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Protein

Calmodulin-regulated spectrin-associated protein 3

Gene

CAMSAP3

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

Functioni

Microtubule minus-end binding protein that acts as a regulator of non-centrosomal microtubule dynamics and organization. Specifically required for the biogenesis and the maintenance of zonula adherens by anchoring the minus-end of microtubules to zonula adherens and by recruiting the kinesin KIFC3 to those junctional sites. May regulate the nucleation and the polymerization of microtubules. Indirectly, through the microtubule cytoskeleton, may regulate the organization of cellular organelles including the Golgi and the early endosomes.2 Publications

GO - Molecular functioni

  • microtubule minus-end binding Source: UniProtKB

GO - Biological processi

  • epithelial cell-cell adhesion Source: UniProtKB
  • microtubule anchoring Source: UniProtKB
  • microtubule cytoskeleton organization Source: UniProtKB
  • negative regulation of phosphatase activity Source: UniProtKB
  • neuron projection development Source: InterPro
  • regulation of microtubule cytoskeleton organization Source: UniProtKB
  • regulation of organelle organization Source: UniProtKB
  • zonula adherens maintenance Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Calmodulin-regulated spectrin-associated protein 3
Alternative name(s):
Protein Nezha
Gene namesi
Name:CAMSAP3
Synonyms:KIAA1543
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:29307. CAMSAP3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • zonula adherens Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134885087.

Polymorphism and mutation databases

BioMutaiCAMSAP3.
DMDMi61213747.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12491249Calmodulin-regulated spectrin-associated protein 3PRO_0000050799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei184 – 1841PhosphothreonineCombined sources
Modified residuei193 – 1931PhosphoserineCombined sources
Modified residuei334 – 3341PhosphoserineCombined sources
Modified residuei341 – 3411PhosphoserineCombined sources
Modified residuei347 – 3471PhosphoserineCombined sources
Modified residuei351 – 3511PhosphoserineBy similarity
Modified residuei368 – 3681PhosphoserineCombined sources
Modified residuei547 – 5471PhosphoserineCombined sources
Modified residuei554 – 5541PhosphoserineCombined sources
Modified residuei560 – 5601PhosphoserineCombined sources
Modified residuei685 – 6851PhosphoserineCombined sources
Modified residuei799 – 7991PhosphothreonineCombined sources
Modified residuei814 – 8141PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9P1Y5.
MaxQBiQ9P1Y5.
PaxDbiQ9P1Y5.
PRIDEiQ9P1Y5.

PTM databases

iPTMnetiQ9P1Y5.
PhosphoSiteiQ9P1Y5.

Expressioni

Gene expression databases

BgeeiQ9P1Y5.
CleanExiHS_KIAA1543.
GenevisibleiQ9P1Y5. HS.

Organism-specific databases

HPAiHPA043830.

Interactioni

Subunit structurei

Interacts with PLEKHA7. Interacts with CAMSAP2 (By similarity).By similarity

GO - Molecular functioni

  • microtubule minus-end binding Source: UniProtKB

Protein-protein interaction databases

BioGridi121695. 22 interactions.
DIPiDIP-52405N.
IntActiQ9P1Y5. 21 interactions.
MINTiMINT-1402687.
STRINGi9606.ENSP00000416797.

Structurei

3D structure databases

ProteinModelPortaliQ9P1Y5.
SMRiQ9P1Y5. Positions 1108-1244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini163 – 312150CHAdd
BLAST
Domaini1109 – 1243135CKKPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi437 – 548112Pro-richAdd
BLAST
Compositional biasi730 – 841112Pro-richAdd
BLAST

Domaini

The CKK domain binds microtubules.PROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the CAMSAP1 family.PROSITE-ProRule annotation
Contains 1 CKK domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3654. Eukaryota.
ENOG4111D0B. LUCA.
GeneTreeiENSGT00390000010026.
HOGENOMiHOG000059671.
InParanoidiQ9P1Y5.
KOiK17493.
OMAiDFTRQEY.
OrthoDBiEOG7P8P6Z.
PhylomeDBiQ9P1Y5.
TreeFamiTF315529.

