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O75330 (HMMR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hyaluronan mediated motility receptor
Alternative name(s):
Intracellular hyaluronic acid-binding protein
Receptor for hyaluronan-mediated motility
CD_antigen=CD168
Gene names
Name:HMMR
Synonyms:IHABP, RHAMM
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length724 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in cell motility. When hyaluronan binds to HMMR, the phosphorylation of a number of proteins, including PTK2/FAK1 occurs. May also be involved in cellular transformation and metastasis formation, and in regulating extracellular-regulated kinase (ERK) activity.

Subunit structure

Subunit of the HARC complex.

Subcellular location

Cell surface. Cytoplasm By similarity.

Tissue specificity

Expressed in breast cancer cell lines and in normal breast tissue.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandHyaluronic acid
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentcell surface

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhyaluronic acid binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75330-1)

Also known as: A;

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.
Isoform 2 (identifier: O75330-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     76-90: Missing.
Isoform 3 (identifier: O75330-3)

The sequence of this isoform differs from the canonical sequence as follows:
     75-75: K → KK
Isoform 4 (identifier: O75330-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: MSFPKAPLKR...DKDLKILEKE → MTLL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 724724Hyaluronan mediated motility receptor
PRO_0000084007

Regions

Region635 – 64511Hyaluronic acid-binding Potential
Region657 – 66610Hyaluronic acid-binding Potential

Amino acid modifications

Modified residue201Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10
Modified residue651Phosphoserine Ref.8
Modified residue7031Phosphothreonine Ref.7
Glycosylation1331N-linked (GlcNAc...) Potential
Glycosylation4771N-linked (GlcNAc...) Potential
Glycosylation5671N-linked (GlcNAc...) Potential
Glycosylation5881N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 9090MSFPK…ILEKE → MTLL in isoform 4.
VSP_041266
Alternative sequence751K → KK in isoform 3.
VSP_038378
Alternative sequence76 – 9015Missing in isoform 2.
VSP_004286
Natural variant921R → C. Ref.6
Corresponds to variant rs299284 [ dbSNP | Ensembl ].
VAR_024155
Natural variant3051N → K.
Corresponds to variant rs2303077 [ dbSNP | Ensembl ].
VAR_031661
Natural variant3201N → K.
Corresponds to variant rs2303077 [ dbSNP | Ensembl ].
VAR_056917
Natural variant3321R → H.
Corresponds to variant rs2303078 [ dbSNP | Ensembl ].
VAR_024156
Natural variant3681V → A. Ref.3 Ref.6
Corresponds to variant rs299290 [ dbSNP | Ensembl ].
VAR_020044
Natural variant4841A → V. Ref.3 Ref.6
Corresponds to variant rs299295 [ dbSNP | Ensembl ].
VAR_024157
Natural variant5571D → H.
Corresponds to variant rs2230362 [ dbSNP | Ensembl ].
VAR_056918
Natural variant5951L → I.
Corresponds to variant rs2230363 [ dbSNP | Ensembl ].
VAR_056919

Experimental info

Sequence conflict1031R → S in AAC32548. Ref.2
Sequence conflict2771E → D in AAC52049. Ref.1
Sequence conflict2981K → T in AAC52049. Ref.1
Sequence conflict3221K → E in AAC52049. Ref.1
Sequence conflict330 – 3323QER → REH in AAC52049. Ref.1
Sequence conflict5471Q → R in BAF83266. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: F2C3C0DBA863955F

FASTA72484,100
        10         20         30         40         50         60 
MSFPKAPLKR FNDPSGCAPS PGAYDVKTLE VLKGPVSFQK SQRFKQQKES KQNLNVDKDT 

        70         80         90        100        110        120 
TLPASARKVK SSESKESQKN DKDLKILEKE IRVLLQERGA QDRRIQDLET ELEKMEARLN 

       130        140        150        160        170        180 
AALREKTSLS ANNATLEKQL IELTRTNELL KSKFSENGNQ KNLRILSLEL MKLRNKRETK 

       190        200        210        220        230        240 
MRGMMAKQEG MEMKLQVTQR SLEESQGKIA QLEGKLVSIE KEKIDEKSET EKLLEYIEEI 

       250        260        270        280        290        300 
SCASDQVEKY KLDIAQLEEN LKEKNDEILS LKQSLEENIV ILSKQVEDLN VKCQLLEKEK 

       310        320        330        340        350        360 
EDHVNRNREH NENLNAEMQN LKQKFILEQQ EREKLQQKEL QIDSLLQQEK ELSSSLHQKL 

       370        380        390        400        410        420 
CSFQEEMVKE KNLFEEELKQ TLDELDKLQQ KEEQAERLVK QLEEEAKSRA EELKLLEEKL 

