Y., Yang S.C., Chan C.H., Kao C.Y., Yang P.C., Huang C.Y.
    J. Proteome Res. 8:4943-4953(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-101 AND THR-102, MUTAGENESIS OF 101-THR-THR-102.

Entry informationi

Entry nameiDPYL1_HUMAN
AccessioniPrimary (citable) accession number: Q14194
Secondary accession number(s): A0EJG6
, Q13024, Q4W5F1, Q96TC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 154 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

Caution

Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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.