Family and domain databases

InterProiIPR032940. CAMSAP.
IPR031372. CAMSAP_CC1.
IPR022613. CAMSAP_CH.
IPR001715. CH-domain.
IPR014797. CKK_domain.
IPR011033. PRC_barrel-like.
[Graphical view]
PANTHERiPTHR21595. PTHR21595. 2 hits.
PfamiPF17095. CAMSAP_CC1. 1 hit.
PF11971. CAMSAP_CH. 1 hit.
PF08683. CAMSAP_CKK. 1 hit.
[Graphical view]
SMARTiSM01051. CAMSAP_CKK. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF50346. SSF50346. 1 hit.
PROSITEiPS51508. CKK. 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: Q9P1Y5-1) [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
MVEAAPPGPG PLRRTFLVPE IKSLDQYDFS RAKAAASLAW VLRAAFGGAE
60 70 80 90 100
HVPPELWEPF YTDQYAQEHV KPPVTRLLLS AELYCRAWRQ ALPQLETPPN
110 120 130 140 150
PSALLALLAR RGTVPALPER PVREADLRHQ PILMGAHLAV IDALMAAFAF
160 170 180 190 200
EWTKTLPGPL ALTSLEHKLL FWVDTTVRRL QEKTEQEAAQ RASPAAPADG
210 220 230 240 250
AAPAQPSIRY RKDRVVARRA PCFPTVTSLQ DLASGAALAA TIHCYCPQLL
260 270 280 290 300
RLEEVCLKDP MSVADSLYNL QLVQDFCASR LPRGCPLSLE DLLYVPPPLK
310 320 330 340 350
VNLVVMLAEL FMCFEVLKPD FVQVKDLPDG HAASPRGTEA SPPQNNSGSS
360 370 380 390 400
SPVFTFRHPL LSSGGPQSPL RGSTGSLKSS PSMSHMEALG KAWNRQLSRP
410 420 430 440 450
LSQAVSFSTP FGLDSDVDVV MGDPVLLRSV SSDSLGPPRP APARTPTQPP
460 470 480 490 500
PEPGDLPTIE EALQIIHSAE PRLLPDGAAD GSFYLHSPEG PSKPSLASPY
510 520 530 540 550
LPEGTSKPLS DRPTKAPVYM PHPETPSKPS PCLVGEASKP PAPSEGSPKA
560 570 580 590 600
VASSPAATNS EVKMTSFAER KKQLVKAEAE AGAGSPTSTP APPEALSSEM
610 620 630 640 650
SELSARLEEK RRAIEAQKRR IEAIFAKHRQ RLGKSAFLQV QPREASGEAE
660 670 680 690 700
AEAEEADSGP VPGGERPAGE GQGEPTSRPK AVTFSPDLGP VPHEGLGEYN
710 720 730 740 750
RAVSKLSAAL SSLQRDMQRL TDQQQRLLAP PEAPGSAPPP AAWVIPGPTT
760 770 780 790 800
GPKAASPSPA RRVPATRRSP GPGPSQSPRS PKHTRPAELR LAPLTRVLTP
810 820 830 840 850
PHDVDSLPHL RKFSPSQVPV QTRSSILLAE ETPPEEPAAR PGLIEIPLGS
860 870 880 890 900
LADPAAEDEG DGSPAGAEDS LEEEASSEGE PRVGLGFFYK DEDKPEDEMA
910 920 930 940 950
QKRASLLERQ QRRAEEARRR KQWQEVEKEQ RREEAARLAQ EEAPGPAPLV
960 970 980 990 1000
SAVPMATPAP AARAPAEEEV GPRKGDFTRQ EYERRAQLKL MDDLDKVLRP
1010 1020 1030 1040 1050
RAAGSGGPGR GGRRATRPRS GCCDDSALAR SPARGLLGSR LSKIYSQSTL
1060 1070 1080 1090 1100
SLSTVANEAH NNLGVKRPTS RAPSPSGLMS PSRLPGSRER DWENGSNASS
1110 1120 1130 1140 1150
PASVPEYTGP RLYKEPSAKS NKFIIHNALS HCCLAGKVNE PQKNRILEEI
1160 1170 1180 1190 1200
EKSKANHFLI LFRDSSCQFR ALYTLSGETE ELSRLAGYGP RTVTPAMVEG
1210 1220 1230 1240
IYKYNSDRKR FTQIPAKTMS MSVDAFTIQG HLWQGKKPTT PKKGGGTPK
Length:1,249
Mass (Da):134,750
Last modified:March 15, 2005 - v2
Checksum:i5A597E13531443CE
GO
Isoform 2 (identifier: Q9P1Y5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     207-207: S → SCPTRWYWKLVPHAIAFCLKESGSKPPM

Show »
Length:1,276
Mass (Da):137,878
Checksum:i4248F67ED7F3CEEE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti824 – 8241S → P in BC035808 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti335 – 3351P → S.
Corresponds to variant rs3745358 [ dbSNP | Ensembl ].
VAR_053991

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei207 – 2071S → SCPTRWYWKLVPHAIAFCLK ESGSKPPM in isoform 2. 1 PublicationVSP_041473

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC008763 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69025.1.
BC020431 mRNA. No translation available.
BC035808 mRNA. No translation available.
AB040976 mRNA. Translation: BAA96067.1.
AL833927 mRNA. Translation: CAD38783.1.
CCDSiCCDS42489.1. [Q9P1Y5-1]
CCDS45947.1. [Q9P1Y5-2]
RefSeqiNP_001073898.1. NM_001080429.2. [Q9P1Y5-2]
NP_065953.1. NM_020902.1. [Q9P1Y5-1]
UniGeneiHs.17686.

Genome annotation databases

EnsembliENST00000160298; ENSP00000160298; ENSG00000076826. [Q9P1Y5-1]
ENST00000446248; ENSP00000416797; ENSG00000076826. [Q9P1Y5-2]
GeneIDi57662.
KEGGihsa:57662.
UCSCiuc002mgu.5. human. [Q9P1Y5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC008763 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69025.1.
BC020431 mRNA. No translation available.
BC035808 mRNA. No translation available.
AB040976 mRNA. Translation: BAA96067.1.
AL833927 mRNA. Translation: CAD38783.1.
CCDSiCCDS42489.1. [Q9P1Y5-1]
CCDS45947.1. [Q9P1Y5-2]
RefSeqiNP_001073898.1. NM_001080429.2. [Q9P1Y5-2]
NP_065953.1. NM_020902.1. [Q9P1Y5-1]
UniGeneiHs.17686.

3D structure databases

ProteinModelPortaliQ9P1Y5.
SMRiQ9P1Y5. Positions 1108-1244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121695. 22 interactions.
DIPiDIP-52405N.
IntActiQ9P1Y5. 21 interactions.
MINTiMINT-1402687.
STRINGi9606.ENSP00000416797.

PTM databases

iPTMnetiQ9P1Y5.
PhosphoSiteiQ9P1Y5.

Polymorphism and mutation databases

BioMutaiCAMSAP3.
DMDMi61213747.

Proteomic databases

EPDiQ9P1Y5.
MaxQBiQ9P1Y5.
PaxDbiQ9P1Y5.
PRIDEiQ9P1Y5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000160298; ENSP00000160298; ENSG00000076826. [Q9P1Y5-1]
ENST00000446248; ENSP00000416797; ENSG00000076826. [Q9P1Y5-2]
GeneIDi57662.
KEGGihsa:57662.
UCSCiuc002mgu.5. human. [Q9P1Y5-1]

Organism-specific databases

CTDi57662.
GeneCardsiCAMSAP3.
H-InvDBHIX0202697.
HGNCiHGNC:29307. CAMSAP3.
HPAiHPA043830.
MIMi612685. gene.
neXtProtiNX_Q9P1Y5.
PharmGKBiPA134885087.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3654. Eukaryota.
ENOG4111D0B. LUCA.
GeneTreeiENSGT00390000010026.
HOGENOMiHOG000059671.
InParanoidiQ9P1Y5.
KOiK17493.
OMAiDFTRQEY.
OrthoDBiEOG7P8P6Z.
PhylomeDBiQ9P1Y5.
TreeFamiTF315529.

Miscellaneous databases

ChiTaRSiCAMSAP3. human.
GenomeRNAii57662.
NextBioi64428.
PROiQ9P1Y5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P1Y5.
CleanExiHS_KIAA1543.
GenevisibleiQ9P1Y5. HS.

Family and domain databases

InterProiIPR032940. CAMSAP.
IPR031372. CAMSAP_CC1.
IPR022613. CAMSAP_CH.
IPR001715. CH-domain.
IPR014797. CKK_domain.
IPR011033. PRC_barrel-like.
[Graphical view]
PANTHERiPTHR21595. PTHR21595. 2 hits.
PfamiPF17095. CAMSAP_CC1. 1 hit.
PF11971. CAMSAP_CH. 1 hit.
PF08683. CAMSAP_CKK. 1 hit.
[Graphical view]
SMARTiSM01051. CAMSAP_CKK. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF50346. SSF50346. 1 hit.
PROSITEiPS51508. CKK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 1 AND 2).
    Tissue: Brain and Retinoblastoma.
  4. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 333-1249 (ISOFORMS 1/2).
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 407-1249 (ISOFORM 1/2).
    Tissue: Testis.
  6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts."
    Meng W., Mushika Y., Ichii T., Takeichi M.
    Cell 135:948-959(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MICROTUBULE-BINDING, INTERACTION WITH PLEKHA7.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-184; SER-193; SER-341; SER-347; SER-368; SER-554; SER-560; SER-685 AND THR-799, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334 AND SER-814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Nezha/CAMSAP3 and CAMSAP2 cooperate in epithelial-specific organization of noncentrosomal microtubules."
    Tanaka N., Meng W., Nagae S., Takeichi M.
    Proc. Natl. Acad. Sci. U.S.A. 109:20029-20034(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193; SER-334; SER-547 AND THR-799, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCAMP3_HUMAN
AccessioniPrimary (citable) accession number: Q9P1Y5
Secondary accession number(s): Q8NDF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 11, 2016
This is version 118 of the entry and version 2 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

Miscellaneous

'Nezha' is a deity in Chinese mythology.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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.