       430        440        450        460        470        480 
KGKEAELEKS SAAHTQATLL LQEKYDSMVQ SLEDVTAQFE SYKALTASEI EDLKLENSSL 

       490        500        510        520        530        540 
QEKAAKAGKN AEDVQHQILA TESSNQEYVR MLLDLQTKSA LKETEIKEIT VSFLQKITDL 

       550        560        570        580        590        600 
QNQLKQQEED FRKQLEDEEG RKAEKENTTA ELTEEINKWR LLYEELYNKT KPFQLQLDAF 

       610        620        630        640        650        660 
EVEKQALLNE HGAAQEQLNK IRDSYAKLLG HQNLKQKIKH VVKLKDENSQ LKSEVSKLRC 

       670        680        690        700        710        720 
QLAKKKQSET KLQEELNKVL GIKHFDPSKA FHHESKENFA LKTPLKEGNT NCYRAPMECQ 


ESWK 

« Hide

Isoform 2 (B) [UniParc].

Checksum: 29E7F070B99FD30C
Show »

FASTA70982,301
Isoform 3 [UniParc].

Checksum: 2515512EEDFB1DA1
Show »

FASTA72584,229
Isoform 4 [UniParc].

Checksum: BFD153D3EC20FE5D
Show »

FASTA63874,495

References

« Hide 'large scale' references
[1]"The characterization of a human RHAMM cDNA: conservation of the hyaluronan-binding domains."
Wang C., Entwistle J., Hou G., Li Q., Turley E.A.
Gene 174:299-306(1996) [PubMed: 8890751] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Mammary gland.
[2]"The human hyaluronan receptor RHAMM is expressed as an intracellular protein in breast cancer cells."
Assmann V., Marshall J.F., Fieber C., Hofmann M., Hart I.R.
J. Cell Sci. 111:1685-1694(1998) [PubMed: 9601098] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2), CHARACTERIZATION.
Tissue: Mammary carcinoma.
[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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), VARIANTS ALA-368 AND VAL-484.
Tissue: Thymus.
[4]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed: 15372022] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANTS CYS-92; ALA-368 AND VAL-484.
[7]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-703, MASS SPECTROMETRY.
Tissue: Cervix adenocarcinoma.
[8]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-65, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[10]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U29343 mRNA. Translation: AAC52049.1.
AF032862 mRNA. Translation: AAC32548.1.
AK290577 mRNA. Translation: BAF83266.1.
AK303616 mRNA. Translation: BAG64626.1.
AC112205 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61522.1.
CH471062 Genomic DNA. Translation: EAW61523.1.
CH471062 Genomic DNA. Translation: EAW61524.1.
CH471062 Genomic DNA. Translation: EAW61525.1.
BC108904 mRNA. Translation: AAI08905.1.
IPIIPI00337325.
IPI00337772.
IPI00844515.
IPI00917607.
PIRJC5016.
RefSeqNP_001136028.1. NM_001142556.1.
NP_001136029.1. NM_001142557.1.
NP_036616.2. NM_012484.2.
NP_036617.2. NM_012485.2.
UniGeneHs.728200.

3D structure databases

ProteinModelPortalO75330.
ModBaseSearch...

Protein-protein interaction databases

IntActO75330. 3 interactions.
STRINGO75330.

PTM databases

PhosphoSiteO75330.

2D gel databases

REPRODUCTION-2DPAGEO75330.

Proteomic databases

PRIDEO75330.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358715; ENSP00000351554; ENSG00000072571.
GeneID3161.
KEGGhsa:3161.
NMPDRfig|9606.3.peg.26125.
UCSCuc003lzf.1. human.

Organism-specific databases

CTD3161.
GeneCardsGC05P162887.
HGNCHGNC:5012. HMMR.
HPACAB002433.
MIM600936. gene.
neXtProtNX_O75330.
PharmGKBPA29340.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG15960.
GeneTreeENSGT00390000007135.
HOVERGENHBG044411.
OMAKLCSFQE.
PhylomeDBO75330.

Gene expression databases

ArrayExpressO75330.
BgeeO75330.
CleanExHS_HMMR.
GenevestigatorO75330.
GermOnlineENSG00000072571. Homo sapiens.

Family and domain databases

KOK06267.
ProtoNetSearch...

Other

NextBio12532.
SOURCESearch...

Entry information

Entry nameHMMR_HUMAN
AccessionPrimary (citable) accession number: O75330
Secondary accession number(s): A8K3G2 expand/collapse secondary AC list , B4E114, D3DQK9, D3DQL0, E9PCS0, Q32N02, Q92767
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 17, 2007
Last modified: January 25, 2012
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

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Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot